Annexin A4 and A6 induce membrane curvature and constriction during cell membrane repair
Theresa Louise Boye,
Kenji Maeda,
Weria Pezeshkian,
Stine Lauritzen Sønder,
Swantje Christin Haeger,
Volker Gerke,
Adam Cohen Simonsen and
Jesper Nylandsted ()
Additional contact information
Theresa Louise Boye: Danish Cancer Society Research Center
Kenji Maeda: Danish Cancer Society Research Center
Weria Pezeshkian: University of Southern Denmark
Stine Lauritzen Sønder: Danish Cancer Society Research Center
Swantje Christin Haeger: Danish Cancer Society Research Center
Volker Gerke: University of Münster
Adam Cohen Simonsen: University of Southern Denmark
Jesper Nylandsted: Danish Cancer Society Research Center
Nature Communications, 2017, vol. 8, issue 1, 1-11
Abstract:
Abstract Efficient cell membrane repair mechanisms are essential for maintaining membrane integrity and thus for cell life. Here we show that the Ca2+- and phospholipid-binding proteins annexin A4 and A6 are involved in plasma membrane repair and needed for rapid closure of micron-size holes. We demonstrate that annexin A4 binds to artificial membranes and generates curvature force initiated from free edges, whereas annexin A6 induces constriction force. In cells, plasma membrane injury and Ca2+ influx recruit annexin A4 to the vicinity of membrane wound edges where its homo-trimerization leads to membrane curvature near the edges. We propose that curvature force is utilized together with annexin A6-mediated constriction force to pull the wound edges together for eventual fusion. We show that annexin A4 can counteract various plasma membrane disruptions including holes of several micrometers indicating that induction of curvature force around wound edges is an early key event in cell membrane repair.
Date: 2017
References: Add references at CitEc
Citations: View citations in EconPapers (1)
Downloads: (external link)
https://www.nature.com/articles/s41467-017-01743-6 Abstract (text/html)
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01743-6
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/s41467-017-01743-6
Access Statistics for this article
Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie
More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().