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Dev Cell. 2009 Dec;17(6):811-22. doi: 10.1016/j.devcel.2009.11.005.

Coordinated actions of actin and BAR proteins upstream of dynamin at endocytic clathrin-coated pits.

Author information

  • 1Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510, USA.

Erratum in

  • Dev Cell. 2010 Feb 16;18(2):332. Ferguson, Shawn [corrected to Ferguson, Shawn M].

Abstract

The GTPase dynamin, a key player in endocytic membrane fission, interacts with numerous proteins that regulate actin dynamics and generate/sense membrane curvature. To determine the functional relationship between these proteins and dynamin, we have analyzed endocytic intermediates that accumulate in cells that lack dynamin (derived from dynamin 1 and 2 double conditional knockout mice). In these cells, actin-nucleating proteins, actin, and BAR domain proteins accumulate at the base of arrested endocytic clathrin-coated pits, where they support the growth of dynamic long tubular necks. These results, which we show reflect the sequence of events in wild-type cells, demonstrate a concerted action of these proteins prior to, and independent of, dynamin and emphasize similarities between clathrin-mediated endocytosis in yeast and higher eukaryotes. Our data also demonstrate that the relationship between dynamin and actin is intimately connected to dynamin's endocytic role and that dynamin terminates a powerful actin- and BAR protein-dependent tubulating activity.

2009 Elsevier Inc. All rights reserved.

PMID:
20059951
[PubMed - indexed for MEDLINE]
PMCID:
PMC2861561
Free PMC Article

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