© The Rockefeller University Press,
0021-9525/1997//1 $5.00
The Journal of Cell Biology, Volume 138, Number 1,
, 1997 1-4
Membrane Dynamics at the Endoplasmic Reticulum–Golgi Interface
Sergei I. Bannykh and
William E. Balch
The Scripps Research Institute, Department of Cell Biology, La Jolla, California 92037
Movement of cargo through the secretory pathway of eukaryotic cells occurs as a discontinuous process involving the activity of 50–80-nm vesicles (28). Vesicles forming on the endoplasmic reticulum (ER) by the COPII coat machinery (35) were first detected as coated elevations on transitional elements directly facing the Golgi apparatus. Subsequently, intermediates harboring ER-derived cargo were found in regions distant from the Golgi stack (16, 33). These structures contained a different coat complex, COPI or coatomer, recognized to be involved in vesicle-mediated recycling (20). It is now apparent that ER export and recycling are tightly coupled. We review recent evidence regarding the organization and role of ER to Golgi intermediates in these events.
 |
Pleomorphic Elements Function in ER to Golgi Transport
|
|---|
Stereological analysis of serial thin sections revealed the general morphological organization and distribution of ER export/recycling sites (4). Export from the ER was found to be associated with one or more COPII-coated bud-bearing ER cisternae that face towards a central cavity (Fig. 1). The central cavity is filled with a collection of closely opposed vesicles and convoluted tubules containing COPI coats (4). We have termed these central compact clusters of pleomorphic elements as vesicular-tubular clusters (VTCs)1 for their morphological appearance (3), but they have also been referred to as ERGIC (ER–Golgi intermediate compartment) (16). The juxtaposition of ER-derived buds and a central VTC composes a morphological unit of organization termed an export complex (4) (Fig. 1). ER-derived buds cannot be detected outside export complexes, suggesting a local specialization of the cytoplasm that is likely to be enriched in transport components. While VTC-containing export complexes are scattered throughout the cytoplasm, VTCs found in the perinuclear region of the cell are believed to form a more extensive array of tubulo-cisternal elements referred to as the cis-Golgi network (CGN) (24).
View larger version (75K):
[in this window]
[in a new window]
[Download PPT slide]
|
Figure 1 Morphological organization of ER export. A diagram summarizing the three tiers of organization of ER export complexes. An individual ER cisterna contains a collection of closely opposed buds that define a local transitional region (light zone with stippled COPII coated buds [Tier I]). A collection of Tier I budding sites (cylindrical region outlined by dashed lines forming Tier II) encompass a central cavity containing a collection of tubular elements (VTCs) that have COPI coats (dense coated buds). Tier III defines the entire export complex consisting of a local concentration of ER budding sites and the central VTC. See cover for a morphological rendering of a typical export complex. Figure taken from reference 4.
| |
|
Biochemical Composition of VTCs
|
|---|
COPII coats direct the sorting and concentration of cargo during export from the ER (1, 3, 5). The dissociation of a COPII vesicular carrier from ER budding elements demarcates the first boundary between the ER and downstream organelles of the secretory pathway. The formation of this boundary is consistent with morphological observations that VTCs lack continuity with the ER (4, 32, 40). Although there have been reports of apparent connections between VTCs and the ER, they appear only when selected viral glycoproteins have been overexpressed (18) or in cells infected with viruses that mature in the early secretory pathway (21). The structures generated under these conditions are likely to be tubular elaborations of ER or ER exit sites in response to the presence of viral proteins. In general, a large body of biochemical and morphological evidence is consistent with the conclusion that VTCs are the first distinct compartment downstream from the ER.
Although VTCs define a unique compartment, their composition remains to be firmly established. During export from the ER, ribophorin and components of the protein translocation machinery such as Sec61, as well as resident ER proteins including the folding chaperones calnexin and BiP, are efficiently excluded from COPII vesicles (5, 31). Therefore, they are unlikely to be functional components of VTCs. An important contribution to the identification of ER to Golgi intermediates came with the discovery of the closely related (90% identity) VTC marker proteins p53 and p58 (16). p53/p58 are type 1 transmembrane proteins that continuously recycle between the ER and VTCs but are concentrated in VTCs at steady state. Other proteins enriched in VTCs are the small GTPases Rab1 (29) and Rab2 (7), p24 family members that are potentially involved in cargo selection during export from the ER (10, 36), and other membrane components involved in the targeting/fusion of COP II vesicles (11). To date, there are no markers that can be defined as resident proteins, emphasizing that VTCs are highly dynamic structures.
|
VTCs Undergo Maturation in a COPI-dependent Fashion
|
|---|
After release from the ER, COPII vesicles rapidly lose their coats (2) and become associated with VTCs containing COPI coats. COPI is involved in the formation of vesicles that promote the retrograde transport of proteins containing terminal KKXX motifs (13, 22) and Phe residues (12, 37). The mechanism by which VTCs initiate the recruitment of COPI coats has been investigated. Using an assay that reconstitutes budding from ER microsomes in vitro (31), it was found that uncoated COPII vesicles can bind COPI components before their fusion to VTCs. This coupled exchange between COPII and COPI coats was proposed to serve as a tagging mechanism to mark components for rapid retrieval to the ER from VTCs (31). More recent studies have demonstrated that p53/p58, possibly in conjunction with p24 family members, is a component of the recruitment machinery (39). Therefore, segregation of retrograde- and anterograde-transported proteins is an important activity of the tubular elements comprising VTCs.
