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Volumn 378, Issue 2, 2008, Pages 425-435

Split Pleckstrin Homology Domain-Mediated Cytoplasmic-Nuclear Localization of PI3-Kinase Enhancer GTPase

Author keywords

cytoplasmic nuclear shuttling; lipid binding; PI3 kinase enhancer; protein structure; split PH domain

Indexed keywords

PHOSPHATIDYLINOSITIDE; PLECKSTRIN; PROTEIN PHOSPHOINOSITOL 3 KIASE ENHANCER A; PROTEIN PHOSPHOINOSITOL 3 KIASE ENHANCER L; UNCLASSIFIED DRUG;

EID: 41249085467     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.02.052     Document Type: Article
Times cited : (13)

References (31)
  • 1
    • 28644434920 scopus 로고    scopus 로고
    • Structure of the split PH domain and distinct lipid-binding properties of the PH-PDZ supramodule of alpha-syntrophin
    • Yan J., Wen W., Xu W., Long J.F., Adams M.E., Froehner S.C., and Zhang M. Structure of the split PH domain and distinct lipid-binding properties of the PH-PDZ supramodule of alpha-syntrophin. EMBO J. 24 (2005) 3985-3995
    • (2005) EMBO J. , vol.24 , pp. 3985-3995
    • Yan, J.1    Wen, W.2    Xu, W.3    Long, J.F.4    Adams, M.E.5    Froehner, S.C.6    Zhang, M.7
  • 2
    • 33744962509 scopus 로고    scopus 로고
    • Structural characterization of the split pleckstrin homology domain in phospholipase C-gamma1 and its interaction with TRPC3
    • Wen W., Yan J., and Zhang M. Structural characterization of the split pleckstrin homology domain in phospholipase C-gamma1 and its interaction with TRPC3. J. Biol. Chem. 281 (2006) 12060-12068
    • (2006) J. Biol. Chem. , vol.281 , pp. 12060-12068
    • Wen, W.1    Yan, J.2    Zhang, M.3
  • 3
    • 33645981584 scopus 로고    scopus 로고
    • ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes
    • Teo H., Gill D.J., Sun J., Perisic O., Veprintsev D.B., Vallis Y., et al. ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes. Cell 125 (2006) 99-111
    • (2006) Cell , vol.125 , pp. 99-111
    • Teo, H.1    Gill, D.J.2    Sun, J.3    Perisic, O.4    Veprintsev, D.B.5    Vallis, Y.6
  • 5
    • 0033637979 scopus 로고    scopus 로고
    • PIKE: a nuclear GTPase that enhances PI3kinase activity and is regulated by protein 4.1N
    • Ye K., Hurt K.J., Wu F.Y., Fang M., Luo H.R., Hong J.J., et al. PIKE: a nuclear GTPase that enhances PI3kinase activity and is regulated by protein 4.1N. Cell 103 (2000) 919-930
    • (2000) Cell , vol.103 , pp. 919-930
    • Ye, K.1    Hurt, K.J.2    Wu, F.Y.3    Fang, M.4    Luo, H.R.5    Hong, J.J.6
  • 6
    • 1642421383 scopus 로고    scopus 로고
    • PIKE GTPase: a novel mediator of phosphoinositide signaling
    • Ye K., and Snyder S.H. PIKE GTPase: a novel mediator of phosphoinositide signaling. J. Cell Sci. 117 (2004) 155-161
    • (2004) J. Cell Sci. , vol.117 , pp. 155-161
    • Ye, K.1    Snyder, S.H.2
  • 7
    • 33947306609 scopus 로고    scopus 로고
    • PIKE GTPase are phosphoinositide-3-kinase enhancers, suppressing programmed cell death
    • Chan C.B., and Ye K. PIKE GTPase are phosphoinositide-3-kinase enhancers, suppressing programmed cell death. J. Cell. Mol. Med. 11 (2007) 39-53
    • (2007) J. Cell. Mol. Med. , vol.11 , pp. 39-53
    • Chan, C.B.1    Ye, K.2
  • 8
    • 28044431833 scopus 로고    scopus 로고
    • Phosphoinositol lipids bind to phosphatidylinositol 3 (PI3)-kinase enhancer GTPase and mediate its stimulatory effect on PI3-kinase and Akt signalings
    • Hu Y., Liu Z., and Ye K. Phosphoinositol lipids bind to phosphatidylinositol 3 (PI3)-kinase enhancer GTPase and mediate its stimulatory effect on PI3-kinase and Akt signalings. Proc. Natl Acad. Sci. USA 102 (2005) 16853-16858
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 16853-16858
    • Hu, Y.1    Liu, Z.2    Ye, K.3
  • 9
    • 0037203868 scopus 로고    scopus 로고
    • Phospholipase Cγ1 is a physiological guanine nucleotide exchange factor for the nuclear GTPase PIKE
    • Ye K., Aghdasi B., Luo H.R., Moriarity J.L., Wu F.Y., Hong J.J., et al. Phospholipase Cγ1 is a physiological guanine nucleotide exchange factor for the nuclear GTPase PIKE. Nature 415 (2002) 541-544
    • (2002) Nature , vol.415 , pp. 541-544
    • Ye, K.1    Aghdasi, B.2    Luo, H.R.3    Moriarity, J.L.4    Wu, F.Y.5    Hong, J.J.6
  • 10
    • 2342484285 scopus 로고    scopus 로고
    • PIKE-A is amplified in human cancers and prevents apoptosis by up-regulating Akt
    • Ahn J.Y., Hu Y., Kroll T.G., Allard P., and Ye K. PIKE-A is amplified in human cancers and prevents apoptosis by up-regulating Akt. Proc. Natl Acad. Sci. USA 101 (2004) 6993-6998
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 6993-6998
    • Ahn, J.Y.1    Hu, Y.2    Kroll, T.G.3    Allard, P.4    Ye, K.5
