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Volumn 6, Issue 7, 2010, Pages 507-513

Translation of the phosphoinositide code by PI effectors

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHATIDYLINOSITIDE;

EID: 77953762012     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.390     Document Type: Review
Times cited : (200)

References (100)
  • 1
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon, M.A. Membrane recognition by phospholipid-binding domains. Nat. Rev. Mol. Cell Biol. 9, 99-111 (2008).
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 2
    • 33748462297 scopus 로고    scopus 로고
    • Membrane binding domains
    • Hurley, J.H. Membrane binding domains. Biochim Biophys Acta 1761, 805-811 (2006).
    • (2006) Biochim Biophys Acta , vol.1761 , pp. 805-811
    • Hurley, J.H.1
  • 3
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo, G. & De Camilli, P. Phosphoinositides in cell regulation and membrane dynamics. Nature 443, 651-657 (2006).
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 4
    • 2342661960 scopus 로고    scopus 로고
    • Phosphoinositides in constitutive membrane traffic
    • Roth, M.G. Phosphoinositides in constitutive membrane traffic. Physiol. Rev. 84, 699-730 (2004).
    • (2004) Physiol. Rev. , vol.84 , pp. 699-730
    • Roth, M.G.1
  • 5
    • 0034911881 scopus 로고    scopus 로고
    • Synthesis and function of 3-phosphorylated inositol lipids
    • Vanhaesebroeck, B. et al. Synthesis and function of 3-phosphorylated inositol lipids. Annu. Rev. Biochem. 70, 535-602 (2001).
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 535-602
    • Vanhaesebroeck, B.1
  • 6
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
    • Harlan, J.E., Hajduk, P.J., Yoon, H.S. & Fesik, S.W. Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate. Nature 371, 168-170 (1994).
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 7
    • 33748329427 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate recognition and membrane docking by the FYVE domain
    • Kutateladze, T.G. Phosphatidylinositol 3-phosphate recognition and membrane docking by the FYVE domain. Biochim. Biophys. Acta 1761, 868-877 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 868-877
    • Kutateladze, T.G.1
  • 8
    • 0032111444 scopus 로고    scopus 로고
    • Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains
    • Burd, C.G. & Emr, S.D. Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains. Mol. Cell 2, 157-162 (1998).
    • (1998) Mol. Cell , vol.2 , pp. 157-162
    • Burd, C.G.1    Emr, S.D.2
  • 9
    • 0032581670 scopus 로고    scopus 로고
    • FYVE fingers bind PtdIns(3)
    • Gaullier, J.M. et al. FYVE fingers bind PtdIns(3)P. Nature 394, 432-433 (1998).
    • (1998) P. Nature , vol.394 , pp. 432-433
    • Gaullier, J.M.1
  • 11
    • 0035199161 scopus 로고    scopus 로고
    • FENS-1 and DFCP1 are FYVE domain-containing proteins with distinct functions in the endosomal and Golgi compartments
    • Ridley, S.H. et al. FENS-1 and DFCP1 are FYVE domain-containing proteins with distinct functions in the endosomal and Golgi compartments. J. Cell Sci. 114, 3991-4000 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 3991-4000
    • Ridley, S.H.1
  • 12
    • 4944247868 scopus 로고    scopus 로고
    • Alfy, a novel FYVE-domain-containing protein associated with protein granules and autophagic membranes
    • Simonsen, A. et al. Alfy, a novel FYVE-domain-containing protein associated with protein granules and autophagic membranes. J. Cell Sci. 117, 4239-4251 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 4239-4251
    • Simonsen, A.1
  • 13
    • 0035871081 scopus 로고    scopus 로고
    • Cellular functions of phosphatidylinositol 3-phosphate and FYVE domain proteins
    • Gillooly, D.J., Simonsen, A. & Stenmark, H. Cellular functions of phosphatidylinositol 3-phosphate and FYVE domain proteins. Biochem. J. 355, 249-258 (2001).
