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A more recent version of this article appeared on July 1, 2002
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Submitted on October 10, 2001
Revised on March 6, 2002
Accepted on March 28, 2002
1 Department of Physiology and Biophysics, The University of Iowa, Iowa City, IA 52242, USA
2 Departments of Internal Medicine and Physiology, Life Sciences Institute, The University of Michigan Medical Center, Ann Arbor, MI 48109
* Corresponding author. E-mail address: Jeffrey-Pessin{at}uiowa.edu.
TC10 is a member of the Rho family of small GTP binding proteins that has been implicated in the regulation of insulin-stimulated GLUT4 translocation in adipocytes (Chiang et al. (2001) Nature 410, 944-948). 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 peri-nuclear region when expressed in 3T3L1 adipocytes. In contrast, expression of TC10/Q75L completely disrupted adipocyte cortical actin which was specific for TC10 as expression of constitutively active Cdc42 was without effect. The effect of TC10/Q75L to disrupt cortical actin was abrogated following deletion of the amino terminal extension (
N-TC10/Q75L) whereas this deletion retained the ability to induce peri-nuclear actin polymerization. In addition, alteration of peri-nuclear 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.
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