메뉴 건너뛰기




Volumn 356, Issue 1, 2007, Pages 255-259

Biochemical characterization of the type I inositol polyphosphate 4-phosphatase C2 domain

Author keywords

C2 domain; Calcium; Phosphatidylinositol 3,4 bisphosphate; PtdIns 3 kinase

Indexed keywords

ARGININE; ASPARTIC ACID; CALCIUM; INOSITOL POLYPHOSPHATE 4 PHOSPHATASE; LIPID; LYSINE; PHOSPHATASE; PHOSPHATE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3 PHOSPHATE; PHOSPHATIDYLINOSITOL 3,4 BISPHOSPHATE; UNCLASSIFIED DRUG;

EID: 33947141370     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.02.115     Document Type: Article
Times cited : (13)

References (25)
  • 1
    • 0029000258 scopus 로고
    • The isolation and characterization of cDNA encoding human and rat brain inositol polyphosphate 4-phosphatase
    • Norris F.A., Auethavekiat V., and Majerus P.W. The isolation and characterization of cDNA encoding human and rat brain inositol polyphosphate 4-phosphatase. J. Biol. Chem. 270 (1995) 16128-16133
    • (1995) J. Biol. Chem. , vol.270 , pp. 16128-16133
    • Norris, F.A.1    Auethavekiat, V.2    Majerus, P.W.3
  • 2
    • 0030890880 scopus 로고    scopus 로고
    • Inositol polyphosphate 4-phosphatase is inactivated by calpain-mediated proteolysis in stimulated human platelets
    • Norris F.A., Atkins R.C., and Majerus P.W. Inositol polyphosphate 4-phosphatase is inactivated by calpain-mediated proteolysis in stimulated human platelets. J. Biol. Chem. 272 (1997) 10987-10989
    • (1997) J. Biol. Chem. , vol.272 , pp. 10987-10989
    • Norris, F.A.1    Atkins, R.C.2    Majerus, P.W.3
  • 4
    • 0035950222 scopus 로고    scopus 로고
    • A null mutation in inositol polyphosphate 4-phosphatase type I causes selective neuronal loss in weeble mutant mice
    • Nystuen A., Legare M.E., Shultz L.D., and Frankel W.N. A null mutation in inositol polyphosphate 4-phosphatase type I causes selective neuronal loss in weeble mutant mice. Neuron 32 (2001) 203-212
    • (2001) Neuron , vol.32 , pp. 203-212
    • Nystuen, A.1    Legare, M.E.2    Shultz, L.D.3    Frankel, W.N.4
  • 7
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: structural and functional diversity
    • Nalefski E.A., and Falke J.J. The C2 domain calcium-binding motif: structural and functional diversity. Protein Sci. 5 (1996) 2375-2390
    • (1996) Protein Sci. , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 8
    • 0032497406 scopus 로고    scopus 로고
    • Mechanism of phospholipid binding by the C2A-domain of synaptotagmin I
    • Zhang X., Rizo J., and Sudhof T.C. Mechanism of phospholipid binding by the C2A-domain of synaptotagmin I. Biochemistry 37 (1998) 12395-12403
    • (1998) Biochemistry , vol.37 , pp. 12395-12403
    • Zhang, X.1    Rizo, J.2    Sudhof, T.C.3
  • 9
    • 0033591353 scopus 로고    scopus 로고
    • Mapping the phospholipid-binding surface and translocation determinants of the C2 domain from cytosolic phospholipase A2
    • Perisic O., Paterson H.F., Mosedale G., Lara-Gonzalez S., and Williams R.L. Mapping the phospholipid-binding surface and translocation determinants of the C2 domain from cytosolic phospholipase A2. J. Biol. Chem. 274 (1999) 14979-14987
    • (1999) J. Biol. Chem. , vol.274 , pp. 14979-14987
    • Perisic, O.1    Paterson, H.F.2    Mosedale, G.3    Lara-Gonzalez, S.4    Williams, R.L.5
  • 12
    • 0032563217 scopus 로고    scopus 로고
    • Calcium-dependent membrane penetration is a hallmark of the C2 domain of cytosolic phospholipase A2 whereas the C2A domain of synaptotagmin binds membranes electrostatically
    • Davletov B., Perisic O., and Williams R.L. Calcium-dependent membrane penetration is a hallmark of the C2 domain of cytosolic phospholipase A2 whereas the C2A domain of synaptotagmin binds membranes electrostatically. J. Biol. Chem. 273 (1998) 19093-19096
    • (1998) J. Biol. Chem. , vol.273 , pp. 19093-19096
    • Davletov, B.1    Perisic, O.2    Williams, R.L.3
  • 14
    • 0035943428 scopus 로고    scopus 로고
    • Structure of the C2 domain from novel protein kinase Cepsilon. A membrane binding model for Ca(2+)-independent C2 domains
