메뉴 건너뛰기




Volumn 1-3, Issue , 2003, Pages 547-550

Glycogen Synthase Kinase 3

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84943252440     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012124546-7/50452-6     Document Type: Chapter
Times cited : (2)

References (39)
  • 1
    • 0019026208 scopus 로고
    • Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase
    • N. Embi, D.B. Rylatt and P. Cohen (1980) Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase. Eur. J. Biochem. 107 519-527.
    • (1980) Eur. J. Biochem , vol.107 , pp. 519-527
    • Embi, N.1    Rylatt, D.B.2    Cohen, P.3
  • 2
    • 0025286104 scopus 로고
    • Molecular cloning and expression of glycogen synthase kinase-3/factor A
    • J.R. Woodgett (1990) Molecular cloning and expression of glycogen synthase kinase-3/factor A. EMBO J. 9 2431-2438.
    • (1990) EMBO J , vol.9 , pp. 2431-2438
    • Woodgett, J.R.1
  • 3
    • 0035477020 scopus 로고    scopus 로고
    • GSK3 takes centre stage more than 20 years after its discovery
    • S. Frame and P. Cohen (2001) GSK3 takes centre stage more than 20 years after its discovery. Biochem. J. 359 1-16.
    • (2001) Biochem. J , vol.359 , pp. 1-16
    • Frame, S.1    Cohen, P.2
  • 5
    • 0035413614 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3, properties, functions, and regulation
    • A. Ali, K.P. Hoeflich and J.R. Woodgett (2001) Glycogen synthase kinase-3, properties, functions, and regulation. Chem. Rev. 101 2527-2540.
    • (2001) Chem. Rev , vol.101 , pp. 2527-2540
    • Ali, A.1    Hoeflich, K.P.2    Woodgett, J.R.3
  • 6
    • 0020481918 scopus 로고
    • Multisite phosphorylation of glycogen synthase from rabbit skeletal muscle. Phosphorylation of site 5 by glycogen synthase kinase-5 (casein kinase-II) is a prerequisite for phosphorylation of sites 3 by glycogen synthase kinase-3
    • C. Picton, J.R. Woodgett, B. Hemmings and P. Cohen (1982) Multisite phosphorylation of glycogen synthase from rabbit skeletal muscle. Phosphorylation of site 5 by glycogen synthase kinase-5 (casein kinase-II) is a prerequisite for phosphorylation of sites 3 by glycogen synthase kinase-3. FEBS Lett. 150 191-196.
    • (1982) FEBS Lett , vol.150 , pp. 191-196
    • Picton, C.1    Woodgett, J.R.2    Hemmings, B.3    Cohen, P.4
  • 7
    • 0023656594 scopus 로고
    • Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3
    • C.J. Fiol, et al. (1987) Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3. J. Biol. Chem. 262 14042-14048.
    • (1987) J. Biol. Chem , vol.262 , pp. 14042-14048
    • Fiol, C.J.1
  • 8
    • 0027430039 scopus 로고
    • Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B
    • G.I. Welsh and C.G. Proud (1993) Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B. Biochem. J. 294 625-629.
    • (1993) Biochem. J , vol.294 , pp. 625-629
    • Welsh, G.I.1    Proud, C.G.2
  • 9
    • 0032498112 scopus 로고    scopus 로고
    • Regulation of eukaryotic initiation factor eIF2B, glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin
    • G.I. Welsh, et al. (1998) Regulation of eukaryotic initiation factor eIF2B, glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin. FEBS Lett. 421 125-130.
    • (1998) FEBS Lett , vol.421 , pp. 125-130
    • Welsh, G.I.1
  • 10
    • 0035340295 scopus 로고    scopus 로고
    • The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bε at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase
    • Y.L. Woods, et al. (2001) The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bε at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase. Biochem. J. 355 609-615.
    • (2001) Biochem. J , vol.355 , pp. 609-615
    • Woods, Y.L.1
  • 11
    • 0026488401 scopus 로고
    • Identification of multifunctional ATP-citrate lyase kinase as the α-isoform of glycogen synthase kinase-3
    • K. Hughes, et al. (1992) Identification of multifunctional ATP-citrate lyase kinase as the α-isoform of glycogen synthase kinase-3. Biochem. J. 288 309-314.
