메뉴 건너뛰기




Volumn 24, Issue 2, 2004, Pages 651-661

Phosphorylation of Critical Serine Residues in Gem Separates Cytoskeletal Reorganization from Down-Regulation of Calcium Channel Activity

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CHANNEL; CALMODULIN; GEM PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE; PROTEIN CDC42; PROTEIN KINASE; RAD PROTEIN; RAS PROTEIN; REM PROTEIN; REM2 PROTEIN; RGK PROTEIN; RHO KINASE; SERINE; UNCLASSIFIED DRUG;

EID: 0346725954     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.24.2.651-661.2004     Document Type: Article
Times cited : (68)

References (32)
  • 1
    • 0036799215 scopus 로고    scopus 로고
    • A novel Rho GTPase-activating-protein interacts with Gem, a member of the Ras superfamily of GTPases
    • Aresta, S., M. F. de Tand-Heim, F. Beranger, and J. de Gunzburg. 2002. A novel Rho GTPase-activating-protein interacts with Gem, a member of the Ras superfamily of GTPases. Biochem. J. 367:57-65.
    • (2002) Biochem. J. , vol.367 , pp. 57-65
    • Aresta, S.1    De Tand-Heim, M.F.2    Beranger, F.3    De Gunzburg, J.4
  • 4
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H. R., D. A. Sanders, and F. McCormick. 1991. The GTPase superfamily: conserved structure and molecular mechanism. Nature 349:117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 5
    • 0035797892 scopus 로고    scopus 로고
    • Insulin stimulates increased catalytic activity of phosphoinositide-dependent kinase-1 by a phosphorylation-dependent mechanism
    • Chen, H., F. H. Nystrom, L. Q. Dong, Y. Li, S. Song, F. Liu, and M. J. Quon. 2001. Insulin stimulates increased catalytic activity of phosphoinositide-dependent kinase-1 by a phosphorylation-dependent mechanism. Biochemistry 40:11851-11859.
    • (2001) Biochemistry , vol.40 , pp. 11851-11859
    • Chen, H.1    Nystrom, F.H.2    Dong, L.Q.3    Li, Y.4    Song, S.5    Liu, F.6    Quon, M.J.7
  • 6
    • 0033621957 scopus 로고    scopus 로고
    • Atypical protein kinases Cλ and -ζ associate with the GTP-binding protein Cdc42 and mediate stress fiber loss
    • Coghlan, M. P., M. M. Chou, and C. L. Carpenter. 2000. Atypical protein kinases Cλ and -ζ associate with the GTP-binding protein Cdc42 and mediate stress fiber loss. Mol. Cell. Biol. 20:2880-2889.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2880-2889
    • Coghlan, M.P.1    Chou, M.M.2    Carpenter, C.L.3
  • 8
    • 0037222950 scopus 로고    scopus 로고
    • Cell polarity: Par6, aPKC and cytoskeletal crosstalk
    • Etienne-Manneville, S., and A. Hall. 2003. Cell polarity: Par6, aPKC and cytoskeletal crosstalk. Curr. Opin. Cell Biol. 15:67-72.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 67-72
    • Etienne-Manneville, S.1    Hall, A.2
  • 9
    • 0033567121 scopus 로고    scopus 로고
    • Phosphorylation-dependent association of the Ras-related GTP-binding protein Rem with 14-3-3 proteins
    • Finlin, B. S., and D. A. Andres. 1999. Phosphorylation-dependent association of the Ras-related GTP-binding protein Rem with 14-3-3 proteins. Arch. Biochem. Biophys. 368:401-412.
    • (1999) Arch. Biochem. Biophys. , vol.368 , pp. 401-412
    • Finlin, B.S.1    Andres, D.A.2
  • 10
    • 0030803793 scopus 로고    scopus 로고
    • Rem is a new member of the Rad- and Gem/Kir Ras-related GTP-binding protein family repressed by lipopolysaccharide stimulation
    • Finlin, B. S., and D. A. Andres. 1997, Rem is a new member of the Rad- and Gem/Kir Ras-related GTP-binding protein family repressed by lipopolysaccharide stimulation. J. Biol. Chem. 272:21982-21988.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21982-21988
    • Finlin, B.S.1    Andres, D.A.2
  • 11
    • 0034177553 scopus 로고    scopus 로고
    • Rem2, a new member of the Rem/Rad/Gem/Kir family of Ras-related GTPases
    • Finlin, B. S., H. Shao, K. Kadono-Okuda, N. Guo, and D. A. Andres. 2000. Rem2, a new member of the Rem/Rad/Gem/Kir family of Ras-related GTPases. Biochem. J. 347:223-231.
    • (2000) Biochem. J. , vol.347 , pp. 223-231
    • Finlin, B.S.1    Shao, H.2    Kadono-Okuda, K.3    Guo, N.4    Andres, D.A.5
  • 12
    • 0029834335 scopus 로고    scopus 로고
    • Calmodulin binds to and inhibits GTP binding of the ras-like GTPase Kir/Gem
