QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Vol. 17, Issue 1, 511-524, January 2006

This Article Full Text Full Text (PDF) Supplemental Material All Versions of this Article: E05-07-0682v1 17/1/511    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Snyder, C. M. Articles by Howell, K. E. Search for Related Content PubMed PubMed Citation Articles by Snyder, C. M. Articles by Howell, K. E.

GMx33 Associates with the Trans-Golgi Matrix in a Dynamic Manner and Sorts within Tubules Exiting the Golgi

Christopher M. Snyder ^*, Gonzalo A. Mardones , Mark S. Ladinsky , and Kathryn E. Howell

Department of Cell and Developmental Biology, University of Colorado School of Medicine, Aurora, CO 80045

Submitted July 28, 2005; Accepted October 12, 2005
Monitoring Editor: Sean Munro

The trans-Golgi matrix consists of a group of proteins dynamically associated with the trans-Golgi and thought to be involved in anterograde and retrograde Golgi traffic, as well as interactions with the cytoskeleton and maintenance of the Golgi structure. GMx33 is localized to the cytoplasmic face of the trans-Golgi and is also present in a large cytoplasmic pool. Here we demonstrate that GMx33 is dynamically associated with the trans-Golgi matrix, associating and dissociating with the Golgi in seconds. GMx33 can be locked onto the trans-Golgi matrix by GTPS, indicating that its association is regulated in a GTP-dependent manner like several other Golgi matrix proteins. Using live-cell imaging we show that GMx33 exits the Golgi associated with tubules and within these tubules GMx33 segregates from transmembrane proteins followed by fragmentation of the tubules into smaller tubules and vesicles. Within vesicles produced by an in vitro budding reaction, GMx33 remains segregated in a matrixlike tail region that sometimes contains Golgin-245. This trans-matrix often links a few vesicles together. Together these data suggest that GMx33 is a member of the trans-Golgi matrix and offer clues regarding the role of the trans-Golgi matrix in sorting and exit from the Golgi.

The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

^* Present address: Department of Molecular Microbiology and Immunology, Oregon Health and Science University, Portland, OR 97239

Present address: Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892

Present address: Boulder Laboratory for 3D Electron Microscopy of Cells, Department of MCD Biology, University of Colorado, Boulder, CO 80309.

Address correspondence to: Kathryn E. Howell (kathryn.howell{at}uchsc.edu).

This article has been cited by other articles:

				L. Tu, W. C. S. Tai, L. Chen, and D. K. Banfield Signal-Mediated Dynamic Retention of Glycosyltransferases in the Golgi Science, July 18, 2008; 321(5887): 404 - 407. [Abstract] [Full Text] [PDF]

				Z. G. Holloway, R. Grabski, T. Szul, M. L. Styers, J. A. Coventry, A. P. Monaco, and E. Sztul Activation of ADP-ribosylation factor regulates biogenesis of the ATP7A-containing trans-Golgi network compartment and its Cu-induced trafficking Am J Physiol Cell Physiol, December 1, 2007; 293(6): C1753 - C1767. [Abstract] [Full Text] [PDF]