Although COPI vesicles are principally associated with VTCs and early Golgi compartments, they have recently also been proposed to participate in ER export. They can form on yeast ER membranes in vitro (6), and COPI components are closely associated with unusual ER cisternae in mammalian cells in vivo (27). However, the COPI vesicles formed in vitro from yeast ER membranes lack cargo molecules typically found in COPII vesicles, and the COPI-enriched region adjacent to the ER elements in mammalian cells does not contain buds. Therefore, it is presently more likely that COPII performs an exclusive role in sorting and concentration of cargo during ER export, while COPI functions in retrograde retrieval from VTCs and Golgi compartments.
|
VTCs Can Be Mobilized to the Golgi Region Along Microtubules
|
|---|
Morphological evidence has now provided clear support for a role for microtubules in ER to Golgi transport (34). When cells are incubated at reduced temperature (15°C), they accumulate VTCs at peripheral sites. After transfer to 37°C, these VTCs redistribute to the central Golgi region in a microtubule-dependent fashion. Live cell imaging using a green-fluorescence protein–cargo chimera (Presley, J.F., N.B. Cole, and J. Lippincott-Schwartz. 1996. Mol. Biol. Cell. 7:74a) revealed that VTCs migrated towards the Golgi in a saltatory fashion at 
1 µm/s. At the cis face of the Golgi, they appeared to fuse to form the CGN. Combined with the fact that ER buds are localized to the region surrounding VTCs at steady state (4), it is apparent that the entire export complex serves as a mobile collecting/recycling device promoting acquisition and delivery of cargo to the Golgi apparatus.
|
Formation and Consumption of VTCs
|
|---|
At least two opposing models can be envisioned for the formation and consumption of VTCs. One model (Fig. 2 A) suggests that the tubular elements of VTC/CGN are unique compartments that contain a core of nonrecycling, resident proteins distinct from those found in either the ER or the Golgi. In this model, ER-derived COPII vesicles undergo heterotypic fusion with these tubular elements. As described above, retrograde recycling would be mediated by COPI vesicles. Anterograde transport from these tubular elements to subsequent Golgi compartments would most likely require a second round of budding to retain compartment identity. However, COPII function is complete after export from the ER (2, 5, 31), and genetic experiments in yeast (13, 22) argue against the involvement of known COPI components in anterograde transport. Therefore, vesicle budding will require either currently unrecognized components of the COPI machinery that distinguish between anterograde or retrograde transport, or a new coat machinery.
View larger version (33K):
[in this window]
[in a new window]
[Download PPT slide]
|
Figure 2 Potential models for transport of cargo through the Golgi stack. (A) The first model illustrates that movement of cargo between the ER, VTC/CGN, and individual cisternae of the Golgi stack requires distinct vesicular carriers at each step. Recycling between stacks is mediated by the COPI machinery. (B) The second model envisions that COPII vesicles fuse to form VTC/CGN, which subsequently assemble to form the first stack. Cargo does not exit the CGN; rather, COPI recycling vesicles harboring Golgi processing enzymes direct its maturation to transform it into the trans-most cisternae. New VTCs continuously replenish the cis face.
| |
In the second model (Fig. 2 B), tubular elements of VTCs could form de novo from the homotypic fusion of ER-derived COPII vesicles. Homotypic fusion between like compartments is a common feature of both the exocytic and endocytic pathways. In this model, the tubular elements of VTCs would then move en bloc to the central Golgi region, where they could undergo further homotypic fusion with elements derived from other peripheral sites to form the CGN (3). During transit to the central Golgi region, COPI vesicles would direct recycling components back to the ER, thereby maintaining a steady-state balance between input and output of membrane. Although this model is attractive, key evidence that COPII vesicles or VTCs undergo homotypic fusion is missing.
|
Movement of Cargo through the Golgi Stack
|
|---|
The method by which VTCs are formed and consumed may provide critical insight into the ensuing mechanism(s) involved in the movement of anterograde-transported cargo through compartments of the Golgi stack. Transport will necessarily involve vesicular carriers since morphological and biochemical evidence favors the view that individual compartments are not in continuity with one another (17, 24).
One model for Golgi function is an extension of the model shown in Fig. 2 A. Here, compartments are discontinuous and each is compositionally distinct. Whereas recycling of transport components could be readily accommodated by the COPI machinery, anterograde transport would require the function of separate vesicular carriers between each compartment. If their formation also involves COPI, as suggested by Rothman and colleagues (30), a collection of additional novel proteins will be necessary not only to allow COPI coats to discriminate between anterograde and recycling cargo as indicated above, but also to direct vectorial movement between sequential Golgi compartments by distinct carriers.
A second possibility is a direct outgrowth of the homotypic assembly model of VTCs (Fig. 2 B). In this view, VTCs, once formed, do not release anterograde-transported cargo into carrier vesicles. Rather, the Golgi stack is composed of a series of progressively maturing, discontinuous compartments initially formed by the fusion of COPII vesicular carriers and peripheral VTCs. A process of "directed maturation" of each compartment would occur through the activity of the COPI recycling machinery. In this case, it would only be necessary to propose that the COPI machinery mediates retrieval of Golgi processing enzymes in response to its relative affinity for these proteins reflecting their observed steady-state cis to trans distribution across the stack. Processing enzymes in the cis-most compartments would have a higher probability of being recruited to a COPI vesicle than those in the trans-most compartments. Selective recruitment of these enzymes would necessarily be coupled to specificity determinants directing vesicle targeting and fusion. In this model, a compartment derived from the fusion of VTCs (lacking processing enzymes) would first become selectively enriched with cis processing enzymes (Fig. 2 B). As the composition of the maturing compartment changes, so does the competition for the COPI machinery by processing enzymes within the compartment for recycling, thereby ensuring "self-directed" maturation to the medial- and trans-Golgi states (Fig. 2 B). The apparent polarized organization of the stack would be a direct consequence of VTCs continuously contributing to the formation of new, cis-most elements (Fig. 2 B). The TGN, where both COPI-mediated recycling and clathrin-mediated anterograde transport would be occurring, may be maintained through additional input of membrane from the endocytic pathway. The concept of directed maturation was proposed as early as 1957 by Grasse (14) and later refined by Morre and co-workers (25) as cisternal progression. New knowledge of the importance of COPI in retrograde traffic provides a potential mechanistic basis for this model.
