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PMID: 16236792 Published · ppublish English Journal Article Research Support, N.I.H., Extramural

GMx33 associates with the trans-Golgi matrix in a dynamic manner and sorts within tubules exiting the Golgi.

Molecular biology of the cell ·Vol. 17 ·No. 1 ·2006-01-00 ·Pages 511-24

Snyder CM, Mardones GA, Ladinsky MS, Howell KE

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 GTPgammaS, 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.

MeSH Terms
Adenosine Triphosphate/pharmacology Animals Carrier Proteins/genetics,metabolism Cell Line Cytosol/drug effects,metabolism Guanosine Triphosphate/pharmacology Intracellular Membranes/metabolism Microscopy, Immunoelectron Phenotype Protein Binding Protein Transport Rats Recombinant Fusion Proteins/genetics,metabolism Time Factors trans-Golgi Network/drug effects,metabolism,ultrastructure
Chemicals
Carrier Proteins GMx33alpha protein, rat Recombinant Fusion Proteins Guanosine Triphosphate Adenosine Triphosphate
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Snyder Christopher M
Department of Cell and Developmental Biology, University of Colorado School of Medicine, Aurora, CO 80045, USA.
Mardones Gonzalo A
Ladinsky Mark S
Howell Kathryn E
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Article Info
Journal
Molecular biology of the cell
Abbr.
Mol Biol Cell
ISSN
1059-1524
Published
2006-01-00
Epub
2005-00-19
Pages
511-24
Language
English
Region
United States
NLM ID
9201390
PMCID
PMC1345686
Subset
IM
Grants
NIGMS NIH HHS · R01 GM042629 · United States
NIGMS NIH HHS · P01 GM061306 · United States
NIGMS NIH HHS · F32 GM072236 · United States
NIGMS NIH HHS · F32 GM072236-01 · United States
NIGMS NIH HHS · GM61306 · United States
NIGMS NIH HHS · GM42629 · United States
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