A phosphoinositide-binding cluster in cavin1 acts as a molecular sensor for cavin1 degradation

Tillu, Vikas A., Kovtun, Oleksiy, McMahon, Kerrie-Ann, Collins, Brett M. and Parton, Robert G. (2015) A phosphoinositide-binding cluster in cavin1 acts as a molecular sensor for cavin1 degradation. Molecular Biology of the Cell, 26 20: 3561-3569. doi:10.1091/mbc.E15-06-0359

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Author Tillu, Vikas A.
Kovtun, Oleksiy
McMahon, Kerrie-Ann
Collins, Brett M.
Parton, Robert G.
Title A phosphoinositide-binding cluster in cavin1 acts as a molecular sensor for cavin1 degradation
Journal name Molecular Biology of the Cell   Check publisher's open access policy
ISSN 1939-4586
1059-1524
Publication date 2015-10-15
Sub-type Article (original research)
DOI 10.1091/mbc.E15-06-0359
Open Access Status File (Publisher version)
Volume 26
Issue 20
Start page 3561
End page 3569
Total pages 9
Place of publication Bethesda, MD, United States
Publisher American Society for Cell Biology
Collection year 2016
Language eng
Abstract Caveolae are abundant surface organelles implicated in a range of cellular processes. Two classes of proteins work together to generate caveolae: integral membrane proteins termed caveolins and cytoplasmic coat proteins called cavins. Caveolae respond to membrane stress by releasing cavins into the cytosol. A crucial aspect of this model is tight regulation of cytosolic pools of cavin under resting conditions. We now show that a recently identified region of cavin1 that can bind phosphoinositide (PI) lipids is also a major site of ubiquitylation. Ubiquitylation of lysines within this site leads to rapid proteasomal degradation. In cells that lack caveolins and caveolae, cavin1 is cytosolic and rapidly degraded as compared with cells in which cavin1 is associated with caveolae. Membrane stretching causes caveolar disassembly, release of cavin complexes into the cytosol, and increased proteasomal degradation of wild-type cavin1 but not mutant cavin1 lacking the major ubiquitylation site. Release of cavin1 from caveolae thus leads to exposure of key lysine residues in the PI-binding region, acting as a trigger for cavin1 ubiquitylation and down-regulation. This mutually exclusive PI-binding/ubiquitylation mechanism may help maintain low levels of cytosolic cavin1 in resting cells, a prerequisite for cavins acting as signaling modules following release from caveolae.
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Q-Index Status Confirmed Code
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Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
Institute for Molecular Bioscience - Publications
Centre for Microscopy and Microanalysis Publications
 
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