Small GTP-binding Protein TC10 Differentially Regulates Two Distinct Populations of Filamentous Actin in 3T3L1 Adipocytes
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- Makoto Kanzaki
- Department of Physiology and Biophysics, The University of Iowa, Iowa City, Iowa 52242; and
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- Robert T. Watson
- Department of Physiology and Biophysics, The University of Iowa, Iowa City, Iowa 52242; and
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- June Chunqiu Hou
- Department of Physiology and Biophysics, The University of Iowa, Iowa City, Iowa 52242; and
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- Mark Stamnes
- Department of Physiology and Biophysics, The University of Iowa, Iowa City, Iowa 52242; and
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- Alan R. Saltiel
- Departments of Internal Medicine and Physiology, Life Sciences Institute, The University of Michigan Medical Center, Ann Arbor, Michigan 48109
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- Jeffrey E. Pessin
- Department of Physiology and Biophysics, The University of Iowa, Iowa City, Iowa 52242; and
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- David Drubin
- editor
抄録
<jats:p>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 (ΔN-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/ΔVCA) 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.</jats:p>
収録刊行物
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- Molecular Biology of the Cell
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Molecular Biology of the Cell 13 (7), 2334-2346, 2002-07
American Society for Cell Biology (ASCB)
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詳細情報 詳細情報について
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- CRID
- 1363670320094523392
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- NII論文ID
- 30018378227
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- ISSN
- 19394586
- 10591524
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