|
Evidence for the Directed Maturation Model
|
|---|
Considerable evidence supports directed maturation. First, it is consistent with a major role for COPI in retrograde transport. Second, it accounts for the striking dependence of both retrograde and anterograde transport of cargo on the COPI machinery because processing of anterograde-directed cargo will not occur when COPI-mediated retrieval is blocked (2, 13, 31). Third, after mitotic disassembly of the Golgi, COPI vesicles appear to be markedly enriched in Golgi processing enzymes relative to anterograde cargo (38). Thus, COPI vesicles may sort and concentrate these enzymes, consistent with their high diffusional mobility in the membrane (9). Indeed, the lack of precise compartmental localization of various processing enzymes is compatible with the predicted variable affinity of COPI for different Golgi enzymes. Fourth, retrograde transport is required to maintain the localization of Golgi processing enzymes (15, 19) and for Golgi enzymes to maintain the structure of the stack (26). Fifth, all molecules migrate through the Golgi stack at a uniform rate, as opposed to variable rates of exit from the ER because of differences in sorting and concentration via COPII vesicles (3). Moreover, assembled structures found in early Golgi compartments that are too large to enter carrier vesicles, such as ApoE containing lipoprotein particles, procollagen, casein submicelles, and scale plates in algae and virus particles, are able to undergo normal processing by Golgi enzymes during their delivery to the surface. Sixth, numerous observations have established that either under- or overexpression of a wide variety of Golgi "marker" proteins leads to dramatic changes in normal Golgi structure, reflecting a dynamic basis for organization of the stack. Finally, directed maturation could account for the observation that the regeneration of Golgi stacks occurs at export complexes after treatment with brefeldin A (a reagent that collapses Golgi compartments to the ER) (8) and during recovery from mitosis (23).
|
The Future
|
|---|
We have focused on recent results that now clearly establish the importance of VTCs as key intermediates in the secretory pathway. New approaches that provide insight into the mechanism(s) of protein retrieval and anterograde flow should help us understand the molecular basis for the function of the VTCs in transport of cargo from the ER to and through the Golgi apparatus.
Submitted: 12 March 1997
Revised: 24 April 1997
1. Abbreviations used in this paper: CGN, cis-Golgi network; VTC, vesicular-tubular cluster.
Address all correspondence to William E. Balch, The Scripps Research Institute, Departments of Cell and Molecular Biology, 10550 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: (619) 784-2310. Fax: (619) 784-9126.
|
References
|
|---|
- Aridor M & Balch WE. Principles of selective transport: coat complexes hold the key, Trends Cell Biol, 1996, 6, 315–320.[Medline]
- Aridor M, Bannykh SI, Rowe T & Balch WE. Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport, J Cell Biol, 1995, 131, 875–893.[Abstract/Free Full Text]
- Balch WE, McCaffery JM, Plutner H & Farquhar MG. Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum, Cell, 1994, 76, 841–852.[Medline]
- Bannykh SI, Rowe T & Balch WE. Organization of endoplasmic reticulum export complexes, J Cell Biol, 1996, 135, 19–35.[Abstract/Free Full Text]
- Barlowe C, Orci L, Yeung T, Hosobuchi M, Hamamoto S, Salama N, Rexach MF, Ravazzola M, Amherdt M & Schekman R. COPII: a membrane coat formed by sec proteins that drive vesicle budding from the endoplasmic reticulum, Cell, 1994, 77, 895–907.[Medline]
- Bednarek SY, Ravazzola M, Hosobuchi M, Amherdt M, Perrelet A, Schekman R & Orci L. COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast, Cell, 1995, 83, 1183–1196.[Medline]
- Chavrier P, Parton RG, Hauri H-P, Simons K & Zerial M. Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments, Cell, 1990, 62, 317–329.[Medline]
- Cole NB, Sciaky N, Marotta A, Song J & Lippincott-Schwartz J. Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites, Mol Biol Cell, 1996, 7, 631–650.[Abstract]
- Cole NB, Smith CL, Sciaky N, Terasaki M, Edidin M & Lippincott-Schwartz J. Diffusional mobility of Golgi proteins in membranes of living cells, Science (Wash DC), 1996, 273, 797–801.[Abstract]
- Elrod-Erickson MJ & Kaiser CA. Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations, Mol Biol Cell, 1996, 7, 1043–1058.[Abstract]
- Ferro-Novick S & Jahn R. Vesicle fusion from yeast to man, Nature (Lond), 1994, 370, 191–193.[Medline]
- Fiedler K, Veit M, Stamnes MA & Rothman JE. Bimodal interaction of coatomer with a family of putative cargo and vesicle coat protein receptors, the p24 proteins, Science (Wash DC), 1996, 273, 1396–1398.[Abstract]
- Gaynor EC & Emr SD. COPI-independent anterograde transport: cargo-selective ER-to-Golgi protein transport in yeast COPI mutants, J Cell Biol, 1997, 136, 789–802.[Abstract/Free Full Text]
- Grasse PP. , Acad Sci (Paris), 1957, 245, 1278–1281.