    • Fischer, R., Y. Wei, J. Anagli, and M. W. Berchtold. 1996. Calmodulin binds to and inhibits GTP binding of the ras-like GTPase Kir/Gem. J. Biol. Chem. 271:25067-25070.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25067-25070
    • Fischer, R.1    Wei, Y.2    Anagli, J.3    Berchtold, M.W.4
  • 13
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • Hamill, O. P., A. Marty, E. Neher, B. Sakmann, and F. J. Sigworth. 1981. Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pflugers Arch. 391:85-100.
    • (1981) Pflugers Arch. , vol.391 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2    Neher, E.3    Sakmann, B.4    Sigworth, F.J.5
  • 14
    • 0030629369 scopus 로고    scopus 로고
    • Heterologous expression of receptors and signaling proteins in adult mammalian sympathetic neurons by microinjection
    • Ikeda, S. R. 1997. Heterologous expression of receptors and signaling proteins in adult mammalian sympathetic neurons by microinjection. Methods Mol. Biol. 83:191-202.
    • (1997) Methods Mol. Biol. , vol.83 , pp. 191-202
    • Ikeda, S.R.1
  • 15
    • 0029037183 scopus 로고
    • Heterologous expression of metabotropic glutamate receptors in adult rat sympathetic neurons: Subtype-specific coupling to ion channels
    • Ikeda, S. R., D. M. Lovinger, B. A. McCool, and D. L. Lewis. 1995. Heterologous expression of metabotropic glutamate receptors in adult rat sympathetic neurons: subtype-specific coupling to ion channels., Neuron 14:1029-1038.
    • (1995) Neuron , vol.14 , pp. 1029-1038
    • Ikeda, S.R.1    Lovinger, D.M.2    McCool, B.A.3    Lewis, D.L.4
  • 16
    • 0034967624 scopus 로고    scopus 로고
    • The Gem GTP-binding protein promotes morphological differentiation in neuroblastoma
    • Leone, A., N. Mitsiades, Y. Ward, B. Spinelli, V. Poulaki, M. Tsokos, and K. Kelly. 2001. The Gem GTP-binding protein promotes morphological differentiation in neuroblastoma. Oncogene 20:3217-3225.
    • (2001) Oncogene , vol.20 , pp. 3217-3225
    • Leone, A.1    Mitsiades, N.2    Ward, Y.3    Spinelli, B.4    Poulaki, V.5    Tsokos, M.6    Kelly, K.7
  • 17
  • 18
    • 0042698618 scopus 로고    scopus 로고
    • Two poles and a compass
    • Meili, R., and R. A. Firtel. 2003. Two poles and a compass. Cell 114:153-156.
    • (2003) Cell , vol.114 , pp. 153-156
    • Meili, R.1    Firtel, R.A.2
  • 19
    • 0023766144 scopus 로고
    • A mutation that prevents GTP-dependent activation of the alpha chain of Gs
    • Miller, R. T., S. B. Masters, K. A. Sullivan, B. Beiderman, and H. R. Bourne. 1988. A mutation that prevents GTP-dependent activation of the alpha chain of Gs. Nature 334: 712-715.
    • (1988) Nature , vol.334 , pp. 712-715
    • Miller, R.T.1    Masters, S.B.2    Sullivan, K.A.3    Beiderman, B.4    Bourne, H.R.5
  • 20
    • 0030910312 scopus 로고    scopus 로고
    • Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II
    • Moyers, J. S., P. J. Bilan, J. Zhu, and C. R. Kahn. 1997. Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II. J. Biol. Chem. 272:11832-11839.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11832-11839
    • Moyers, J.S.1    Bilan, P.J.2    Zhu, J.3    Kahn, C.R.4
  • 21
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: Implications for the mechanism of GTP hydrolysis
    • Pai, E. F., U. Krengel, G. A. Petsko, R. S. Goody, W. Kabsch, and A. Wittinghofer. 1990. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9: 2351-2359.
    • (1990) EMBO J. , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Krengel, U.2    Petsko, G.A.3    Goody, R.S.4    Kabsch, W.5    Wittinghofer, A.6
  • 22
    • 0034729198 scopus 로고    scopus 로고
    • Ges, a human GTPase of the Rad/Gem/Kir family, promotes endothelial cell sprouting and cytoskeleton reorganization
    • Pan, J. Y., W. E. Fieles, A. M. White, M. M. Egerton, and D. S. Silberstein. 2000. Ges, a human GTPase of the Rad/Gem/Kir family, promotes endothelial cell sprouting and cytoskeleton reorganization. J. Cell Biol. 149: 1107-1116.
    • (2000) J. Cell Biol. , vol.149 , pp. 1107-1116
    • Pan, J.Y.1    Fieles, W.E.2    White, A.M.3    Egerton, M.M.4    Silberstein, D.S.5
  • 23
    • 0035422395 scopus 로고    scopus 로고
    • The Ras-like GTPase Gem is involved in cell shape remodelling and interacts with the novel kinesin-like protein KIF9
