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First published online June 20, 2006

Journal of Cell Science 119, 1302e (2006)
© The Company of Biologists Limited
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In this issue

Tuba ruffles cells


Figure 1

Scaffolding proteins, such as Tuba, help to coordinate cellular processes by bringing together proteins that need to interact. Frank Gertler and co-authors now suggest that Tuba helps to assemble the molecular machinery needed for certain cytoskeletal rearrangements dependent on N-WASP (see p. 2715). N-WASP, a member of the Wiskott-Aldrich syndrome protein family that regulates actin nucleation, binds to a C-terminal SH3 domain in Tuba. Other domains in Tuba include a GTPase exchange factor (GEF) domain specific for the Rho-family GTPase Cdc42 (which activates N-WASP), a BAR domain (which senses/induces membrane curvature), and several N-terminal SH3 domains that bind dynamin 1 (a GTPase involved in vesicle trafficking). The authors report that overexpression of a Tuba isoform that lacks dynamin-1-binding domains stimulates membrane ruffling in human melanoma cells by interacting with N-WASP and other actin-regulatory proteins; knocking down this isoform by RNAi inhibits the invasive behaviour of these cells. Given these results, the authors conclude that Tuba coordinates signalling and trafficking pathways with cytoskeletal rearrangements during ruffling and other motility processes.


Related articles in JCS:

Tuba stimulates intracellular N-WASP-dependent actin assembly
Eva M. Kovacs, Robert S. Makar, and Frank B. Gertler
JCS 2006 119: 2715-2726. [Abstract] [Full Text]  




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