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

This Article Full Text PDF (Full Text) 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 Pfeffer, S. R. Search for Related Content PubMed PubMed Citation Articles by Pfeffer, S. R. Social Bookmarking                      What's this?

Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305

Address correspondence to Suzanne R. Pfeffer, Department of Biochemistry, B400, Stanford University School of Medicine, Stanford, CA 94305. Tel.: (650) 723-6169. Fax: (650) 723-6776. E-mail: pfeffer{at}cmgm.stanford.edu

In this issue, Short et al. report the discovery of a protein named Golgin-45 that is located on the surface of the middle (or medial) cisternae of the Golgi complex. Depletion of this protein disrupts the Golgi complex and leads to the return of a resident, lumenal, medial Golgi enzyme to the endoplasmic reticulum. These findings suggest that Golgin-45 serves as a linchpin for the maintenance of Golgi complex structure, and offer hints as to the mechanisms by which the polarized Golgi complex is constructed.

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

This article has been cited by other articles:

• Tang, D., Mar, K., Warren, G., Wang, Y. (2008). Molecular Mechanism of Mitotic Golgi Disassembly and Reassembly Revealed by a Defined Reconstitution Assay. J. Biol. Chem. 283: 6085-6094 [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]  
• Derby, M. C., van Vliet, C., Brown, D., Luke, M. R., Lu, L., Hong, W., Stow, J. L., Gleeson, P. A. (2004). Mammalian GRIP domain proteins differ in their membrane binding properties and are recruited to distinct domains of the TGN. J. Cell Sci. 117: 5865-5874 [Abstract] [Full Text]  
• Preisinger, C., Short, B., De Corte, V., Bruyneel, E., Haas, A., Kopajtich, R., Gettemans, J., Barr, F. A. (2004). YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3{zeta}. J. Cell Biol. 164: 1009-1020 [Abstract] [Full Text]  
• Luke, M. R., Kjer-Nielsen, L., Brown, D. L., Stow, J. L., Gleeson, P. A. (2003). GRIP Domain-mediated Targeting of Two New Coiled-coil Proteins, GCC88 and GCC185, to Subcompartments of the trans-Golgi Network. J. Biol. Chem. 278: 4216-4226 [Abstract] [Full Text]  
• Diao, A., Rahman, D., Pappin, D. J.C., Lucocq, J., Lowe, M. (2003). The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation. J. Cell Biol. 160: 201-212 [Abstract] [Full Text]  
• Seemann, J., Pypaert, M., Taguchi, T., Malsam, J., Warren, G. (2002). Partitioning of the Matrix Fraction of the Golgi Apparatus During Mitosis in Animal Cells. Science 295: 848-851 [Abstract] [Full Text]  

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