- Harris SL & Waters G. Localization of a yeast early Golgi mannosyltransferase, Och1p, involves retrograde transport, J Cell Biol, 1996, 132, 985–998.[Abstract/Free Full Text]
- Hauri H-P & Schweizer A. The endoplasmic reticulum-Golgi intermediate compartment, Curr Opin Cell Biol, 1992, 4, 600–608.[Medline]
- Hayes BK, Freeze HH & Varki A. Biosynthesis of oligosaccharides in intact Golgi preparations from rat liver: analysis of N-linked glycans labeled by UDP[6-3H]N-acetylglucosamine, J Biol Chem, 1993, 268, 16139–16154.[Abstract/Free Full Text]
- Hobman TC, Woodward L & Farquhar MG. The rubella virus E1 glycoprotein is arrested in a novel post-ER, pre-Golgi compartment, J Cell Biol, 1992, 118, 795–811.[Abstract/Free Full Text]
- Hoe MH, Slusarewicz P, Misteli T, Watson R & Warren G. Evidence for recycling of the resident medial/trans Golgi enzyme, N-acetylglucosaminyltransferase I, in ldlD cells, J Biol Chem, 1995, 270, 25057–25063.[Abstract/Free Full Text]
- Kreis TE, Lowe M & Pepperkok R. COPs regulating membrane traffic, Annu Rev Cell Dev Biol, 1995, 11, 677–706.[Medline]
- Krijnse-Locker J, Ericsson M, Rottier PJM & Griffiths G. Characterization of the budding compartment of mouse hepatitis virus: evidence that transport from the RER to the Golgi complex requires only one vesicular transport step, J Cell Biol, 1994, 124, 55–70.[Abstract/Free Full Text]
- Letourneur F, Gaynor EC, Hennecke S, Demolliere C, Duden R, Emr SD, Riezman H & Cosson P. Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum, Cell, 1994, 79, 1199–1207.[Medline]
- Lucocq JM, Berger EG & Warren G. Mitotic Golgi fragments in HeLa cells and their role in the reassembly pathway, J Cell Biol, 1989, 109, 463–474.[Abstract/Free Full Text]
- Mellman I & Simon K. The Golgi complex: in vitro veritas? , Cell, 1992, 68, 829–840.[Medline]
- Morre, D.J. 1977. International Cell Biology, 1976–1977. B.R. Brinkley and K.R. Porter, editors. Rockefeller University Press, New York. 293–303.
- Nilsson T, Rabouille C, Hui N, Watson R & Warren G. The role of the membrane-spanning domain and stalk region of N-acetylglucosaminyltransferase I in retention, in recognition and structural maintenance of the Golgi apparatus in HeLa cells, J Cell Sci, 1996, 109, 1975–1989.[Abstract]
- Orci L, Perrelet A, Mariella R, Amherdt M, Rothman JE & Schekman R. Coatomer-rich endoplasmic reticulum, Proc Natl Acad Sci USA, 1994, 91, 11924–11928.[Abstract/Free Full Text]
- Palade GE. Intracellular aspects of the process of protein transport, Science (Wash DC), 1975, 189, 347–354.[Free Full Text]
- Pind S, Nuoffer C, McCaffery JM, Plutner H, Davidson HW, Farquhar MG & Balch WE. Rab1 and Ca2+are required for the fusion of carrier vesicles mediating endoplasmic reticulum to Golgi transport, J Cell Biol, 1994, 125, 239–252.[Abstract/Free Full Text]
- Rothman JE & Wieland F. Protein sorting by transport vesicles, Science (Wash DC), 1996, 272, 227–234.[Abstract]
- Rowe T, Aridor M, McCaffery JM, Plutner H & Balch WE. COPII vesicles derived from mammalian endoplasmic reticulum (ER) microsomes recruit COPI, J Cell Biol, 1996, 135, 895–911.[Abstract/Free Full Text]
- Saraste J & Kuismanen E. Pre- and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface, Cell, 1984, 38, 535–549.[Medline]
- Saraste J & Kuismanen E. Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulum and the Golgi complex, Semin Cell Biol, 1992, 3, 343–355.[Medline]
- Saraste J & Thyberg J. Function of microtubules in protein secretion and organization of the Golgi complex, Cytoskeleton, 1996, 2, 239–273.
- Schekman R & Orci L. Coat proteins and vesicle budding, Science (Wash DC), 1996, 271, 1526–1533.[Abstract]
- Schimmoller F, Singer-Kruger B, Schroder S, Kruger U, Barlowe C & Riezman H. The absence of Emp24p, a component of ER- derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi, EMBO (Eur Mol Biol Organ) J, 1995, 14, 1329–1339.[Medline]
- Sohn K, Orci L, Ravazzola M, Bremser M, Lottspeich F, Fiedler K, Helms JB & Wieland FT. A major transmembrane protein of Golgi-derived COPI-coated vesicles involved in coatomer binding, J Cell Biol, 1996, 135, 12239–12248.
- Sonnichsen B, Watson R, Clausen H, Misteli T & Warren G. Sorting COPI-coated vesicles under interphase and mitotic conditions, J Cell Biol, 1996, 124, 1411–1425.[Medline]
- Tisdale EJ, Plutner H, Matteson J & Balch WE. P53/58 binds COPI and is required for selective transport through the early secretory pathway, J Cell Biol, 1997, 137, 581–594.[Abstract/Free Full Text]
- Tooze SA, Tooze J & Warren G. Site of addition of N-acetyl- galactosamine to the E1 glycoprotein of mouse hepatitis virus-A59, J Cell Biol, 1988, 106, 1475–1487.[Abstract/Free Full Text]
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Facebook 
Reddit 
Technorati 
Twitter What's this?
