Umeå University's logo

umu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Membrane insertion mechanism of the caveola coat protein Cavin1
Umeå University, Faculty of Medicine, Department of Integrative Medical Biology (IMB).
Umeå University, Faculty of Medicine, Department of Integrative Medical Biology (IMB). Umeå University, Faculty of Medicine, Department of Clinical Microbiology. Umeå University, Faculty of Medicine, Wallenberg Centre for Molecular Medicine at Umeå University (WCMM).ORCID iD: 0000-0001-5116-2577
Umeå University, Faculty of Medicine, Department of Integrative Medical Biology (IMB). Umeå University, Faculty of Medicine, Department of Medical Biosciences, Medical and Clinical Genetics. Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
Department of Pharmacy, Uppsala Biomedical Center, Uppsala University, Uppsala, Sweden.
Show others and affiliations
2022 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 119, no 25, article id 2202295119Article in journal (Refereed) Published
Abstract [en]

Caveolae are small plasma membrane invaginations, important for control of membrane tension, signaling cascades, and lipid sorting. The caveola coat protein Cavin1 is essential for shaping such high curvature membrane structures. Yet, a mechanistic understanding of how Cavin1 assembles at the membrane interface is lacking. Here, we used model membranes combined with biophysical dissection and computational modeling to show that Cavin1 inserts into membranes. We establish that initial phosphatidylinositol (4, 5) bisphosphate [PI(4,5)P2]-dependent membrane adsorption of the trimeric helical region 1 (HR1) of Cavin1 mediates the subsequent partial separation and membrane insertion of the individual helices. Insertion kinetics of HR1 is further enhanced by the presence of flanking negatively charged disordered regions, which was found important for the coassembly of Cavin1 with Caveolin1 in living cells. We propose that this intricate mechanism potentiates membrane curvature generation and facilitates dynamic rounds of assembly and disassembly of Cavin1 at the membrane.

Place, publisher, year, edition, pages
Proceedings of the National Academy of Sciences , 2022. Vol. 119, no 25, article id 2202295119
Keywords [en]
caveolae, Cavin1, membrane curvature, membrane-shaping protein, protein-lipid interactions
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-203198DOI: 10.1073/pnas.2202295119ISI: 000838706900008Scopus ID: 2-s2.0-85133725056OAI: oai:DiVA.org:umu-203198DiVA, id: diva2:1728397
Funder
Swedish Research Council, 2018-05973European CommissionThe Kempe FoundationsSwedish Cancer SocietyWallenberg FoundationsAvailable from: 2023-01-18 Created: 2023-01-18 Last updated: 2023-01-18Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textScopus

Authority records

Liu, Kang-ChengPace, HudsonLarsson, ElinShukla, AnkitaMohan, JaganBally, MartaHubert, MadlenLundmark, Richard

Search in DiVA

By author/editor
Liu, Kang-ChengPace, HudsonLarsson, ElinShukla, AnkitaMohan, JaganBally, MartaHubert, MadlenLundmark, Richard
By organisation
Department of Integrative Medical Biology (IMB)Department of Clinical MicrobiologyWallenberg Centre for Molecular Medicine at Umeå University (WCMM)Medical and Clinical GeneticsDepartment of Medical Biochemistry and BiophysicsUmeå Centre for Microbial Research (UCMR)Molecular Infection Medicine Sweden (MIMS)
In the same journal
Proceedings of the National Academy of Sciences of the United States of America
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 133 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf