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Volumn 51, Issue 6, 2008, Pages 487-494

Recent progress on the structure of Ser/Thr protein phosphatases

Author keywords

Crystal structure; Ser Thr phosphatases; Similarities and differences; Subunit composition

Indexed keywords

PHOSPHOPROTEIN PHOSPHATASE;

EID: 44049096251     PISSN: 10069305     EISSN: 18622798     Source Type: Journal    
DOI: 10.1007/s11427-008-0068-y     Document Type: Article
Times cited : (13)

References (31)
  • 1
    • 33947316434 scopus 로고    scopus 로고
    • The skeletal muscle-specific glycogen-targeted protein phosphatase 1 plays a major role in the regulation of glycogen metabolism by adrenaline in vivo
    • 5
    • Toole B J, Cohen P T. The skeletal muscle-specific glycogen-targeted protein phosphatase 1 plays a major role in the regulation of glycogen metabolism by adrenaline in vivo. Cell Signal, 2007, 19(5): 1044-1055
    • (2007) Cell Signal , vol.19 , pp. 1044-1055
    • Toole, B.J.1    Cohen, P.T.2
  • 2
    • 33846280480 scopus 로고    scopus 로고
    • Protein phosphatase 2A play a crucial role in Giardia differentiation
    • 1
    • Lauwaet T, Davids B J, Torres-Escobar A, et al. Protein phosphatase 2A play a crucial role in Giardia differentiation. Mol Biochem Parasitology, 2007, 152(1): 80-89
    • (2007) Mol Biochem Parasitology , vol.152 , pp. 80-89
    • Lauwaet, T.1    Davids, B.J.2    Torres-Escobar, A.3
  • 3
    • 0032577483 scopus 로고    scopus 로고
    • Regulation of the calmodulin-stimulated protein phosphatase, calcineurin
    • 22
    • Klee C B, Ren H, Wang X. Regulation of the calmodulin-stimulated protein phosphatase, calcineurin. J Biol Chem, 1998, 273(22): 13367-13370
    • (1998) J Biol Chem , vol.273 , pp. 13367-13370
    • Klee, C.B.1    Ren, H.2    Wang, X.3
  • 4
    • 3042547846 scopus 로고    scopus 로고
    • Structure basis of protein phosphatase 1 regulation
    • 17
    • Terrak M, Kerff F, Langsetmo K, et al. Structure basis of protein phosphatase 1 regulation. Nature, 2004, 429(17): 780-784
    • (2004) Nature , vol.429 , pp. 780-784
    • Terrak, M.1    Kerff, F.2    Langsetmo, K.3
  • 5
    • 0032101295 scopus 로고    scopus 로고
    • Differential subcellular localization of protein phosphatase-1 alpha, gammal and delta isoforms during both interphase and mitosis in mammalian cells
    • 5
    • Andreassen P R, Lacroix F B, Moruzzi V E, et al. Differential subcellular localization of protein phosphatase-1 alpha, gammal and delta isoforms during both interphase and mitosis in mammalian cells. J Cell Biol, 1998, 141(5): 1207-1215
    • (1998) J Cell Biol , vol.141 , pp. 1207-1215
    • Andreassen, P.R.1    Lacroix, F.B.2    Moruzzi, V.E.3
  • 6
    • 0025275038 scopus 로고
    • Alpha-and beta-forms of the 65-kDa subunit of protein phosphatase2A have a similar 39 amino acid repeating structure
    • 13
    • Hemmings B A, Adams-Pearson C, Maurer F, et al. alpha-and beta-forms of the 65-kDa subunit of protein phosphatase2A have a similar 39 amino acid repeating structure. Biochemistry, 1990, 29(13): 3166-3173
    • (1990) Biochemistry , vol.29 , pp. 3166-3173
    • Hemmings, B.A.1    Adams-Pearson, C.2    Maurer, F.3
  • 7
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase2A: A highly regulated family of serine/threonine phosphatases implicated inc ell growth and signaling
    • 3
    • Janssens V, Goris J. Protein phosphatase2A: A highly regulated family of serine/threonine phosphatases implicated inc ell growth and signaling. Biochem J, 2001, 353(3): 417-439
    • (2001) Biochem J , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 8
    • 0033779701 scopus 로고    scopus 로고
    • Calcineurin: Form and function
    • 4
    • Rusnak F, Mertz P. Calcineurin: Form and function. Physiological Rev, 2000, 80(4): 1483-1521
    • (2000) Physiological Rev , vol.80 , pp. 1483-1521
    • Rusnak, F.1    Mertz, P.2
  • 9
    • 33750006297 scopus 로고    scopus 로고
    • Structure of proteinphosphatase2A core enzyme bound to tumor-inducing toxins
    • 20
    • Xing Y N, Xu Y H, Chen Y, et al. Structure of proteinphosphatase2A core enzyme bound to tumor-inducing toxins. Cell, 2006, 127(20): 341-353
    • (2006) Cell , vol.127 , pp. 341-353
    • Xing, Y.N.1    Xu, Y.H.2    Chen, Y.3
  • 10
    • 33846118688 scopus 로고    scopus 로고
    • Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme
    • 1
    • Cho U S, Xu W Q. Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme. Nature, 2006, 445(1): 53-57
    • (2006) Nature , vol.445 , pp. 53-57
    • Cho, U.S.1    Xu, W.Q.2
  • 11
    • 0029583122 scopus 로고
    • Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate
    • 5
    • Egloff M P, Cohen P T W, Reinemer P, et al. Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate. J Mol Biol, 1995, 254(5): 942-959
    • (1995) J Mol Biol , vol.254 , pp. 942-959
    • Egloff, M.P.1    Cohen, P.T.W.2    Reinemer, P.3
  • 12
    • 0029094754 scopus 로고
    • Three dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
    • 31
    • Goldberg J, Huang H B, Kwon Y G, et al. Three dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature, 1995, 376(31): 745-753
    • (1995) Nature , vol.376 , pp. 745-753
    • Goldberg, J.1    Huang, H.B.2    Kwon, Y.G.3
  • 13
    • 0035941284 scopus 로고    scopus 로고
    • Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1
    • 47
    • Maynes J T, Bateman K S, Cherney M M, et al. Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1. J Biol Chem, 2001, 276(47): 44078-44882
    • (2001) J Biol Chem , vol.276 , pp. 44078-44882
    • Maynes, J.T.1    Bateman, K.S.2    Cherney, M.M.3
  • 14
    • 18144395012 scopus 로고    scopus 로고
    • Importance of a surface hydrophobic pocket on protein phosphatase-1 catalytic subunit in recognizing cellular regulators
    • 16
    • Gibbons J A, Weiser D C, Shenolikar S. Importance of a surface hydrophobic pocket on protein phosphatase-1 catalytic subunit in recognizing cellular regulators. J Biol Chem, 2005, 280(16): 15903-15911
    • (2005) J Biol Chem , vol.280 , pp. 15903-15911
    • Gibbons, J.A.1    Weiser, D.C.2    Shenolikar, S.3
  • 15
    • 33750611319 scopus 로고    scopus 로고
    • The β12-β13 loop is a key regulatory element for activity and property in the catalytic domain of protein phosphatase 1 and 2B
    • 10
    • Xie X J, Huang W, Xue C Z, et al. The β12-β13 loop is a key regulatory element for activity and property in the catalytic domain of protein phosphatase 1 and 2B. Biol Chem, 2006, 387(10): 1461-1467
    • (2006) Biol Chem , vol.387 , pp. 1461-1467
    • Xie, X.J.1    Huang, W.2    Xue, C.Z.3
  • 16
    • 30344447686 scopus 로고    scopus 로고
    • Crystal structure of protein phosphatase-1 bound to Motuporin and Dihydromicrocystin-LA: Elucidation of the mechanism of enzyme inhibition by cyanobacterial toxins
    • 10
    • Maynes J T, Luu H A, Cherney M M, et al. Crystal structure of protein phosphatase-1 bound to Motuporin and Dihydromicrocystin-LA: Elucidation of the mechanism of enzyme inhibition by cyanobacterial toxins. J Mol Biol, 2006, 356(10): 111-120
    • (2006) J Mol Biol , vol.356 , pp. 111-120
    • Maynes, J.T.1    Luu, H.A.2    Cherney, M.M.3
  • 17
    • 0033534405 scopus 로고    scopus 로고
    • The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs
    • 1
    • Groves M R, Hanlon N, Turowski P, et al. The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs. Cell, 1999, 96(1): 99-110
    • (1999) Cell , vol.96 , pp. 99-110
    • Groves, M.R.1    Hanlon, N.2    Turowski, P.3
  • 18
    • 33845404441 scopus 로고    scopus 로고
    • Structure of the protein phosphatase2A holoenzyme
    • 15
    • Xu Y H, Xing Y N, Chen Y, et al. Structure of the protein phosphatase2A holoenzyme. Cell, 2006, 127(15): 1239-1251
    • (2006) Cell , vol.127 , pp. 1239-1251
    • Xu, Y.H.1    Xing, Y.N.2    Chen, Y.3
  • 19
    • 0029133116 scopus 로고
    • X-ray structure of calcineurin inhibited by the immunophilin- immunosuppressant FKBP12-FK506 complex
    • 11
    • Griffith J P, Kim J L, Kim E E, et al. X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex. Cell, 1995, 82(11): 507-522
    • (1995) Cell , vol.82 , pp. 507-522
    • Griffith, J.P.1    Kim, J.L.2    Kim, E.E.3
  • 20
    • 0028848524 scopus 로고
    • Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex
    • 7
    • Kissinger C R, Parge H E, Knighton D R, et al. Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. Nature, 1995, 378(7): 641-644
    • (1995) Nature , vol.378 , pp. 641-644
    • Kissinger, C.R.1    Parge, H.E.2    Knighton, D.R.3
  • 21
    • 0037126026 scopus 로고    scopus 로고
    • Crystal structure of calcineurincyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes
    • 17
    • Qing H, Kim H Y, Liu Y D, et al. Crystal structure of calcineurincyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes. Proc Natl Acad Sci USA, 2002, 99(17): 12037-12042
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12037-12042
    • Qing, H.1    Kim, H.Y.2    Liu, Y.D.3
  • 22
    • 0037108767 scopus 로고    scopus 로고
    • Crystal structure of human calcineurin complexed with cyclosporine and human cyclophilin
    • 15
    • Jin L, Harrison S C. Crystal structure of human calcineurin complexed with cyclosporine and human cyclophilin. Proc Natl Acad Sci USA, 2002, 99(15): 13522-13526
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13522-13526
    • Jin, L.1    Harrison, S.C.2
  • 23
    • 0242690189 scopus 로고    scopus 로고
    • Structures of calcineurin and its complexes with immunophilins- immunosuppressants
    • 4
    • Ke H M, Huai Q. Structures of calcineurin and its complexes with immunophilins-immunosuppressants. Biochem Biophys Res Commun, 2003, 311(4): 1095-1102
    • (2003) Biochem Biophys Res Commun , vol.311 , pp. 1095-1102
    • Ke, H.M.1    Huai, Q.2
  • 24
    • 34247868090 scopus 로고    scopus 로고
    • Structure of the calcineurin-NFAT complex: Defining a T cell activation switch using solution NMR and crystal coordinates
    • 5
    • Takeuchi K, Roehrl M H, Sun Z Y, et al. Structure of the calcineurin-NFAT complex: Defining a T cell activation switch using solution NMR and crystal coordinates. Structure, 2007, 15(5): 587-597
    • (2007) Structure , vol.15 , pp. 587-597
    • Takeuchi, K.1    Roehrl, M.H.2    Sun, Z.Y.3
  • 25
    • 7544237946 scopus 로고    scopus 로고
    • The salt bridge of calcineurin is important for transferring the effect of CNB binding to CAN
    • 1
    • Hou Q, Yi X, Jiang G H, Wei Q. The salt bridge of calcineurin is important for transferring the effect of CNB binding to CAN. FEBS Lett, 2004, 577(1): 294-298
    • (2004) FEBS Lett , vol.577 , pp. 294-298
    • Hou, Q.1    Yi, X.2    Jiang, G.H.3    Wei, Q.4
  • 26
    • 0034697320 scopus 로고    scopus 로고
    • Synergism between the calmodulin-binding and autoinhibitory domains on calcineurin is essential for the induction of their phosphatase activity
    • 16
    • Tokoyoda K, Takemoto Y, Nakayama T, et al. Synergism between the calmodulin-binding and autoinhibitory domains on calcineurin is essential for the induction of their phosphatase activity. J Biol Chem, 2000, 275(16): 11728-11735
    • (2000) J Biol Chem , vol.275 , pp. 11728-11735
    • Tokoyoda, K.1    Takemoto, Y.2    Nakayama, T.3
  • 27
    • 31044452100 scopus 로고    scopus 로고
    • Structure of calmodulin bound to a calcineurin peptide: A new way of making an old binding mode
    • Ye Q L, Li X, Wong A, et al. Structure of calmodulin bound to a calcineurin peptide: A new way of making an old binding mode. Biochemistry, 2006, 45: 738-745
    • (2006) Biochemistry , vol.45 , pp. 738-745
    • Ye, Q.L.1    Li, X.2    Wong, A.3
  • 28
    • 0035407298 scopus 로고    scopus 로고
    • Roles of serine/threonine phosphatases in hippocampal synaptic plasticity
    • Winder D G, Sweatt J D. Roles of serine/threonine phosphatases in hippocampal synaptic plasticity. Nat Rev Neurosci, 2001, 2: 461-474
    • (2001) Nat Rev Neurosci , vol.2 , pp. 461-474
    • Winder, D.G.1    Sweatt, J.D.2
  • 29
    • 0028332599 scopus 로고
    • Localization of phosphatase inhibitor-1 mRNA in the developing and adult rat brain in comparison with that of protein phosphatase-1 mRNAs
    • Sakagami H, Ebina K, Kondo H. Localization of phosphatase inhibitor-1 mRNA in the developing and adult rat brain in comparison with that of protein phosphatase-1 mRNAs. Brain Res Mol Brain Res, 1994, 25: 7-18
    • (1994) Brain Res Mol Brain Res , vol.25 , pp. 7-18
    • Sakagami, H.1    Ebina, K.2    Kondo, H.3
  • 30
    • 0032511826 scopus 로고    scopus 로고
    • Quantitative immunocytochemistry of DARPP-32-expressing neurons in the rat caudatoputamen
    • Ouimet C C, Langley-Gullion K C, Greengard P. Quantitative immunocytochemistry of DARPP-32-expressing neurons in the rat caudatoputamen. Brain Res, 1998, 808: 8-12
    • (1998) Brain Res , vol.808 , pp. 8-12
    • Ouimet, C.C.1    Langley-Gullion, K.C.2    Greengard, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.