This article has been cited by other articles:
-
Hughes, H., Budnik, A., Schmidt, K., Palmer, K. J., Mantell, J., Noakes, C., Johnson, A., Carter, D. A., Verkade, P., Watson, P., Stephens, D. J.
(2009). Organisation of human ER-exit sites: requirements for the localisation of Sec16 to transitional ER. J. Cell Sci.
122: 2924-2934
[Abstract]
[Full Text]
-
Lehmann, J., Reichel, A., Buguin, A., Libchaber, A.
(2007). Efficiency of a self-aminoacylating ribozyme: Effect of the length and base-composition of its 3' extension. RNA
13: 1191-1197
[Abstract]
[Full Text]
-
Zuber, C., Cormier, J. H., Guhl, B., Santimaria, R., Hebert, D. N., Roth, J.
(2007). EDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sites. Proc. Natl. Acad. Sci. USA
104: 4407-4412
[Abstract]
[Full Text]
-
Bhattacharyya, D., Glick, B. S.
(2007). Two Mammalian Sec16 Homologues Have Nonredundant Functions in Endoplasmic Reticulum (ER) Export and Transitional ER Organization. Mol. Biol. Cell
18: 839-849
[Abstract]
[Full Text]
-
Zhao, X., Claude, A., Chun, J., Shields, D. J., Presley, J. F., Melancon, P.
(2006). GBF1, a cis-Golgi and VTCs-localized ARF-GEF, is implicated in ER-to-Golgi protein traffic. J. Cell Sci.
119: 3743-3753
[Abstract]
[Full Text]
-
Kapetanovich, L., Baughman, C., Lee, T. H.
(2005). Nm23H2 Facilitates Coat Protein Complex II Assembly and Endoplasmic Reticulum Export in Mammalian Cells. Mol. Biol. Cell
16: 835-848
[Abstract]
[Full Text]
-
Ben-Tekaya, H., Miura, K., Pepperkok, R., Hauri, H.-P.
(2005). Live imaging of bidirectional traffic from the ERGIC. J. Cell Sci.
118: 357-367
[Abstract]
[Full Text]
-
Nadanaka, S., Yoshida, H., Kano, F., Murata, M., Mori, K.
(2004). Activation of Mammalian Unfolded Protein Response Is Compatible with the Quality Control System Operating in the Endoplasmic Reticulum. Mol. Biol. Cell
15: 2537-2548
[Abstract]
[Full Text]
-
Almagro, S., Riveline, D., Hirano, T., Houchmandzadeh, B., Dimitrov, S.
(2004). The Mitotic Chromosome Is an Assembly of Rigid Elastic Axes Organized by Structural Maintenance of Chromosomes (SMC) Proteins and Surrounded by a Soft Chromatin Envelope. J. Biol. Chem.
279: 5118-5126
[Abstract]
[Full Text]
-
O'Callaghan, D. W., Hasdemir, B., Leighton, M., Burgoyne, R. D.
(2003). Residues within the myristoylation motif determine intracellular targeting of the neuronal Ca2+ sensor protein KChIP1 to post-ER transport vesicles and traffic of Kv4 K+ channels. J. Cell Sci.
116: 4833-4845
[Abstract]
[Full Text]
-
Polishchuk, E. V., Di Pentima, A., Luini, A., Polishchuk, R. S.
(2003). Mechanism of Constitutive Export from the Golgi: Bulk Flow via the Formation, Protrusion, and En Bloc Cleavage of large trans-Golgi Network Tubular Domains. Mol. Biol. Cell
14: 4470-4485
[Abstract]
[Full Text]
-
Garcia-Mata, R., Szul, T., Alvarez, C., Sztul, E.
(2003). ADP-Ribosylation Factor/COPI-dependent Events at the Endoplasmic Reticulum-Golgi Interface Are Regulated by the Guanine Nucleotide Exchange Factor GBF1. Mol. Biol. Cell
14: 2250-2261
[Abstract]
[Full Text]
-
Mogelsvang, S., Gomez-Ospina, N., Soderholm, J., Glick, B. S., Staehelin, L. A.
(2003). Tomographic Evidence for Continuous Turnover of Golgi Cisternae in Pichia pastoris. Mol. Biol. Cell
14: 2277-2291
[Abstract]
[Full Text]
-
Horstmann, H., Ng, C. P., Tang, B. L., Hong, W.
(2002). Ultrastructural characterization of endoplasmic reticulum -- Golgi transport containers (EGTC). J. Cell Sci.
115: 4263-4273
[Abstract]
[Full Text]
-
Poirier, M. G., Eroglu, S., Marko, J. F.
(2002). The Bending Rigidity of Mitotic Chromosomes. Mol. Biol. Cell
13: 2170-2179
[Abstract]
[Full Text]
-
Ferreira, T., Mason, A. B., Pypaert, M., Allen, K. E., Slayman, C. W.
(2002). Quality Control in the Yeast Secretory Pathway. A MISFOLDED PMA1 H+-ATPase REVEALS TWO CHECKPOINTS. J. Biol. Chem.
277: 21027-21040
[Abstract]
[Full Text]
-
Rust, R. C., Landmann, L., Gosert, R., Tang, B. L., Hong, W., Hauri, H.-P., Egger, D., Bienz, K.
