Dynamin at the actin-membrane interface.
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.
Orth
James D
JD
Department of Biochemistry and Molecular Biology and the Center for Basic Research in Digestive Diseases, Mayo Clinic and Foundation, Rochester, MN 55905, USA.
McNiven
Mark A
MA
D008841:Actin Cytoskeleton / Q000378:metabolism* / Q000648:ultrastructure; D000818:Animals; D048429:Cell Size / Q000502:physiology; D022081:Cell Surface Extensions / Q000378:metabolism* / Q000648:ultrastructure; D034281:Dynamins / Q000378:metabolism* / Q000648:ultrastructure; D005057:Eukaryotic Cells / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D008840:Microfilament Proteins / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000502:physiology
D008840:Microfilament Proteins; D034281:Dynamins