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Harnessing actin dynamics for clathrin-mediated endocytosis. Nat Rev Mol Cell Biol 7:404-414

Department of Molecular and Cell Biology, University of California, Berkeley, California 94720-3202, USA.
Nature Reviews Molecular Cell Biology (Impact Factor: 36.46). 07/2006; 7(6):404-14. DOI: 10.1038/nrm1940
Source: PubMed

ABSTRACT Actin polymerization often occurs at the plasma membrane to drive the protrusion of lamellipodia and filopodia at the leading edge of migrating cells. A role for actin polymerization in another cellular process that involves the reshaping of the plasma membrane--namely endocytosis--has recently been established. Live-cell imaging studies are shedding light on the order and timing of the molecular events and mechanisms of actin function during endocytosis.

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Available from: Christopher Pierre Toret, Aug 27, 2015
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    • "Actin filament assembly can generate mechanical forces to induce membrane deformation (Kaksonen et al., 2006) and to facilitate vesicle trafficking, providing a platform to affect receptor turnover (Zech et al., 2012). It is not clear whether formins being the largest group of actin nucleation and assembly factors play a role in integrin traffic and function. "
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    • "Although actin is dispensable for the process of endocytosis in higher eukaryotes, several studies have indicated an important regulatory role for actin in integrin endosomal traffic particularly on endosomes. Actin-related protein (Arp)2/3, a multiprotein complex and actin nucleator, promotes the assembly of branched F-actin networks at the plasma membrane and on endosomes (Goley and Welch, 2006; Kaksonen et al., 2006). Activation of Arp2/3 is mediated by nucleation-promoting factors such as members of the Wiskott– Aldrich syndrome protein (WASP) family, all of which function in distinct subcellular locations (reviewed in Takenawa and Suetsugu, 2007). "
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    • "Although girdin was reported to be a component of a protein complex that included dynamin (Simpson et al, 2005), the role of girdin in CME has not been investigated. Also, our previous finding that girdin colocalizes with submembranous actin network (Enomoto et al, 2005), which possess critical roles in CME (Kaksonen et al, 2006), led to the idea of girdin's involvement in CME. "
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