Evidence map›Paper›PMID 26269585›Full record

ArticleMolecular biology of the cell2015

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

Vikas A Tillu, Oleksiy Kovtun, Kerrie-Ann McMahon, Brett M Collins, Robert G Parton

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 21% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 32 citations in OpenAlex.

  1. Caveolae mechanics in cellular functions and disease.Nature reviews. Molecular cell biology · 2026
    Review
  2. Review
  3. Caveolin assemblies displace one bilayer leaflet to organize and bend membranes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. The Role of Membrane Lipids in the Formation and Function of Caveolae.Cold Spring Harbor perspectives in biology · 2023
    Review
  7. Article
  8. Article
  9. The male germline-specific protein MAPS is indispensable for pachynema progression and fertility.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Article
  11. Review
  12. Article
  13. Caveolae as Potential Hijackable Gates in Cell Communication.Frontiers in cell and developmental biology · 2020
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Vikas A TilluInstitute for Molecular Bioscience, University of Queensland, St. Lucia, Queensland 4072, Australia.
Oleksiy KovtunInstitute for Molecular Bioscience, University of Queensland, St. Lucia, Queensland 4072, Australia.
Kerrie-Ann McMahonInstitute for Molecular Bioscience, University of Queensland, St. Lucia, Queensland 4072, Australia.
Brett M CollinsInstitute for Molecular Bioscience, University of Queensland, St. Lucia, Queensland 4072, Australia.
Robert G PartonInstitute for Molecular Bioscience, University of Queensland, St. Lucia, Queensland 4072, Australia Centre for Microscopy and Microanalysis, University of Queensland, St. Lucia, Queensland 4072, Australia r.parton@imb.uq.edu.au.
The University of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

AnimalsBinding SitesCaveolaeCaveolin 1Cells, CulturedCytoplasmDogsHumansMadin Darby Canine Kidney CellsMCF-7 CellsMembrane ProteinsPhosphatidylinositolsProteasome Endopeptidase ComplexProtein Structure, TertiaryRNA-Binding ProteinsSignal TransductionCaveolin 1CAVIN1 protein, humanCavin1 protein, mouseMembrane ProteinsPhosphatidylinositolsProteasome Endopeptidase ComplexRNA-Binding Proteins

Identifiers

PMID26269585
PMCPMC4603927
OpenAlexW1919756525

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.