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

This Article Full Text Full Text (PDF, 296K) PPT slides of all figures 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 Barr, F. A. Articles by Körner, R. Search for Related Content PubMed PubMed Citation Articles by Barr, F. A. Articles by Körner, R. Social Bookmarking                            What's this?

© The Rockefeller University Press, 0021-9525/2001/12/885 $5.00
The Journal of Cell Biology, Volume 155, Number 6, December 10, 2001 885-892

Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus

Department of Cell Biology, Max-Planck-Institute of Biochemistry, 82152 Martinsried, Germany

Address correspondence to Francis Barr, Dept. of Cell Biology, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18a, 82152 Martinsried, Germany. Tel.: 49-89-8578-3135. Fax: 49-89-8578-3102. E-mail: barr{at}biochem.mpg.de

The Golgi apparatus is a highly complex organelle comprised of a stack of cisternal membranes on the secretory pathway from the ER to the cell surface. This structure is maintained by an exoskeleton or Golgi matrix constructed from a family of coiled-coil proteins, the golgins, and other peripheral membrane components such as GRASP55 and GRASP65. Here we find that TMP21, p24a, and gp25L, members of the p24 cargo receptor family, are present in complexes with GRASP55 and GRASP65 in vivo. GRASPs interact directly with the cytoplasmic domains of specific p24 cargo receptors depending on their oligomeric state, and mutation of the GRASP binding site in the cytoplasmic tail of one of these, p24a, results in it being transported to the cell surface. These results suggest that one function of the Golgi matrix is to aid efficient retention or sequestration of p24 cargo receptors and other membrane proteins in the Golgi apparatus.

Key Words: GRASPs; p24 proteins; Golgi matrix; protein transport; cargo receptors

CiteULike    Complore    Connotea    Del.icio.us    Digg    Facebook    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

• Struck, N. S., Herrmann, S., Langer, C., Krueger, A., Foth, B. J., Engelberg, K., Cabrera, A. L., Haase, S., Treeck, M., Marti, M., Cowman, A. F., Spielmann, T., Gilberger, T. W. (2008). Plasmodium falciparum possesses two GRASP proteins that are differentially targeted to the Golgi complex via a higher- and lower-eukaryote-like mechanism. J. Cell Sci. 121: 2123-2129 [Abstract] [Full Text]  
• Feinstein, T. N., Linstedt, A. D. (2008). GRASP55 Regulates Golgi Ribbon Formation. Mol. Biol. Cell 19: 2696-2707 [Abstract] [Full Text]  
• Mitrovic, S., Ben-Tekaya, H., Koegler, E., Gruenberg, J., Hauri, H.-P. (2008). The Cargo Receptors Surf4, Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC)-53, and p25 Are Required to Maintain the Architecture of ERGIC and Golgi. Mol. Biol. Cell 19: 1976-1990 [Abstract] [Full Text]  
• Haas, A. K., Yoshimura, S.-i., Stephens, D. J., Preisinger, C., Fuchs, E., Barr, F. A. (2007). Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs required to maintain a functional Golgi complex in human cells. J. Cell Sci. 120: 2997-3010 [Abstract] [Full Text]  
• Gupta, V., Swarup, G. (2006). Evidence for a role of transmembrane protein p25 in localization of protein tyrosine phosphatase TC48 to the ER. J. Cell Sci. 119: 1703-1714 [Abstract] [Full Text]  
• Struck, N. S., de Souza Dias, S., Langer, C., Marti, M., Pearce, J. A., Cowman, A. F., Gilberger, T. W. (2005). Re-defining the Golgi complex in Plasmodium falciparum using the novel Golgi marker PfGRASP. J. Cell Sci. 118: 5603-5613 [Abstract] [Full Text]  
• Kondylis, V., Spoorendonk, K. M., Rabouille, C. (2005). dGRASP Localization and Function in the Early Exocytic Pathway in Drosophila S2 Cells. Mol. Biol. Cell 16: 4061-4072 [Abstract] [Full Text]  
• Yoshimura, S.-i., Yoshioka, K., Barr, F. A., Lowe, M., Nakayama, K., Ohkuma, S., Nakamura, N. (2005). Convergence of Cell Cycle Regulation and Growth Factor Signals on GRASP65. J. Biol. Chem. 280: 23048-23056 [Abstract] [Full Text]  
• Wang, Y., Satoh, A., Warren, G. (2005). Mapping the Functional Domains of the Golgi Stacking Factor GRASP65. J. Biol. Chem. 280: 4921-4928 [Abstract] [Full Text]  
• Yoshimura, S.-i., Yamamoto, A., Misumi, Y., Sohda, M., Barr, F. A., Fujii, G., Shakoori, A., Ohno, H., Mihara, K., Nakamura, N. (2004). Dynamics of Golgi Matrix Proteins after the Blockage of ER to Golgi Transport. J Biochem 135: 201-216 [Abstract] [Full Text]  
• Emery, G., Parton, R. G., Rojo, M., Gruenberg, J. (2003). The trans-membrane protein p25 forms highly specialized domains that regulate membrane composition and dynamics. J. Cell Sci. 116: 4821-4832 [Abstract] [Full Text]  
• Urbe, S., Sachse, M., Row, P. E., Preisinger, C., Barr, F. A., Strous, G., Klumperman, J., Clague, M. J. (2003). The UIM domain of Hrs couples receptor sorting to vesicle formation. J. Cell Sci. 116: 4169-4179 [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]  
• Jenne, N., Frey, K., Brugger, B., Wieland, F. T. (2002). Oligomeric State and Stoichiometry of p24 Proteins in the Early Secretory Pathway. J. Biol. Chem. 277: 46504-46511 [Abstract] [Full Text]  

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