Structural basis of membrane bending by the N-BAR protein endophilin

Carsten Mim, Haosheng Cui, Joseph A. Gawronski-Salerno, Adam Frost, Edward Lyman, Gregory A. Voth, Vinzenz M. Unger*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

157 Scopus citations

Abstract

Functioning as key players in cellular regulation of membrane curvature, BAR domain proteins bend bilayers and recruit interaction partners through poorly understood mechanisms. Using electron cryomicroscopy, we present reconstructions of full-length endophilin and its N-terminal N-BAR domain in their membrane-bound state. Endophilin lattices expose large areas of membrane surface and are held together by promiscuous interactions between endophilin's amphipathic N-terminal helices. Coarse-grained molecular dynamics simulations reveal that endophilin lattices are highly dynamic and that the N-terminal helices are required for formation of a stable and regular scaffold. Furthermore, endophilin accommodates different curvatures through a quantized addition or removal of endophilin dimers, which in some cases causes dimerization of endophilin's SH3 domains, suggesting that the spatial presentation of SH3 domains, rather than affinity, governs the recruitment of downstream interaction partners.

Original languageEnglish (US)
Pages (from-to)137-145
Number of pages9
JournalCell
Volume149
Issue number1
DOIs
StatePublished - Mar 30 2012

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Fingerprint Dive into the research topics of 'Structural basis of membrane bending by the N-BAR protein endophilin'. Together they form a unique fingerprint.

Cite this