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Nat Cell Biol. 2012 Aug;14(8):874-81. doi: 10.1038/ncb2533. Epub 2012 Jul 1.

External push and internal pull forces recruit curvature-sensing N-BAR domain proteins to the plasma membrane.

Author information

1
Department of Chemical and Systems Biology, Stanford University, 318 Campus Drive, Clark Building W200, Stanford, California 94305, USA. milos@stanford.edu

Abstract

Many of the more than 20 mammalian proteins with N-BAR domains control cell architecture and endocytosis by associating with curved sections of the plasma membrane. It is not well understood whether N-BAR proteins are recruited directly by processes that mechanically curve the plasma membrane or indirectly by plasma-membrane-associated adaptor proteins that recruit proteins with N-BAR domains that then induce membrane curvature. Here, we show that externally induced inward deformation of the plasma membrane by cone-shaped nanostructures (nanocones) and internally induced inward deformation by contracting actin cables both trigger recruitment of isolated N-BAR domains to the curved plasma membrane. Markedly, live-cell imaging in adherent cells showed selective recruitment of full-length N-BAR proteins and isolated N-BAR domains to plasma membrane sub-regions above nanocone stripes. Electron microscopy confirmed that N-BAR domains are recruited to local membrane sites curved by nanocones. We further showed that N-BAR domains are periodically recruited to curved plasma membrane sites during local lamellipodia retraction in the front of migrating cells. Recruitment required myosin-II-generated force applied to plasma-membrane-connected actin cables. Together, our results show that N-BAR domains can be directly recruited to the plasma membrane by external push or internal pull forces that locally curve the plasma membrane.

PMID:
22750946
PMCID:
PMC3519285
DOI:
10.1038/ncb2533
[Indexed for MEDLINE]
Free PMC Article

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