  • 11
    • 33947322795 scopus 로고    scopus 로고
    • PIKE-A is a proto-oncogene promoting cell growth, transformation and invasion
    • Liu X., Hu Y., Hao C., Rempel S.A., and Ye K. PIKE-A is a proto-oncogene promoting cell growth, transformation and invasion. Oncogene 26 (2007) 4918-4927
    • (2007) Oncogene , vol.26 , pp. 4918-4927
    • Liu, X.1    Hu, Y.2    Hao, C.3    Rempel, S.A.4    Ye, K.5
  • 15
    • 0037162293 scopus 로고    scopus 로고
    • High-resolution structure of the pleckstrin homology domain of protein kinase B/Akt bound to phosphatidylinositol (3,4,5)-triphosphate
    • Thomas C.C., Deak M., Alessi D.R., and van Aalten D.M. High-resolution structure of the pleckstrin homology domain of protein kinase B/Akt bound to phosphatidylinositol (3,4,5)-triphosphate. Curr. Biol. 12 (2002) 1256-1262
    • (2002) Curr. Biol. , vol.12 , pp. 1256-1262
    • Thomas, C.C.1    Deak, M.2    Alessi, D.R.3    van Aalten, D.M.4
  • 16
    • 6344229320 scopus 로고    scopus 로고
    • Structural determinants of phosphoinositide selectivity in splice variants of Grp1 family PH domains
    • Cronin T.C., DiNitto J.P., Czech M.P., and Lambright D.G. Structural determinants of phosphoinositide selectivity in splice variants of Grp1 family PH domains. EMBO J. 23 (2004) 3711-3720
    • (2004) EMBO J. , vol.23 , pp. 3711-3720
    • Cronin, T.C.1    DiNitto, J.P.2    Czech, M.P.3    Lambright, D.G.4
  • 17
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    • Ferguson K.M., Lemmon M.A., Schlessinger J., and Sigler P.B. Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell 83 (1995) 1037-1046
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 20
    • 33748313080 scopus 로고    scopus 로고
    • Membrane and juxtamembrane targeting by PH and PTB domains
    • DiNitto J.P., and Lambright D.G. Membrane and juxtamembrane targeting by PH and PTB domains. Biochim. Biophys. Acta 1761 (2006) 850-867
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 850-867
    • DiNitto, J.P.1    Lambright, D.G.2
  • 21
    • 1642367563 scopus 로고    scopus 로고
    • Genome-wide analysis of membrane targeting by S. cerevisiae pleckstrin homology domains
    • Yu J.W., Mendrola J.M., Audhya A., Singh S., Keleti D., DeWald D.B., et al. Genome-wide analysis of membrane targeting by S. cerevisiae pleckstrin homology domains. Mol. Cell 13 (2004) 677-688
    • (2004) Mol. Cell , vol.13 , pp. 677-688
    • Yu, J.W.1    Mendrola, J.M.2    Audhya, A.3    Singh, S.4    Keleti, D.5    DeWald, D.B.6
  • 22
    • 33746625935 scopus 로고    scopus 로고
    • Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly
    • Saad J.S., Miller J., Tai J., Kim A., Ghanam R.H., and Summers M.F. Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly. Proc. Natl Acad. Sci. USA 103 (2006) 11364-11369
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 11364-11369
    • Saad, J.S.1    Miller, J.2    Tai, J.3    Kim, A.4    Ghanam, R.H.5    Summers, M.F.6
  • 24
    • 0037205420 scopus 로고    scopus 로고
    • Interaction of elongation factor-1alpha and pleckstrin homology domain of phospholipase C-gamma 1 with activating its activity
    • Chang J.-S., Seok H., Kwon T.K., Min D.S., Ahn B.-H., Lee Y.H., et al. Interaction of elongation factor-1alpha and pleckstrin homology domain of phospholipase C-gamma 1 with activating its activity. J. Biol. Chem. 277 (2002) 19697-19702
    • (2002) J. Biol. Chem. , vol.277 , pp. 19697-19702
    • Chang, J.-S.1    Seok, H.2    Kwon, T.K.3    Min, D.S.4    Ahn, B.-H.5    Lee, Y.H.6
  • 25
    • 28444477387 scopus 로고    scopus 로고
    • Plasma membrane phosphoinositide organization by protein electrostatics
    • McLaughlin S., and Murray D. Plasma membrane phosphoinositide organization by protein electrostatics. Nature 438 (2005) 605-611
    • (2005) Nature , vol.438 , pp. 605-611
    • McLaughlin, S.1    Murray, D.2
  • 26
    • 2342520109 scopus 로고    scopus 로고
    • The tetrameric L27 domain complex as an organization platform for supramolecular assemblies
    • Feng W., Long J.F., Fan J.S., Suetake T., and Zhang M. The tetrameric L27 domain complex as an organization platform for supramolecular assemblies. Nat. Struct. Mol. Biol. 11 (2004) 475-480
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 475-480
    • Feng, W.1    Long, J.F.2    Fan, J.S.3    Suetake, T.4    Zhang, M.5
  • 29
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., and Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13 (1999) 289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 31
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 14 (1996) 51-55
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.