A peripheral protein associated with the cis-Golgi network redistributes in the intermediate compartment upon brefeldin A treatment

doi:10.1083/jcb.125.5.997

This Article

	Full Text (PDF, 6771K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Rios, R. M.
	Articles by Bornens, M.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Rios, R. M.
	Articles by Bornens, M.


Social Bookmarking

	What's this?

ARTICLES

A peripheral protein associated with the cis-Golgi network redistributes in the intermediate compartment upon brefeldin A treatment

RM Rios, AM Tassin, C Celati, C Antony, MC Boissier, JC Homberg and M Bornens
Centre de Genetique Moleculaire, Centre National de la Recherche Scientifique, Yvette, France.

Human autoantibodies offer unique tools for the study of cellular constituents since they usually recognize highly conserved components, the most difficult to detect due to their low immunogenicity. The serum from a patient with Sjogren's syndrome (RM serum) showing a very high reactivity to the Golgi complex has been shown to immunoprecipitate and to immunodetect by Western blotting experiments a protein mol wt 210,000 (p210) that was shown to be peripheral and cytoplasmically disposed. A close examination of the p210 labeling revealed some differences with Golgi markers: RM serum staining was slightly more extensive than several Golgi markers and showed a discontinuous or granular appearance. Nocodazole induced a specific and early segregation of many p210-associated vesicles or tubules from Golgi apparatus. Upon brefeldin A treatment, p210 did not redistribute in the ER as did other Golgi proteins. In contrast, it exhibited a vesicular pattern reminiscent to that displayed by proteins residing in the intermediate compartment. Double staining immunofluorescence using the RM serum and the marker of the intermediate compartment, p58, revealed segregation of both proteins in control conditions but colocalization in BFA-treated cells. We have further demonstrated by combining different drug treatments that p210-containing elements in brefeldin A- treated cells belong indeed to the intermediate compartment. Experiments on brefeldin A recovery suggested that these p210 elements might play a role in reformation and repositioning of the Golgi apparatus. Ultrastructural localization performed by immunoperoxidase staining allowed us to establish that p210 interacted with the external side of an abundant tubulo-vesicular system on the cis side of the Golgi complex which extended to connecting structures and vesicles between saccules or stacks of cisternae, p210 appears to be a novel protein residing in the cis-Golgi network that may cycle between the Golgi apparatus and the intermediate compartment.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Drin, G., Morello, V., Casella, J.-F., Gounon, P., Antonny, B. (2008). Asymmetric Tethering of Flat and Curved Lipid Membranes by a Golgin. Science 320: 670-673 [Abstract] [Full Text]
Chen, Y., Chen, C., Wang, Y., Liu-Chen, L.-Y. (2006). Ligands Regulate Cell Surface Level of the Human {kappa} Opioid Receptor by Activation-Induced Down-Regulation and Pharmacological Chaperone-Mediated Enhancement: Differential Effects of Nonpeptide and Peptide Agonists. J. Pharmacol. Exp. Ther. 319: 765-775 [Abstract] [Full Text]
Barr, F. A., Egerer, J. (2005). Golgi positioning: are we looking at the right MAP?. JCB 168: 993-998 [Abstract] [Full Text]