(2001). Cellular COPII Proteins Are Involved in Production of the Vesicles That Form the Poliovirus Replication Complex. J. Virol.
75: 9808-9818
[Abstract]
[Full Text]
-
Zuber, C., Fan, J.-y., Guhl, B., Parodi, A., Fessler, J. H., Parker, C., Roth, J.
(2001). Immunolocalization of UDP-glucose:glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality control. Proc. Natl. Acad. Sci. USA
10.1073/pnas.191359198v1
[Abstract]
[Full Text]
-
Kondylis, V., Goulding, S. E., Dunne, J. C., Rabouille, C.
(2001). Biogenesis of Golgi Stacks in Imaginal Discs of Drosophila melanogaster. Mol. Biol. Cell
12: 2308-2327
[Abstract]
[Full Text]
-
Rossanese, O. W., Reinke, C. A., Bevis, B. J., Hammond, A. T., Sears, I. B., O'Connor, J., Glick, B. S.
(2001). A Role for Actin, Cdc1p, and Myo2p in the Inheritance of Late Golgi Elements in Saccharomyces cerevisiae. JCB
153: 47-62
[Abstract]
[Full Text]
-
Brugger, B., Sandhoff, R., Wegehingel, S., Gorgas, K., Malsam, J., Helms, J. B., Lehmann, W.-D., Nickel, W., Wieland, F. T.
(2000). Evidence for Segregation of Sphingomyelin and Cholesterol during Formation of Copi-Coated Vesicles. JCB
151: 507-518
[Abstract]
[Full Text]
-
Hammond, A. T., Glick, B. S.
(2000). Dynamics of Transitional Endoplasmic Reticulum Sites in Vertebrate Cells. Mol. Biol. Cell
11: 3013-3030
[Abstract]
[Full Text]
-
Sanchez, V., Sztul, E., Britt, W. J.
(2000). Human Cytomegalovirus pp28 (UL99) Localizes to a Cytoplasmic Compartment Which Overlaps the Endoplasmic Reticulum-Golgi-Intermediate Compartment. J. Virol.
74: 3842-3851
[Abstract]
[Full Text]
-
Pedrazzini, E., Villa, A., Longhi, R., Bulbarelli, A., Borgese, N.
(2000). Mechanism of Residence of Cytochrome B(5), a Tail-Anchored Protein, in the Endoplasmic Reticulum. JCB
148: 899-914
[Abstract]
[Full Text]
-
Weise, F, Stierhof, Y., Kuhn, C, Wiese, M, Overath, P
(2000). Distribution of GPI-anchored proteins in the protozoan parasite Leishmania, based on an improved ultrastructural description using high-pressure frozen cells. J. Cell Sci.
113: 4587-4603
[Abstract]
-
Polishchuk, R. S., Polishchuk, E. V., Marra, P., Alberti, S., Buccione, R., Luini, A., Mironov, A. A.
(2000). Correlative Light-Electron Microscopy Reveals the Tubular-Saccular Ultrastructure of Carriers Operating between Golgi Apparatus and Plasma Membrane. JCB
148: 45-58
[Abstract]
[Full Text]
-
Ying, M, Flatmark, T, Saraste, J
(2000). The p58-positive pre-golgi intermediates consist of distinct subpopulations of particles that show differential binding of COPI and COPII coats and contain vacuolar H(+)-ATPase. J. Cell Sci.
113: 3623-3638
[Abstract]
-
De Matteis, M., Morrow, J.
(2000). Spectrin tethers and mesh in the biosynthetic pathway. J. Cell Sci.
113: 2331-2343
[Abstract]
-
Kuiper, R. P., Waterham, H. R., Rötter, J., Bouw, G., Martens, G. J. M.
(2000). Differential Induction of Two p24delta Putative Cargo Receptors upon Activation of a Prohormoneproducing Cell. Mol. Biol. Cell
11: 131-140
[Abstract]
[Full Text]
-
Lin, C.-C., Love, H. D., Gushue, J. N., Bergeron, J. J.M., Ostermann, J.
(1999). ER/Golgi Intermediates Acquire Golgi Enzymes by Brefeldin a-Sensitive Retrograde Transport in Vitro. JCB
147: 1457-1472
[Abstract]
[Full Text]
-
Alvarez, C., Fujita, H., Hubbard, A., Sztul, E.
(1999). ER to Golgi Transport: Requirement for P115 at a Pre-Golgi Vtc Stage. JCB
147: 1205-1222
[Abstract]
[Full Text]
-
Annaert, W. G., Levesque, L., Craessaerts, K., Dierinck, I., Snellings, G., Westaway, D., George-Hyslop, P. St., Cordell, B., Fraser, P., De Strooper, B.
(1999). Presenilin 1 Controls {gamma}-Secretase Processing of Amyloid Precursor Protein in Pre-Golgi Compartments of Hippocampal Neurons. JCB
147: 277-294
[Abstract]
[Full Text]
-
Allan, B. B., Balch, W. E.
(1999). Protein Sorting by Directed Maturation of Golgi Compartments. Science
285: 63-66
[Abstract]
[Full Text]
-
Dominguez, M., Fazel, A., Dahan, S., Lovell, J., Hermo, L., Claude, A., Melancon, P., Bergeron, J.J.M.
(1999). Fusogenic Domains of Golgi Membranes Are Sequestered into Specialized Regions of the Stack that Can Be Released by Mechanical Fragmentation. JCB
145: 673-688
[Abstract]
[Full Text]
-
Lee, T. H., Linstedt, A. D.
