Document Detail

p125 is localized in endoplasmic reticulum exit sites and involved in their organization.
MedLine Citation:
PMID:  15623529     Owner:  NLM     Status:  MEDLINE    
Transport vesicles coated with the COPII complex, which is assembled from Sar1p, Sec23p-Sec24p, and Sec13p-Sec31p, are involved in protein export from the endoplasmic reticulum (ER). We previously identified and characterized a novel Sec23p-interacting protein, p125, that is only expressed in mammals and exhibits sequence homology with phosphatidic acid-preferring phospholipase A(1) (PA-PLA(1)). In this study, we examined the localization and function of p125 in detail. By using immunofluorescence and electron microscopy, we found that p125 is principally localized in ER exit sites where COPII-coated vesicles are produced. Analyses of chimeric proteins comprising p125 and two other members of the mammalian PA-PLA(1) family (PA-PLA(1) and KIAA0725p) showed that, for localization to ER exit sites, the p125-specific N-terminal region is critical, and the putative lipase domain is interchangeable with KIAA0725p but not with PA-PLA(1). RNA interference-mediated depletion of p125 affected the organization of ER exit sites. The structure of the cis-Golgi compartment was also substantially disturbed, whereas the medial-Golgi was not. Protein export from the ER occurred without a significant delay in p125-depleted cells. Our study suggests that p125 is a mammalian-specific component of ER exit sites and participates in the organization of this compartment.
Wakako Shimoi; Ichiko Ezawa; Koji Nakamoto; Shihoko Uesaki; Gavin Gabreski; Meir Aridor; Akitsugu Yamamoto; Masami Nagahama; Mitsuo Tagaya; Katsuko Tani
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2004-12-28
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  280     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2005 Mar 
Date Detail:
Created Date:  2005-03-14     Completed Date:  2005-04-25     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  10141-8     Citation Subset:  IM    
School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan.
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MeSH Terms
Binding Sites
Biological Transport
Carrier Proteins / biosynthesis*,  metabolism,  physiology*
Cell Line
Cell Membrane / metabolism
DNA, Complementary / metabolism
Electrophoresis, Polyacrylamide Gel
Endoplasmic Reticulum / metabolism*,  ultrastructure
Golgi Apparatus / metabolism,  ultrastructure
Hela Cells
Intracellular Membranes / metabolism
Membrane Proteins / metabolism
Microscopy, Confocal
Microscopy, Electron
Microscopy, Fluorescence
Microscopy, Immunoelectron
Monomeric GTP-Binding Proteins / metabolism
Nuclear Pore Complex Proteins
Phosphoproteins / metabolism
Plasmids / metabolism
Protein Binding
Protein Structure, Tertiary
Proteins / metabolism
Recombinant Fusion Proteins / metabolism
Saccharomyces cerevisiae Proteins / metabolism
Time Factors
Vesicular Transport Proteins / metabolism
Reg. No./Substance:
0/Carrier Proteins; 0/DNA, Complementary; 0/Membrane Proteins; 0/Nuclear Pore Complex Proteins; 0/Phosphoproteins; 0/Proteins; 0/Recombinant Fusion Proteins; 0/SEC13 protein, S cerevisiae; 0/SEC23A protein, human; 0/SEC23IP protein, human; 0/SEC24 protein, S cerevisiae; 0/SEC31 protein, S cerevisiae; 0/Saccharomyces cerevisiae Proteins; 0/Sec23a protein, rat; 0/Vesicular Transport Proteins; EC 3.6.1.-/SAR1A protein, human; EC 3.6.1.-/SAR1B protein, human; EC GTP-Binding Proteins

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