Gillingham, A. K., Tong, A. H. Y., Boone, C., Munro, S. (2004). The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi. JCB 167: 281-292 [Abstract] [Full Text]
Lu, L., Tai, G., Hong, W. (2004). Autoantigen Golgin-97, an Effector of Arl1 GTPase, Participates in Traffic from the Endosome to the Trans-Golgi Network. Mol. Biol. Cell 15: 4426-4443 [Abstract] [Full Text]
Ohta, E., Misumi, Y., Sohda, M., Fujiwara, T., Yano, A., Ikehara, Y. (2003). Identification and Characterization of GCP16, a Novel Acylated Golgi Protein That Interacts with GCP170. J. Biol. Chem. 278: 51957-51967 [Abstract] [Full Text]
Chantalat, S., Courbeyrette, R., Senic-Matuglia, F., Jackson, C. L., Goud, B., Peyroche, A. (2003). A Novel Golgi Membrane Protein Is a Partner of the ARF Exchange Factors Gea1p and Gea2p. Mol. Biol. Cell 14: 2357-2371 [Abstract] [Full Text]
Pfannenschmid, F., Wimmer, V. C., Rios, R.-M., Geimer, S., Krockel, U., Leiherer, A., Haller, K., Nemcova, Y., Mages, W. (2003). Chlamydomonas DIP13 and human NA14: a new class of proteins associated with microtubule structures is involved in cell division. J. Cell Sci. 116: 1449-1462 [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]
Ramos-Morales, F., Infante, C., Fedriani, C., Bornens, M., Rios, R. M. (1998). NA14 Is a Novel Nuclear Autoantigen with a Coiled-coil Domain. J. Biol. Chem. 273: 1634-1639 [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]
Levi, S, Vannier, C, Triller, A (1998). Strychnine-sensitive stabilization of postsynaptic glycine receptor clusters. J. Cell Sci. 111: 335-345 [Abstract]
Rojo, M., Pepperkok, R., Emery, G., Kellner, R., Stang, E., Parton, R. G., Gruenberg, J. (1997). Involvement of the Transmembrane Protein p23 in Biosynthetic Protein Transport. JCB 139: 1119-1135 [Abstract] [Full Text]
Mironov, A., Colanzi, A., Silletta, M. G., Fiucci, G., Flati, S., Fusella, A., Polishchuk, R., Mironov, A. Jr., Tullio, G. D., Weigert, R., Malhotra, V., Corda, D., Matteis, M. A. D., Luini, A. (1997). Role of NAD+ and ADP-Ribosylation in the Maintenance of the Golgi Structure. JCB 139: 1109-1118 [Abstract] [Full Text]
Misumi, Y., Sohda, M., Yano, A., Fujiwara, T., Ikehara, Y. (1997). Molecular Characterization of GCP170, a 170-kDa Protein Associated with the Cytoplasmic Face of the Golgi Membrane. J. Biol. Chem. 272: 23851-23858 [Abstract] [Full Text]
Racca, C., Gardiol, A., Triller, A. (1997). Dendritic and Postsynaptic Localizations of Glycine Receptor alpha �Subunit mRNAs. J. Neurosci. 17: 1691-1700 [Abstract] [Full Text]
Mikus, P., Ny, T. (1996). Intracellular Polymerization of the Serpin Plasminogen Activator Inhibitor Type 2. J. Biol. Chem. 271: 10048-10053 [Abstract] [Full Text]
Erlich, R., Gleeson, P. A., Campbell, P., Dietzsch, E., Toh, B.-H. (1996). Molecular Characterization of trans-Golgi p230. J. Biol. Chem. 271: 8328-8337 [Abstract] [Full Text]
Hay, J. C., Hirling, H., Scheller, R. H. (1996). Mammalian Vesicle Trafficking Proteins of the Endoplasmic Reticulum and Golgi Apparatus. J. Biol. Chem. 271: 5671-5679 [Abstract] [Full Text]
Wang, C.-N., Hobman, T. C., Brindley, D. N. (1995). Degradation of Apolipoprotein B in Cultured Rat Hepatocytes Occurs in a Post-endoplasmic Reticulum Compartment. J. Biol. Chem. 270: 24924-24931 [Abstract] [Full Text]
Charest, A., Lane, K., McMahon, K., Housman, D. E. (2001). Association of a Novel PDZ Domain-containing Peripheral Golgi Protein with the Q-SNARE (Q-soluble N-Ethylmaleimide-sensitive Fusion Protein (NSF) Attachment Protein Receptor) Protein Syntaxin 6. J. Biol. Chem. 276: 29456-29465 [Abstract] [Full Text]