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Vol. 13, Issue 7, 2334-2346, July 2002
and
*Department of Physiology and Biophysics, The University of Iowa,
Iowa City, Iowa 52242; and TC10 is a member of the Rho family of small GTP-binding proteins
that has previously been implicated in the regulation of insulin-stimulated GLUT4 translocation in adipocytes. In a
manner similar to Cdc42-stimulated actin-based motility, we have
observed that constitutively active TC10 (TC10/Q75L) can induce actin
comet tails in Xenopus oocyte extracts in vitro and
extensive actin polymerization in the perinuclear region when expressed
in 3T3L1 adipocytes. In contrast, expression of TC10/Q75L completely
disrupted adipocyte cortical actin, which was specific for TC10,
because expression of constitutively active Cdc42 was without effect. The effect of TC10/Q75L to disrupt cortical actin was abrogated after
deletion of the amino terminal extension (Departments of Internal
Medicine and Physiology, Life Sciences Institute, The University of
Michigan Medical Center, Ann Arbor, Michigan 48109
N-TC10/Q75L), whereas this
deletion retained the ability to induce perinuclear actin
polymerization. In addition, alteration of perinuclear actin by
expression of TC10/Q75L, a dominant-interfering TC10/T31N mutant or a
mutant N-WASP protein (N-WASP/VCA) reduced the rate of VSV G protein
trafficking to the plasma membrane. Furthermore, TC10 directly bound to
Golgi COPI coat proteins through a dilysine motif in the carboxyl
terminal domain consistent with a role for TC10 regulating actin
polymerization on membrane transport vesicles. Together, these data
demonstrate that TC10 can differentially regulate two types of
filamentous actin in adipocytes dependent on distinct functional
domains and its subcellular compartmentalization.
Corresponding author. E-mail address:
jeffrey-pessin{at}uiowa.edu.
Online version of this article
contains video material. Online version is available at
www.molbiolcell.org.
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