    • (1992) Biochem. J , vol.288 , pp. 309-314
    • Hughes, K.1
  • 12
    • 0028362181 scopus 로고
    • ATP citrate-lyase and glycogen synthase kinase-3β in 3T3-L1 cells during differentiation into adipocytes
    • W.B. Benjamin, et al. (1994) ATP citrate-lyase and glycogen synthase kinase-3β in 3T3-L1 cells during differentiation into adipocytes. Biochem. J. 300 477-482.
    • (1994) Biochem. J , vol.300 , pp. 477-482
    • Benjamin, W.B.1
  • 13
    • 0028670773 scopus 로고
    • 341 at Ser129 is required for the cAMP-mediated control of gene expression. A role for glycogen synthase kinase-3 in the control of gene expression
    • C.J. Fiol, et al. (1994) A secondary phosphorylation of CREB341 at Ser129 is required for the cAMP-mediated control of gene expression. A role for glycogen synthase kinase-3 in the control of gene expression. J. Biol. Chem. 269 32187-32193.
    • (1994) J. Biol. Chem , vol.269 , pp. 32187-32193
    • Fiol, C.J.1
  • 14
    • 0034969088 scopus 로고    scopus 로고
    • A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation
    • S. Frame, P. Cohen and R.M. Biondi (2001) A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation. Mol. Cell. 7 1321-1327.
    • (2001) Mol. Cell , vol.7 , pp. 1321-1327
    • Frame, S.1    Cohen, P.2    Biondi, R.M.3
  • 15
    • 0034743516 scopus 로고    scopus 로고
    • Structure of GSK3β reveals a primed phosphorylation mechanism
    • E. ter Haar, et al. (2001) Structure of GSK3β reveals a primed phosphorylation mechanism. Nat. Struct. Biol. 8 593-596.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 593-596
    • ter Haar, E.1
  • 16
    • 0035875098 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase kinase 3β: structural basis for phosphate-primed substrate specificity and autoinhibition
    • R. Dajani, et al. (2001) Crystal structure of glycogen synthase kinase 3β: structural basis for phosphate-primed substrate specificity and autoinhibition. Cell. 105 721-732.
    • (2001) Cell , vol.105 , pp. 721-732
    • Dajani, R.1
  • 17
    • 0027475421 scopus 로고
    • Modulation of the glycogen synthase kinase-3 family by tyrosine phosphorylation
    • K. Hughes, et al. (1993) Modulation of the glycogen synthase kinase-3 family by tyrosine phosphorylation. EMBO J. 12 803-808.
    • (1993) EMBO J , vol.12 , pp. 803-808
    • Hughes, K.1
  • 18
    • 0030712317 scopus 로고    scopus 로고
    • Further evidence that the inhibition of glycogen synthase kinase-3β by IGF-1 is mediated by PDK1/PKB-induced phosphorylation of Ser-9 and not by dephosphorylation of Tyr-216
    • M. Shaw, P. Cohen and D.R. Alessi (1997) Further evidence that the inhibition of glycogen synthase kinase-3β by IGF-1 is mediated by PDK1/PKB-induced phosphorylation of Ser-9 and not by dephosphorylation of Tyr-216. FEBS Lett. 416 307-311.
    • (1997) FEBS Lett , vol.416 , pp. 307-311
    • Shaw, M.1    Cohen, P.2    Alessi, D.R.3
  • 19
    • 0032734021 scopus 로고    scopus 로고
    • The novel tyrosine kinase ZAK1 activates GSK3 to direct cell fate specification
    • L. Kim, J. Liu and A.R. Kimmel (1999) The novel tyrosine kinase ZAK1 activates GSK3 to direct cell fate specification. Cell 99 399-408.
