Vps26B-retromer negatively regulates plasma membrane resensitization of PAR-2

Bugarcic, Andrea, Vetter, Irina, Chalmers, Silke, Kinna, Genevieve, Collins, Brett M. and Teasdale, Rohan D. (2015) Vps26B-retromer negatively regulates plasma membrane resensitization of PAR-2. Cell Biology International, 39 11: 1299-1306. doi:10.1002/cbin.10508

Author Bugarcic, Andrea
Vetter, Irina
Chalmers, Silke
Kinna, Genevieve
Collins, Brett M.
Teasdale, Rohan D.
Title Vps26B-retromer negatively regulates plasma membrane resensitization of PAR-2
Journal name Cell Biology International   Check publisher's open access policy
ISSN 1095-8355
Publication date 2015-11-01
Year available 2015
Sub-type Article (original research)
DOI 10.1002/cbin.10508
Open Access Status Not yet assessed
Volume 39
Issue 11
Start page 1299
End page 1306
Total pages 8
Place of publication Oxford, United Kingdom
Publisher John Wiley & Sons
Collection year 2016
Language eng
Abstract Retromer is a trimeric complex composed of Vps26, Vps29, and Vps35 and has been shown to be involved in trafficking and sorting of transmembrane proteins within the endosome. The Vps26 paralog, Vps26B, defines a distinct retromer complex (Vps26B-retromer) in vivo and in vitro. Although endosomally associated, Vps26B-retromer does not bind the established retromer transmembrane cargo protein, cation-independent mannose 6-phosphate receptor (CI-M6PR), indicating it has a distinct role to retromer containing the Vps26A paralog. In the present study we use the previously established Vps26B-expressing HEK293 cell model to address the role of Vps26B-retromer in trafficking of the protease activated G-protein coupled receptor PAR-2 to the plasma membrane. In these cells there is no apparent defect in the initial activation of the receptor, as evidenced by release of intracellular calcium, ERK1/2 signaling and endocytosis of activated receptor PAR-2 into degradative organelles. However, we observe a significant delay in plasma membrane repopulation of the protease activated G protein-coupled receptor PAR-2 following stimulation, resulting in a defect in PAR-2 activation after resensitization. Here we propose that PAR-2 plasma membrane repopulation is regulated by Vps26B-retromer, describing a potential novel role for this complex.
Keyword Endosome
Protein trafficking
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
Institute for Molecular Bioscience - Publications
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