    • Piddini, E., J. A. Schmid, R. de Martin, and C. G. Dotti. 2001. The Ras-like GTPase Gem is involved in cell shape remodelling and interacts with the novel kinesin-like protein KIF9. EMBO J. 20:4076-4087.
    • (2001) EMBO J. , vol.20 , pp. 4076-4087
    • Piddini, E.1    Schmid, J.A.2    De Martin, R.3    Dotti, C.G.4
  • 25
    • 0035793592 scopus 로고    scopus 로고
    • Protein kinase C-zeta phosphorylates insulin receptor substrate-1 and impairs its ability to activate phosphatidylinositol 3-kinase in response to insulin
    • Ravichandran, L. V., D. L. Esposito, J. Chen, and M. J. Quon. 2001. Protein kinase C-zeta phosphorylates insulin receptor substrate-1 and impairs its ability to activate phosphatidylinositol 3-kinase in response to insulin. J. Biol. Chem. 276:3543-3549.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3543-3549
    • Ravichandran, L.V.1    Esposito, D.L.2    Chen, J.3    Quon, M.J.4
  • 26
    • 0027741390 scopus 로고
    • Rad: A member of the Ras family overexpressed in muscle of type II diabetic humans
    • Reynet, C., and C. R. Kahn. 1993. Rad: a member of the Ras family overexpressed in muscle of type II diabetic humans. Science 262:1441-1444.
    • (1993) Science , vol.262 , pp. 1441-1444
    • Reynet, C.1    Kahn, C.R.2
  • 27
    • 0036702196 scopus 로고    scopus 로고
    • Regulating the actin cytoskeleton during vesicular transport
    • Stamnes, M. 2002. Regulating the actin cytoskeleton during vesicular transport. Curr. Opin. Cell Biol. 14:428-433.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 428-433
    • Stamnes, M.1
  • 28
    • 0030810216 scopus 로고    scopus 로고
    • Protein kinase C-zeta as a downstream effector of phosphatidylinositol 3-kinase during insulin stimulation in rat adipocytes. Potential role in glucose transport
    • Standaert, M. L., L. Galloway, P. Karnam, G. Bandyopadhyay, J. Moscat, and R. V. Farese. 1997. Protein kinase C-zeta as a downstream effector of phosphatidylinositol 3-kinase during insulin stimulation in rat adipocytes. Potential role in glucose transport. J. Biol. Chem. 272:30075-30082.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30075-30082
    • Standaert, M.L.1    Galloway, L.2    Karnam, P.3    Bandyopadhyay, G.4    Moscat, J.5    Farese, R.V.6
  • 29
    • 0034128641 scopus 로고    scopus 로고
    • Binding of 14-3-3Β to the carboxyl terminus of Weel increases Weel stability, kinase activity, and G2-M cell population
    • Wang, Y., C. Jacobs, K. E. Hook, H. Duan, R. N. Booher, and Y. Sun. 2000. Binding of 14-3-3Β to the carboxyl terminus of Weel increases Weel stability, kinase activity, and G2-M cell population. Cell Growth Differ. 11:211-219.
    • (2000) Cell Growth Differ. , vol.11 , pp. 211-219
    • Wang, Y.1    Jacobs, C.2    Hook, K.E.3    Duan, H.4    Booher, R.N.5    Sun, Y.6
  • 30
    • 0037092045 scopus 로고    scopus 로고
    • The GTP binding proteins Gem and Rad are negative regulators of the Rho-Rho kinase pathway
    • Ward, Y., S. F. Yap, V. Ravichandran, F. Matsumura, M. Ito, B. Spinelli, and K. Kelly. 2002. The GTP binding proteins Gem and Rad are negative regulators of the Rho-Rho kinase pathway. J. Cell Biol. 157:291-302.
    • (2002) J. Cell Biol. , vol.157 , pp. 291-302
    • Ward, Y.1    Yap, S.F.2    Ravichandran, V.3    Matsumura, F.4    Ito, M.5    Spinelli, B.6    Kelly, K.7
  • 31
    • 0037138389 scopus 로고    scopus 로고
    • How do 14-3-3 proteins work? Gatekeeper phosphorylation and the molecular anvil hypothesis
    • Yaffe, M. B. 2002. How do 14-3-3 proteins work? Gatekeeper phosphorylation and the molecular anvil hypothesis. FEBS Lett. 513:53-57.
    • (2002) FEBS Lett. , vol.513 , pp. 53-57
    • Yaffe, M.B.1
  • 32
    • 0029670787 scopus 로고    scopus 로고
    • Rad, a novel Ras-related GTPase, interacts with skeletal muscle beta-tropomyosin
    • Zhu, J., P. J. Bilan, J. S. Moyers, D. A. Antonetti, and C. R. Kahn. 1996. Rad, a novel Ras-related GTPase, interacts with skeletal muscle beta-tropomyosin. J. Biol. Chem. 271:768-773.
    • (1996) J. Biol. Chem. , vol.271 , pp. 768-773
    • Zhu, J.1    Bilan, P.J.2    Moyers, J.S.3    Antonetti, D.A.4    Kahn, C.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.