    • (1999) Cell , vol.99 , pp. 399-408
    • Kim, L.1    Liu, J.2    Kimmel, A.R.3
  • 20
    • 0034718421 scopus 로고    scopus 로고
    • Regulation and localization of tyrosine216 phosphorylation of glycogen synthase kinase-3β in cellular and animal models of neuronal degeneration
    • R.V. Bhat, et al. (2000) Regulation and localization of tyrosine216 phosphorylation of glycogen synthase kinase-3β in cellular and animal models of neuronal degeneration. Proc. Natl. Acad. Sci. USA 97 11074-11079.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11074-11079
    • Bhat, R.V.1
  • 21
    • 0033597936 scopus 로고    scopus 로고
    • Transient increases in intracellular calcium result in prolonged site-selective increases in tau phosphorylation through a glycogen synthase kinase 3β-dependent pathway
    • J.A. Hartigan and G.V. Johnson (1999) Transient increases in intracellular calcium result in prolonged site-selective increases in tau phosphorylation through a glycogen synthase kinase 3β-dependent pathway. J. Biol. Chem. 274 21395-21401.
    • (1999) J. Biol. Chem , vol.274 , pp. 21395-21401
    • Hartigan, J.A.1    Johnson, G.V.2
  • 22
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • D.A. Cross, et al. (1995) Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378 785-789.
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1
  • 23
    • 0027960448 scopus 로고
    • Mitogen inactivation of glycogen synthase kinase-3β in intact cells via serine 9 phosphorylation
    • V. Stambolic and J.R. Woodgett (1994) Mitogen inactivation of glycogen synthase kinase-3β in intact cells via serine 9 phosphorylation. Biochem. J. 303 701-704.
    • (1994) Biochem. J , vol.303 , pp. 701-704
    • Stambolic, V.1    Woodgett, J.R.2
  • 24
    • 0032746343 scopus 로고    scopus 로고
    • Role of protein kinase B and the MAP kinase cascade in mediating the EGF-dependent inhibition of glycogen synthase kinase 3 in Swiss 3T3 cells
    • M. Shaw and P. Cohen (1999) Role of protein kinase B and the MAP kinase cascade in mediating the EGF-dependent inhibition of glycogen synthase kinase 3 in Swiss 3T3 cells. FEBS Lett. 461 120-124.
    • (1999) FEBS Lett , vol.461 , pp. 120-124
    • Shaw, M.1    Cohen, P.2
  • 25
    • 0035846952 scopus 로고    scopus 로고
    • Regulation of glycogen synthesis by amino acids in cultured human muscle cells
    • J.L. Armstrong, et al. (2001) Regulation of glycogen synthesis by amino acids in cultured human muscle cells. J. Biol. Chem. 276 952-956.
    • (2001) J. Biol. Chem , vol.276 , pp. 952-956
    • Armstrong, J.L.1
  • 26
    • 0034176579 scopus 로고    scopus 로고
    • The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells
    • M.R. Williams, et al. (2000) The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells. Curr. Biol. 10 439-448.
    • (2000) Curr. Biol , vol.10 , pp. 439-448
    • Williams, M.R.1
  • 27
    • 0020585165 scopus 로고
    • Glycogen synthase from rabbit skeletal muscle: effect of insulin on the state of phosphorylation of the seven phosphoserine residues in vivo
    • P.J. Parker, F.B. Caudwell and P. Cohen (1983) Glycogen synthase from rabbit skeletal muscle: effect of insulin on the state of phosphorylation of the seven phosphoserine residues in vivo. Eur. J. Biochem. 130 227-234.
    • (1983) Eur. J. Biochem , vol.130 , pp. 227-234
    • Parker, P.J.1    Caudwell, F.B.2    Cohen, P.3
  • 28
    • 0032802629 scopus 로고    scopus 로고
    • Increased glycogen synthase kinase-3 activity in diabetes- and obesity- prone C57BL/6J mice
    • H. Eldar-Finkelman, et al. (1999) Increased glycogen synthase kinase-3 activity in diabetes- and obesity- prone C57BL/6J mice. Diabetes. 48 1662-1666.
    • (1999) Diabetes , vol.48 , pp. 1662-1666
    • Eldar-Finkelman, H.1
  • 29
    • 0033776383 scopus 로고    scopus 로고
    • Selective small molecule inhibitors of glycogen synthase kinase-3 modulate glycogen metabolism and gene transcription
    • M.P. Coghlan, et al. (2000) Selective small molecule inhibitors of glycogen synthase kinase-3 modulate glycogen metabolism and gene transcription. Chem. Biol. 7 793-803.