    • (2001) Biochem. J. , vol.355 , pp. 249-258
    • Gillooly, D.J.1    Simonsen, A.2    Stenmark, H.3
  • 14
    • 0037135529 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs
    • Stahelin, R.V. et al. Phosphatidylinositol 3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs. J. Biol. Chem. 277, 26379-26388 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 26379-26388
    • Stahelin, R.V.1
  • 15
    • 0345700741 scopus 로고    scopus 로고
    • Computer modeling of the membrane interaction of FYVE domains
    • Diraviyam, K., Stahelin, R.V., Cho, W. & Murray, D. Computer modeling of the membrane interaction of FYVE domains. J. Mol. Biol. 328, 721-736 (2003).
    • (2003) J. Mol. Biol. , vol.328 , pp. 721-736
    • Diraviyam, K.1    Stahelin, R.V.2    Cho, W.3    Murray, D.4
  • 16
    • 1642494667 scopus 로고    scopus 로고
    • Multivalent mechanism of membrane insertion by the FYVE domain
    • Kutateladze, T.G. et al. Multivalent mechanism of membrane insertion by the FYVE domain. J. Biol. Chem. 279, 3050-3057 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 3050-3057
    • Kutateladze, T.G.1
  • 17
    • 24944499610 scopus 로고    scopus 로고
    • Targeting of the FYVE domain to endosomal membranes is regulated by a histidine switch
    • Lee, S.A. et al. Targeting of the FYVE domain to endosomal membranes is regulated by a histidine switch. Proc. Natl. Acad. Sci. USA 102, 13052-13057 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13052-13057
    • Lee, S.A.1
  • 18
    • 68149182252 scopus 로고    scopus 로고
    • Membrane insertion of the FYVE domain is modulated by pH
    • He, J. et al. Membrane insertion of the FYVE domain is modulated by pH. Proteins 76, 852-860 (2009).
    • (2009) Proteins , vol.76 , pp. 852-860
    • He, J.1
  • 20
    • 0033612372 scopus 로고    scopus 로고
    • Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p
    • Misra, S. & Hurley, J.H. Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p. Cell 97, 657-666 (1999).
    • (1999) Cell , vol.97 , pp. 657-666
    • Misra, S.1    Hurley, J.H.2
  • 21
    • 0035793903 scopus 로고    scopus 로고
    • Structural mechanism of endosome docking by the FYVE domain
    • Kutateladze, T. & Overduin, M. Structural mechanism of endosome docking by the FYVE domain. Science 291, 1793-1796 (2001).
    • (2001) Science , vol.291 , pp. 1793-1796
    • Kutateladze, T.1    Overduin, M.2
  • 22
    • 11144230909 scopus 로고    scopus 로고
    • The molecular basis of the differential subcellular localization of FYVE domains
    • Blatner, N.R. et al. The molecular basis of the differential subcellular localization of FYVE domains. J. Biol. Chem. 279, 53818-53827 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 53818-53827
    • Blatner, N.R.1
  • 23
    • 0035943055 scopus 로고    scopus 로고
    • High affinity binding of a FYVE domain to phosphatidylinositol 3-phosphate requires intact phospholipid but not FYVE domain oligomerization
    • Sankaran, V.G., Klein, D.E., Sachdeva, M.M. & Lemmon, M.A. High affinity binding of a FYVE domain to phosphatidylinositol 3-phosphate requires intact phospholipid but not FYVE domain oligomerization. Biochemistry 40, 8581-8587 (2001).
    • (2001) Biochemistry , vol.40 , pp. 8581-8587
    • Sankaran, V.G.1    Klein, D.E.2    Sachdeva, M.M.3    Lemmon, M.A.4
  • 24
    • 28944451676 scopus 로고    scopus 로고
    • Investigation of the binding geometry of a peripheral membrane protein
    • Brunecky, R. et al. Investigation of the binding geometry of a peripheral membrane protein. Biochemistry 44, 16064-16071 (2005).
