Dynamin at the actin-membrane interface

James D. Orth, Mark A. McNiven

Research output: Contribution to journalReview article

202 Scopus citations

Abstract

Many important cellular processes such as phagocytosis, cell motility and endocytosis require the participation of a dynamic and interactive actin cytoskeleton that acts to deform cellular membranes. The extensive family of non-traditional myosins has been implicated in linking the cortical actin gel with the plasma membrane. Recently, however, the dynamins have also been included in these cell processes as a second family of mechanochemical enzymes that self-associate and hydrolyze nucleotides to perform 'work' while linking cellular membranes to the actin cytoskeleton. The dynamins are believed to form large helical polymers from which extend many interactive proline-rich tail domains, and these domains bind to a variety of SH3-domain-containing proteins, many of which appear to be actin-binding proteins. Recent data support the concept that the dynamin family might act as a 'polymeric contractile scaffold' at the interface between biological membranes and filamentous actin.

Original languageEnglish (US)
Pages (from-to)31-39
Number of pages9
JournalCurrent Opinion in Cell Biology
Volume15
Issue number1
DOIs
StatePublished - Feb 2002

ASJC Scopus subject areas

  • Cell Biology

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