(1999). Osmotically Induced Cell Volume Changes Alter Anterograde and Retrograde Transport, Golgi Structure, and COPI Dissociation. Mol. Biol. Cell
10: 1445-1462
[Abstract]
[Full Text]
-
Houchmandzadeh, B., Dimitrov, S.
(1999). Elasticity Measurements Show the Existence of Thin Rigid Cores Inside Mitotic Chromosomes. JCB
145: 215-223
[Abstract]
[Full Text]
-
Rossanese, O. W., Soderholm, J., Bevis, B. J., Sears, I. B., O'Connor, J., Williamson, E. K., Glick, B. S.
(1999). Golgi Structure Correlates with Transitional Endoplasmic Reticulum Organization in Pichia pastoris and Saccharomyces cerevisiae. JCB
145: 69-81
[Abstract]
[Full Text]
-
Infante, C., Ramos-Morales, F., Fedriani, C., Bornens, M., Rios, R. M.
(1999). GMAP-210, A Cis-Golgi Network-associated Protein, Is a Minus End Microtubule-binding Protein. JCB
145: 83-98
[Abstract]
[Full Text]
-
Hu, T., Kao, C.-Y., Hudson, R. T., Chen, A., Draper, R. K.
(1999). Inhibition of Secretion by 1,3-Cyclohexanebis(methylamine), a Dibasic Compound That Interferes with Coatomer Function. Mol. Biol. Cell
10: 921-933
[Abstract]
[Full Text]
-
Ladinsky, M. S., Mastronarde, D. N., McIntosh, J. R., Howell, K. E., Staehelin, L. A.
(1999). Golgi Structure in Three Dimensions: Functional Insights from the Normal Rat Kidney Cell. JCB
144: 1135-1149
[Abstract]
[Full Text]
-
Dannies, P. S.
(1999). Protein Hormone Storage in Secretory Granules: Mechanisms for Concentration and Sorting. Endocr. Rev.
20: 3-21
[Abstract]
[Full Text]
-
Zhang, T., Wong, S. H., Tang, B. L., Xu, Y., Hong, W.
(1999). Morphological and Functional Association of Sec22b/ERS-24 with the pre-Golgi Intermediate Compartment. Mol. Biol. Cell
10: 435-453
[Abstract]
[Full Text]
-
Martin, M., Hidalgo, J, Vega, F., Velasco, A
(1999). Trimeric G proteins modulate the dynamic interaction of PKAII with the Golgi complex. J. Cell Sci.
112: 3869-3878
[Abstract]
-
Skoudy, A, Nhieu, G., Mantis, N, Arpin, M, Mounier, J, Gounon, P, Sansonetti, P
(1999). A functional role for ezrin during Shigella flexneri entry into epithelial cells. J. Cell Sci.
112: 2059-2068
[Abstract]
-
Gao, Y.-s., Alvarez, C., Nelson, D. S., Sztul, E.
(1998). Molecular Cloning, Characterization, and Dynamics of Rat Formiminotransferase Cyclodeaminase, a Golgi-associated 58-kDa Protein. J. Biol. Chem.
273: 33825-33834
[Abstract]
[Full Text]
-
Nelson, D. S., Alvarez, C., Gao, Y.-s., Garcia-Mata, R., Fialkowski, E., Sztul, E.
(1998). The Membrane Transport Factor TAP/p115 Cycles between the Golgi and Earlier Secretory Compartments and Contains Distinct Domains Required for Its Localization and Function. JCB
143: 319-331
[Abstract]
[Full Text]
-
Sun, X., Alzhanova-Ericsson, A. T., Visa, N., Aissouni, Y., Zhao, J., Daneholt, B.
(1998). The hrp23 Protein in the Balbiani Ring Pre-mRNP Particles Is Released Just before or at the Binding of the Particles to the Nuclear Pore Complex. JCB
142: 1181-1193
[Abstract]
[Full Text]
-
Olichney, J. M., Galasko, D., Salmon, D. P., Hofstetter, C. R., Hansen, L. A., Katzman, R., Thal, L. J.
(1998). Cognitive decline is faster in Lewy body variant than in Alzheimer's disease. Neurology
51: 351-357
[Abstract]
[Full Text]
-
Vollenweider, F., Kappeler, F., Itin, C., Hauri, H.-P.
(1998). Mistargeting of the Lectin ERGIC-53 to the Endoplasmic Reticulum of HeLa Cells Impairs the Secretion of a Lysosomal Enzyme. JCB
142: 377-389
[Abstract]
[Full Text]
-
Godi, A., Santone, I., Pertile, P., Devarajan, P., Stabach, P. R., Morrow, J. S., Di Tullio, G., Polishchuk, R., Petrucci, T. C., Luini, A., De Matteis, M. A.
(1998). ADP ribosylation factor regulates spectrin binding to the Golgi complex. Proc. Natl. Acad. Sci. USA
95: 8607-8612
[Abstract]
[Full Text]
-
Brown, C. L., Meise, K. S., Plowman, G. D., Coffey, R. J., Dempsey, P. J.
(1998). Cell Surface Ectodomain Cleavage of Human Amphiregulin Precursor Is Sensitive to a Metalloprotease Inhibitor. RELEASE OF A PREDOMINANT N-GLYCOSYLATED 43-kDa SOLUBLE FORM. J. Biol. Chem.
273: 17258-17268
[Abstract]
[Full Text]
-
Price, L. S., Leng, J., Schwartz, M. A., Bokoch, G. M.
(1998). Activation of Rac and Cdc42 by Integrins Mediates Cell Spreading. Mol. Biol. Cell
9: 1863-1871
[Abstract]
[Full Text]
-
Kim, P. S., Arvan, P.