    • (2005) Biochemistry , vol.44 , pp. 16064-16071
    • Brunecky, R.1
  • 25
    • 0033105847 scopus 로고    scopus 로고
    • The endosome fusion regulator early-endosomal autoantigen 1 (EEA1) is a dimer
    • Callaghan, J., Simonsen, A., Gaullier, J.M., Toh, B.H. & Stenmark, H. The endosome fusion regulator early-endosomal autoantigen 1 (EEA1) is a dimer. Biochem. J. 338, 539-543 (1999).
    • (1999) Biochem. J. , vol.338 , pp. 539-543
    • Callaghan, J.1    Simonsen, A.2    Gaullier, J.M.3    Toh, B.H.4    Stenmark, H.5
  • 26
    • 0035930332 scopus 로고    scopus 로고
    • Multivalent endosome targeting by homodimeric EEA1
    • Dumas, J.J. et al. Multivalent endosome targeting by homodimeric EEA1. Mol. Cell 8, 947-958 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 947-958
    • Dumas, J.J.1
  • 27
    • 0034602964 scopus 로고    scopus 로고
    • The FYVE domain of early endosome antigen 1 is required for both phosphatidylinositol 3-phosphate and Rab5 binding. Critical role of this dual interaction for endosomal localization
    • Lawe, D.C., Patki, V., Heller-Harrison, R., Lambright, D. & Corvera, S. The FYVE domain of early endosome antigen 1 is required for both phosphatidylinositol 3-phosphate and Rab5 binding. Critical role of this dual interaction for endosomal localization. J. Biol. Chem. 275, 3699-3705 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 3699-3705
    • Lawe, D.C.1    Patki, V.2    Heller-Harrison, R.3    Lambright, D.4    Corvera, S.5
  • 28
    • 1242316975 scopus 로고    scopus 로고
    • Structural basis for endosomal targeting by FYVE domains
    • Hayakawa, A. et al. Structural basis for endosomal targeting by FYVE domains. J. Biol. Chem. 279, 5958-5966 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 5958-5966
    • Hayakawa, A.1
  • 29
    • 0034681262 scopus 로고    scopus 로고
    • Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction
    • Mao, Y. et al. Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction. Cell 100, 447-456 (2000).
    • (2000) Cell , vol.100 , pp. 447-456
    • Mao, Y.1
  • 30
    • 0034663568 scopus 로고    scopus 로고
    • Signal-dependent membrane targeting by pleckstrin homology (PH) domains
    • Lemmon, M.A. & Ferguson, K.M. Signal-dependent membrane targeting by pleckstrin homology (PH) domains. Biochem. J. 350, 1-18 (2000).
    • (2000) Biochem. J. , vol.350 , pp. 1-18
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 31
    • 33748313080 scopus 로고    scopus 로고
    • Membrane and juxtamembrane targeting by PH and PTB domains
    • DiNitto, J.P. & Lambright, D.G. Membrane and juxtamembrane targeting by PH and PTB domains. Biochim. Biophys. Acta 1761, 850-867 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 850-867
    • Dinitto, J.P.1    Lambright, D.G.2
  • 33
    • 0027288910 scopus 로고
    • A putative modular domain present in diverse signaling proteins
    • Mayer, B.J., Ren, R., Clark, K.L. & Baltimore, D. A putative modular domain present in diverse signaling proteins. Cell 73, 629-630 (1993).
    • (1993) Cell , vol.73 , pp. 629-630
    • Mayer, B.J.1    Ren, R.2    Clark, K.L.3    Baltimore, D.4
  • 34
    • 0029824848 scopus 로고    scopus 로고
    • Mutation of the pleckstrin homology domain of Bruton's tyrosine kinase in immunodeficiency impaired inositol 1 3 4,5-tetrakisphosphate binding capacity
    • Fukuda, M., Kojima, T., Kabayama, H. & Mikoshiba, K. Mutation of the pleckstrin homology domain of Bruton's tyrosine kinase in immunodeficiency impaired inositol 1,3,4,5-tetrakisphosphate binding capacity. J. Biol. Chem. 271, 30303-30306 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 30303-30306
    • Fukuda, M.1    Kojima, T.2    Kabayama, H.3    Mikoshiba, K.4
  • 35
    • 0030975196 scopus 로고    scopus 로고
    • Signaling by phosphoinositide-3 4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains
    • Klarlund, J.K. et al. Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains. Science 275, 1927-1930 (1997).