    • Ochoa W.F., Garcia-Garcia J., Fita I., Corbalan-Garcia S., Verdaguer N., and Gomez-Fernandez J.C. Structure of the C2 domain from novel protein kinase Cepsilon. A membrane binding model for Ca(2+)-independent C2 domains. J. Mol. Biol. 311 (2001) 837-849
    • (2001) J. Mol. Biol. , vol.311 , pp. 837-849
    • Ochoa, W.F.1    Garcia-Garcia, J.2    Fita, I.3    Corbalan-Garcia, S.4    Verdaguer, N.5    Gomez-Fernandez, J.C.6
  • 16
    • 0033615538 scopus 로고    scopus 로고
    • Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association
    • Lee J.O., Yang H., Georgescu M.M., Di Cristofano A., Maehama T., Shi Y., Dixon J.E., Pandolfi P., and Pavletich N.P. Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. Cell 99 (1999) 323-334
    • (1999) Cell , vol.99 , pp. 323-334
    • Lee, J.O.1    Yang, H.2    Georgescu, M.M.3    Di Cristofano, A.4    Maehama, T.5    Shi, Y.6    Dixon, J.E.7    Pandolfi, P.8    Pavletich, N.P.9
  • 17
    • 0034671221 scopus 로고    scopus 로고
    • Stabilization and productive positioning roles of the C2 domain of PTEN tumor suppressor
    • Georgescu M.M., Kirsch K.H., Kaloudis P., Yang H., Pavletich N.P., and Hanafusa H. Stabilization and productive positioning roles of the C2 domain of PTEN tumor suppressor. Cancer Res. 60 (2000) 7033-7038
    • (2000) Cancer Res. , vol.60 , pp. 7033-7038
    • Georgescu, M.M.1    Kirsch, K.H.2    Kaloudis, P.3    Yang, H.4    Pavletich, N.P.5    Hanafusa, H.6
  • 19
    • 0034804631 scopus 로고    scopus 로고
    • Identification of a novel spliceoform of inositol polyphosphate 4-phosphatase type I alpha expressed in human platelets: structure of human inositol polyphosphate 4-phosphatase type I gene
    • Shearn C.T., Walker J., and Norris F.A. Identification of a novel spliceoform of inositol polyphosphate 4-phosphatase type I alpha expressed in human platelets: structure of human inositol polyphosphate 4-phosphatase type I gene. Biochem. Biophys. Res. Commun. 286 (2001) 119-125
    • (2001) Biochem. Biophys. Res. Commun. , vol.286 , pp. 119-125
    • Shearn, C.T.1    Walker, J.2    Norris, F.A.3
  • 20
    • 0030863996 scopus 로고    scopus 로고
    • The cDNA cloning and characterization of inositol polyphosphate 4-phosphatase type II. Evidence for conserved alternative splicing in the 4-phosphatase family
    • Norris F.A., Atkins R.C., and Majerus P.W. The cDNA cloning and characterization of inositol polyphosphate 4-phosphatase type II. Evidence for conserved alternative splicing in the 4-phosphatase family. J. Biol. Chem. 272 (1997) 23859-23864
    • (1997) J. Biol. Chem. , vol.272 , pp. 23859-23864
    • Norris, F.A.1    Atkins, R.C.2    Majerus, P.W.3
  • 22
    • 0036318064 scopus 로고    scopus 로고
    • Role of electrostatic and hydrophobic interactions in a Ca2+ dependent phospholipid binding by the C2A domain from synaptotagmin I
    • Gerber S.H., Rizo J., and Sudhof T.C. Role of electrostatic and hydrophobic interactions in a Ca2+ dependent phospholipid binding by the C2A domain from synaptotagmin I. Diabetes 51 (2002) S12-S18
    • (2002) Diabetes , vol.51
    • Gerber, S.H.1    Rizo, J.2    Sudhof, T.C.3
  • 23
    • 0842269784 scopus 로고    scopus 로고
    • A conformational switch in the Piccolo C2A domain regulated by alternative splicing
    • Garcia J., Gerber S.H., Sugita S., Sudhof T.C., and Rizo J. A conformational switch in the Piccolo C2A domain regulated by alternative splicing. Nat. Struct. Mol. Biol. 11 (2004) 45-53
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 45-53
    • Garcia, J.1    Gerber, S.H.2    Sugita, S.3    Sudhof, T.C.4    Rizo, J.5
  • 24
    • 0030890880 scopus 로고    scopus 로고
    • Inositol polyphosphate 4-phosphatase is inactivated by calpain-mediated proteolysis in stimulated human platelets
    • Norris F.A., Atkins R.C., and Majerus P.W. Inositol polyphosphate 4-phosphatase is inactivated by calpain-mediated proteolysis in stimulated human platelets. J. Biol. Chem. 272 (1997) 10987-10989
    • (1997) J. Biol. Chem. , vol.272 , pp. 10987-10989
    • Norris, F.A.1    Atkins, R.C.2    Majerus, P.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.