GMx33 Associates with the Trans-Golgi Matrix in a Dynamic Manner and Sorts within Tubules Exiting the Golgi
Abstract
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 GTPγS, 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.
Additional Information
© 2005 by The American Society for Cell Biology. Submitted July 28, 2005; Accepted October 12, 2005. This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E05–07–0682) on October 19, 2005. We thank Francis Barr, John Bergeron, Alfonso Gonzalez, and Elizabeth Sztul for kindly providing antibodies. The live cell imaging and photobleachingwas carried out at the UCHSC Light Microscopy Facility, and we thank Steven Fadul for his help. We also thank Rytis Prekeris for the use of the Zeiss Axiovert 200. This work was supported by Grants GM42629 and PO1 GM61306 from the National Institutes of Health, awarded to K.E.H. and a postdoctoral fellowship from the NIH, F32 GM072236-01, awarded to C.M.S.Attached Files
Published - mbc.e05-07-0682.pdf
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Additional details
- PMCID
- PMC1345686
- Eprint ID
- 99681
- Resolver ID
- CaltechAUTHORS:20191105-155146398
- GM42629
- NIH
- PO1 GM61306
- NIH
- F32 GM072236-01
- NIH Postdoctoral Fellowship
- Created
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2019-11-06Created from EPrint's datestamp field
- Updated
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2021-11-16Created from EPrint's last_modified field