Single-molecule analysis reveals self assembly and nanoscale segregation of two distinct cavin subcomplexes on caveolae

Gambin, Yann, Ariotti, Nicholas, McMahon, Kerrie-Ann, Bastiani, Michele, Sierecki, Emma, Kovtun, Oleksiy, Polinkovsky, Mark E., Magenau, Astrid, Jung, WooRam, Okano, Satomi, Zhou, Yong, Leneva, Natalya, Mureev, Sergey, Johnston, Wayne, Gaus, Katharina, Hancock, John F., Collins, Brett M., Alexandrov, Kirill and Parton, Robert G. (2014) Single-molecule analysis reveals self assembly and nanoscale segregation of two distinct cavin subcomplexes on caveolae. eLIFE, 3 e01434.1-e01434.18. doi:10.7554/eLife.01434

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Author Gambin, Yann
Ariotti, Nicholas
McMahon, Kerrie-Ann
Bastiani, Michele
Sierecki, Emma
Kovtun, Oleksiy
Polinkovsky, Mark E.
Magenau, Astrid
Jung, WooRam
Okano, Satomi
Zhou, Yong
Leneva, Natalya
Mureev, Sergey
Johnston, Wayne
Gaus, Katharina
Hancock, John F.
Collins, Brett M.
Alexandrov, Kirill
Parton, Robert G.
Title Single-molecule analysis reveals self assembly and nanoscale segregation of two distinct cavin subcomplexes on caveolae
Journal name eLIFE   Check publisher's open access policy
ISSN 2050-084X
Publication date 2014-01-28
Year available 2014
Sub-type Article (original research)
DOI 10.7554/eLife.01434
Open Access Status DOI
Volume 3
Start page e01434.1
End page e01434.18
Total pages 18
Place of publication Cambridge, United Kingdom
Publisher eLife Sciences Publications
Language eng
Abstract In mammalian cells three closely related cavin proteins cooperate with the scaffolding protein caveolin to form membrane invaginations known as caveolae. Here we have developed a novel single-molecule fluorescence approach to directly observe interactions and stoichiometries in protein complexes from cell extracts and from in vitro synthesized components. We show that up to 50 cavins associate on a caveola. However, rather than forming a single coat complex containing the three cavin family members, single-molecule analysis reveals an exquisite specificity of interactions between cavin1, cavin2 and cavin3. Changes in membrane tension can flatten the caveolae, causing the release of the cavin coat and its disassembly into separate cavin1-cavin2 and cavin1-cavin3 subcomplexes. Each of these subcomplexes contain 9 ± 2 cavin molecules and appear to be the building blocks of the caveolar coat. High resolution immunoelectron microscopy suggests a remarkable nanoscale organization of these separate subcomplexes, forming individual striations on the surface of caveolae.
Keyword Biology
Life Sciences & Biomedicine - Other Topics
Q-Index Code C1
Q-Index Status Confirmed Code
Grant ID FT0991611
APP1025082
569542
511005
DP120101298
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
Institute for Molecular Bioscience - Publications
Centre for Microscopy and Microanalysis Publications
 
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Citation counts: TR Web of Science Citation Count  Cited 31 times in Thomson Reuters Web of Science Article | Citations
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Created: Wed, 05 Mar 2014, 20:39:39 EST by Susan Allen on behalf of Institute for Molecular Bioscience