(1998). Endocrinopathies in the Family of Endoplasmic Reticulum (ER) Storage Diseases: Disorders of Protein Trafficking and the Role of ER Molecular Chaperones. Endocr. Rev.
19: 173-202
[Abstract]
[Full Text]
-
Love, H. D., Lin, C.-C., Short, C. S., Ostermann, J.
(1998). Isolation of Functional Golgi-derived Vesicles with a Possible Role in Retrograde Transport. JCB
140: 541-551
[Abstract]
[Full Text]
-
Mironov, A. JR., Luini, A., Mironov, A.
(1998). A synthetic model of intra-Golgi traffic. FASEB J.
12: 249-252
[Abstract]
[Full Text]
-
Fujiwara, T., Takami, N., Misumi, Y., Ikehara, Y.
(1998). Nordihydroguaiaretic Acid Blocks Protein Transport in the Secretory Pathway Causing Redistribution of Golgi Proteins into the Endoplasmic Reticulum. J. Biol. Chem.
273: 3068-3075
[Abstract]
[Full Text]
-
Rowe, T., Dascher, C., Bannykh, S., Plutner, H., Balch, W. E.
(1998). Role of Vesicle-Associated Syntaxin 5 in the Assembly of Pre-Golgi Intermediates. Science
279: 696-700
[Abstract]
[Full Text]
-
Klumperman, J, Schweizer, A, Clausen, H, Tang, B., Hong, W, Oorschot, V, Hauri, H.
(1998). The recycling pathway of protein ERGIC-53 and dynamics of the ER-Golgi intermediate compartment. J. Cell Sci.
111: 3411-3425
[Abstract]
-
Monier, S, Chardin, P, Robineau, S, Goud, B
(1998). Overexpression of the ARF1 exchange factor ARNO inhibits the early secretory pathway and causes the disassembly of the Golgi complex. J. Cell Sci.
111: 3427-3436
[Abstract]
-
Hong, W
(1998). Protein transport from the endoplasmic reticulum to the Golgi apparatus. J. Cell Sci.
111: 2831-2839
[Abstract]
-
Nickel, W, Malsam, J, Gorgas, K, Ravazzola, M, Jenne, N, Helms, J., Wieland, F.
(1998). Uptake by COPI-coated vesicles of both anterograde and retrograde cargo is inhibited by GTPgammaS in vitro. J. Cell Sci.
111: 3081-3090
[Abstract]
-
Pepperkok, R, Lowe, M, Burke, B, Kreis, T.
(1998). Three distinct steps in transport of vesicular stomatitis virus glycoprotein from the ER to the cell surface in vivo with differential sensitivities to GTP gamma S. J. Cell Sci.
111: 1877-1888
[Abstract]
-
Kappeler, F., Klopfenstein, D. R. Ch., Foguet, M., Paccaud, J.-P., Hauri, H.-P.
(1997). The Recycling of ERGIC-53 in the Early Secretory Pathway. ERGIC-53 CARRIES A CYTOSOLIC ENDOPLASMIC RETICULUM-EXIT DETERMINANT INTERACTING WITH COPII. J. Biol. Chem.
272: 31801-31808
[Abstract]
[Full Text]
-
Zhang, T., Wong, S. H., Tang, B. L., Xu, Y., Peter, F., Subramaniam, V. N., Hong, W.
(1997). The Mammalian Protein (rbet1) Homologous to Yeast Bet1p Is Primarily Associated with the Pre-Golgi Intermediate Compartment and Is Involved in Vesicular Transport from the Endoplasmic Reticulum to the Golgi Apparatus. JCB
139: 1157-1168
[Abstract]
[Full Text]
-
Devarajan, P., Stabach, P. R., De Matteis, M. A., Morrow, J. S.
(1997). Na,K-ATPase transport from endoplasmic reticulum to Golgi requires the Golgi spectrin-ankyrin G119 skeleton in Madin Darby canine kidney cells. Proc. Natl. Acad. Sci. USA
94: 10711-10716
[Abstract]
[Full Text]
-
Gomez, M., Scales, S. J., Kreis, T. E., Perez, F.
(2000). Membrane Recruitment of Coatomer and Binding to Dilysine Signals Are Separate Events. J. Biol. Chem.
275: 29162-29169
[Abstract]
[Full Text]
-
Zuber, C., Fan, J.-y., Guhl, B., Parodi, A., Fessler, J. H., Parker, C., Roth, J.
(2001). Immunolocalization of UDP-glucose:glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality control. Proc. Natl. Acad. Sci. USA
98: 10710-10715
[Abstract]
[Full Text]
-
Martinez-Menarguez, J. A., Prekeris, R., Oorschot, V. M.J., Scheller, R., Slot, J. W., Geuze, H. J., Klumperman, J.
(2001). Peri-Golgi vesicles contain retrograde but not anterograde proteins consistent with the cisternal progression model of intra-Golgi transport. JCB
155: 1213-1224
[Abstract]
[Full Text]
-
Mironov, A. A., Beznoussenko, G. V., Nicoziani, P., Martella, O., Trucco, A., Kweon, H.-S., Di Giandomenico, D., Polishchuk, R. S., Fusella, A., Lupetti, P., Berger, E. G., Geerts, W. J.C., Koster, A. J., Burger, K. N.J., Luini, A.
(2001). Small cargo proteins and large aggregates can traverse the Golgi by a common mechanism without leaving the lumen of cisternae. JCB
155: 1225-1238
[Abstract]
[Full Text]
Top
Pleomorphic Elements Function in...
Biochemical Composition of VTCs