The Journal of Cell Biology, Vol 124, 649-665, Copyright © 1994 by The Rockefeller University Press

ARTICLES

gp74 a membrane glycoprotein of the cis-Golgi network that cycles through the endoplasmic reticulum and intermediate compartment

J Alcalde, G Egea and IV Sandoval
Centro de Biologia Molecular Severo Ochoa, Facultad de Ciencias, Universidad Autonoma de Madrid, Cantoblanco, Spain.

A monoclonal antibody CC92 (IgM), raised against a fraction of rat liver enriched in Golgi membranes, recognizes a novel Endo H-resistant 74-kD membrane glycoprotein (gp74). The bulk of gp74 is confined to the cis-Golgi network (CGN). Outside the Golgi gp74 is found in tubulovesicular structures and ER foci. In cells incubated at 37 degrees C the majority of gp74 is segregated from the intermediate compartment (IC) marker p58. However, in cells treated with organelle perturbants such as low temperature, BFA, and [AIF4]- the patterns of the two proteins become indistinguishable. Both proteins are retained in the Golgi complex at 20 degrees C and in the IC at 15 degrees C. Incubation of cells with BFA results in relocation of gp74 to p58 positive IC elements. [AIF4]- induces the redistribution of gp74 from the Golgi to p58-positive vesicles and does not retard the translocation of gp74 to IC elements in cells treated with BFA. Disruption of microtubules by nocodazol results in the rapid disappearance of the Golgi elements stained by gp74 and redistribution of the protein into vesicle-like structures. The responses of gp74 to cell perturbants are in sharp contrast with those of cis/middle and trans-Golgi resident proteins whose location is not affected by low temperatures or [AIF4]-, are translocated to the ER upon addition of BFA, and stay in slow disintegrating Golgi elements in cells treated with nocodazol. The results suggest that gp74 is an itinerant protein that resides most of the time in the CGN and cycles through the ER/IC following the pathway used by p58.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Facebook    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

• Martin-Acebes, M. A., Gonzalez-Magaldi, M., Vazquez-Calvo, A., Armas-Portela, R., Sobrino, F. (2009). Internalization of Swine Vesicular Disease Virus into Cultured Cells: a Comparative Study with Foot-and-Mouth Disease Virus. J. Virol. 83: 4216-4226 [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]  
• Lavoie, C., Meerloo, T., Lin, P., Farquhar, M. G. (2002). Calnuc, an EF-Hand Ca2+-Binding Protein, Is Stored and Processed in the Golgi and Secreted by the Constitutive-Like Pathway in AtT20 Cells. Mol. Endocrinol. 16: 2462-2474 [Abstract] [Full Text]  
• Rojo, M, Emery, G, Marjomaki, V, McDowall, A., Parton, R., Gruenberg, J (2000). The transmembrane protein p23 contributes to the organization of the Golgi apparatus. J. Cell Sci. 113: 1043-1057 [Abstract]  
• Hauri, H., Kappeler, F, Andersson, H, Appenzeller, C (2000). ERGIC-53 and traffic in the secretory pathway. J. Cell Sci. 113: 587-596 [Abstract]  
• 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]  
• del Valle, M, Robledo, Y, Sandoval, I. (1999). Membrane flow through the Golgi apparatus: specific disassembly of the cis-Golgi network by ATP depletion. J. Cell Sci. 112: 4017-4029 [Abstract]  
• Babia, T, Ayala, I, Valderrama, F, Mato, E, Bosch, M, Santaren, J., Renau-Piqueras, J, Kok, J., Thomson, T., Egea, G (1999). N-Ras induces alterations in Golgi complex architecture and in constitutive protein transport. J. Cell Sci. 112: 477-489 [Abstract]  
• Andres, G., Garcia-Escudero, R., Simon-Mateo, C., Vinuela, E. (1998). African Swine Fever Virus Is Enveloped by a Two-Membraned Collapsed Cisterna Derived from the Endoplasmic Reticulum. J. Virol. 72: 8988-9001 [Abstract] [Full Text]  
• Kok, J. W., Babia, T., Filipeanu, C. M., Nelemans, A., Egea, G., Hoekstra, D. (1998). PDMP Blocks Brefeldin A-induced Retrograde Membrane Transport from Golgi to ER: Evidence for Involvement of Calcium Homeostasis and Dissociation from Sphingolipid Metabolism. JCB 142: 25-38 [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]  
• 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]  
• Hoe, M. H., Slusarewicz, P., Misteli, T., Watson, R., Warren, G. (1995). Evidence for Recycling of the Resident medial/trans Golgi Enzyme, N-Acetylglucosaminyltransferase I, in ldlD Cells. J. Biol. Chem. 270: 25057-25063 [Abstract] [Full Text]  
• Subramaniam, V., Krijnse-Locker, J, Tang, B., Ericsson, M, Yusoff, A., Griffiths, G, Hong, W (1995). Monoclonal antibody HFD9 identifies a novel 28 kDa integral membrane protein on the cis-Golgi. J. Cell Sci. 108: 2405-2414 [Abstract]  
• Rabouille, C, Hui, N, Hunte, F, Kieckbusch, R, Berger, E., Warren, G, Nilsson, T (1995). Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides. J. Cell Sci. 108: 1617-1627 [Abstract]  
• 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]  

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents