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Actin' roles in endocytosis

Reorganization of the actin cytoskeleton is thought to play an important role in endocytosis, but the precise role of actin rearrangements and the specific actin-associated proteins involved have remained obscure. Kathryn Ayscough and co-workers now implicate two budding yeast proteins in the process: Sla1p, an adaptor that binds to the yeast homologue of the actin regulator Wiskott-Aldrich syndrome protein (WASP); and Sla2p, a yeast homologue of huntingtin-interacting protein (HIP1) that localizes to clathrin-coated pits (seep. 2551). The authors show that Sla1p and Sla2p interact in vitro, map the regions of the proteins responsible and demonstrate that the two proteins exist as a complex in vivo. They also show that sla1 and sla2 mutations impair endocytosis and that a truncated Slap1p construct containing the Slap2-interacting region inhibits both endocytosis and subsequent vesicle trafficking.

Interestingly, Ayscough and co-workers find that the proteins have opposing effects on actin dynamics, using the actin-disrupting drug latrunculin A to show that Sla1p destabilizes F-actin whereas Sla2p stabilizes it. They therefore propose that Sla1p and Sla2p facilitate cycles of actin assembly and disassembly required for reorganization of the cytoskeleton during endocytosis.

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Related articles in JCS:

An interaction between Sla1p and Sla2p plays a role in regulating actin dynamics and endocytosis in budding yeast

Campbell W. Gourlay, Hilary Dewar, Derek T. Warren, Rosaria Costa, Nilima Satish, and Kathryn R. Ayscough
JCS 2003 116: 2551-2564. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?