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  Cytoskeletal Pinning Controls Phase Separation in Multicomponent Lipid Membranes

Arumugam, S., Petrov, E. P., & Schwille, P. (2015). Cytoskeletal Pinning Controls Phase Separation in Multicomponent Lipid Membranes. Biophysical Journal, 108(5), 1104-1113. doi:10.1016/j.bpj.2014.12.050.

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 Creators:
Arumugam, Senthil1, Author
Petrov, Eugene P.2, Author           
Schwille, Petra2, Author           
Affiliations:
1external, ou_persistent22              
2Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565169              

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Free keywords: CRITICAL FLUCTUATIONS; MODEL MEMBRANES; CELL-MEMBRANES; FTSZ; VESICLES; BILAYERS; ACTIN; TRANSITION; PROTEINS; DOMAINS
 Abstract: We study the effect of a minimal cytoskeletal network formed on the surface of giant unilamellar vesicles by the prokaryotic tubulin homolog, FtsZ, on phase separation in freestanding lipid membranes. FtsZ has been modified to interact with the membrane through a membrane targeting sequence from the prokaryotic protein MinD. FtsZ with the attached membrane targeting sequence efficiently forms a highly interconnected network on membranes with a concentration-dependent mesh size, much similar to the eukaryotic cytoskeletal network underlying the plasma membrane. Using giant unilamellar vesicles formed from a quaternary lipid mixture, we demonstrate that the artificial membrane-associated cytoskeleton, on the one hand, suppresses large-scale phase separation below the phase transition temperature, and, on the other hand, preserves phase separation above the transition temperature. Our experimental observations support the ideas put forward in our previous simulation study: In particular, the picket fence effect on phase separation may explain why micrometer-scale membrane domains are observed in isolated, cytoskeleton-free giant plasma membrane vesicles, but not in intact cell membranes. The experimentally observed suppression of large-scale phase separation much below the transition temperatures also serves as an argument in favor of the cryoprotective role of the cytoskeleton.

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Language(s): eng - English
 Dates: 2015
 Publication Status: Issued
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000350969000012
DOI: 10.1016/j.bpj.2014.12.050
 Degree: -

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Title: Biophysical Journal
  Other : Biophys. J.
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 108 (5) Sequence Number: - Start / End Page: 1104 - 1113 Identifier: ISSN: 0006-3495
CoNE: https://pure.mpg.de/cone/journals/resource/954925385117