    • (2000) Chem. Biol , vol.7 , pp. 793-803
    • Coghlan, M.P.1
  • 30
    • 0034959714 scopus 로고    scopus 로고
    • Emerging fundamental themes in modern medicinal chemistry
    • P. Norman (2001) Emerging fundamental themes in modern medicinal chemistry. Drug News Perspect. 14 242-247.
    • (2001) Drug News Perspect , vol.14 , pp. 242-247
    • Norman, P.1
  • 31
    • 0035038729 scopus 로고    scopus 로고
    • Inhibition of GSK-3 selectively reduces glucose-6-phosphatase and phosphoenolpyruvate carbokykinase gene expression
    • P.A. Lochhead, et al. (2001) Inhibition of GSK-3 selectively reduces glucose-6-phosphatase and phosphoenolpyruvate carbokykinase gene expression. Diabetes. 50 937-946.
    • (2001) Diabetes , vol.50 , pp. 937-946
    • Lochhead, P.A.1
  • 32
    • 0035087123 scopus 로고    scopus 로고
    • Selective small-molecule inhibitors of glycogen synthase kinase-3 activity protect primary neurones from death
    • D.A. Cross, et al. (2001) Selective small-molecule inhibitors of glycogen synthase kinase-3 activity protect primary neurones from death. J. Neurochem. 77 94-102.
    • (2001) J. Neurochem , vol.77 , pp. 94-102
    • Cross, D.A.1
  • 33
    • 0032518695 scopus 로고    scopus 로고
    • Signal transduction by the Wnt family of ligands
    • T.C. Dale (1998) Signal transduction by the Wnt family of ligands. Biochem. J. 329 209-223.
    • (1998) Biochem. J , vol.329 , pp. 209-223
    • Dale, T.C.1
  • 34
    • 0033517102 scopus 로고    scopus 로고
    • Axin and Frat1 interact with dv1 and GSK, bridging Dv1 to GSK in Wnt-mediated regulation of LEF-1
    • L. Li, et al. (1999) Axin and Frat1 interact with dv1 and GSK, bridging Dv1 to GSK in Wnt-mediated regulation of LEF-1. EMBO J. 18 4233-4240.
    • (1999) EMBO J , vol.18 , pp. 4233-4240
    • Li, L.1
  • 35
    • 0032821768 scopus 로고    scopus 로고
    • A GSK3-binding peptide from FRAT1 selectively inhibits the GSK3-catalysed phosphorylation of axin and β-catenin
    • G.M. Thomas, et al. (1999) A GSK3-binding peptide from FRAT1 selectively inhibits the GSK3-catalysed phosphorylation of axin and β-catenin. FEBS Lett. 458 247-251.
    • (1999) FEBS Lett , vol.458 , pp. 247-251
    • Thomas, G.M.1
  • 36
    • 0034695912 scopus 로고    scopus 로고
    • Interaction among GSK-3, GBP, axin, and APC in Xenopus axis specification
    • G.H.R. Farr, et al. (2000) Interaction among GSK-3, GBP, axin, and APC in Xenopus axis specification. J. Cell Biol. 148 691-702.
    • (2000) J. Cell Biol , vol.148 , pp. 691-702
    • Farr, G.H.R.1
  • 37
    • 0034612636 scopus 로고    scopus 로고
    • Requirement for glycogen synthase kinase-3β in cell survival and NF-κB activation
    • K.P. Hoeflich, et al. (2000) Requirement for glycogen synthase kinase-3β in cell survival and NF-κB activation. Nature 406 86-90.
    • (2000) Nature , vol.406 , pp. 86-90
    • Hoeflich, K.P.1
  • 38
    • 0033895709 scopus 로고    scopus 로고
    • Wnt signaling and cancer
    • P. Polakis (2000) Wnt signaling and cancer. Genes Dev. 14 1837-1851.
    • (2000) Genes Dev , vol.14 , pp. 1837-1851
    • Polakis, P.1
  • 39
    • 0037127255 scopus 로고    scopus 로고
    • Identification of the Axin and Frat binding region of glycogen synthase kinase-3
    • E. Fraser, et al. (2002) Identification of the Axin and Frat binding region of glycogen synthase kinase-3. J. Biol. Chem. 277 2176-2185.
    • (2002) J. Biol. Chem , vol.277 , pp. 2176-2185
    • Fraser, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.