    • (1997) Science , vol.275 , pp. 1927-1930
    • Klarlund, J.K.1
  • 36
    • 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. & Lambright, D.G. Structural determinants of phosphoinositide selectivity in splice variants of Grp1 family PH domains. EMBO J. 23, 3711-3720 (2004).
    • (2004) EMBO J. , vol.23 , pp. 3711-3720
    • Cronin, T.C.1    Dinitto, J.P.2    Czech, M.P.3    Lambright, D.G.4
  • 37
    • 8744219635 scopus 로고    scopus 로고
    • Pleckstrin homology domains: Not just for phosphoinositides
    • Lemmon, M.A. Pleckstrin homology domains: not just for phosphoinositides. Biochem. Soc. Trans. 32, 707-711 (2004).
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 707-711
    • Lemmon, M.A.1
  • 38
    • 0041510168 scopus 로고    scopus 로고
    • Molecular modeling of the membrane targeting of phospholipase C pleckstrin homology domains
    • Singh, S.M. & Murray, D. Molecular modeling of the membrane targeting of phospholipase C pleckstrin homology domains. Protein Sci. 12, 1934-1953 (2003).
    • (2003) Protein Sci. , vol.12 , pp. 1934-1953
    • Singh, S.M.1    Murray, D.2
  • 39
    • 36148957855 scopus 로고    scopus 로고
    • Mechanistic basis of differential cellular responses of phosphatidylinositol 3 4-bisphosphate-and phosphatidylinositol 34,5-trisphosphate-binding pleckstrin homology domains
    • Manna, D., Albanese, A., Park, W.S. & Cho, W. Mechanistic basis of differential cellular responses of phosphatidylinositol 3,4-bisphosphate-and phosphatidylinositol 3,4,5-trisphosphate-binding pleckstrin homology domains. J. Biol. Chem. 282, 32093-32105 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 32093-32105
    • Manna, D.1    Albanese, A.2    Park, W.S.3    Cho, W.4
  • 40
    • 51449111718 scopus 로고    scopus 로고
    • Molecular mechanism of membrane targeting by the GRP1 PH domain
    • He, J. et al. Molecular mechanism of membrane targeting by the GRP1 PH domain. J. Lipid Res. 49, 1807-1815 (2008).
    • (2008) J. Lipid Res. , vol.49 , pp. 1807-1815
    • He, J.1
  • 41
    • 58849094579 scopus 로고    scopus 로고
    • Single-molecule fluorescence studies of a PH domain: New insights into the membrane docking reaction
    • Knight, J.D. & Falke, J.J. Single-molecule fluorescence studies of a PH domain: new insights into the membrane docking reaction. Biophys. J. 96, 566-582 (2009).
    • (2009) Biophys. J. , vol.96 , pp. 566-582
    • Knight, J.D.1    Falke, J.J.2
  • 42
    • 0033635275 scopus 로고    scopus 로고
    • Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains
    • Ferguson, K.M. et al. Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains. Mol. Cell 6, 373-384 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 373-384
    • Ferguson, K.M.1
  • 43
    • 0033634785 scopus 로고    scopus 로고
    • Structural basis of 3-phosphoinositide recognition by pleckstrin homology domains
    • Lietzke, S.E. et al. Structural basis of 3-phosphoinositide recognition by pleckstrin homology domains. Mol. Cell 6, 385-394 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 385-394
    • Lietzke, S.E.1
  • 44
    • 22544461027 scopus 로고    scopus 로고
    • Membrane activity of the phospholipase C-delta1 pleckstrin homology (PH) domain
    • Flesch, F.M., Yu, J.W., Lemmon, M.A. & Burger, K.N. Membrane activity of the phospholipase C-delta1 pleckstrin homology (PH) domain. Biochem. J. 389, 435-441 (2005).
    • (2005) Biochem. J. , vol.389 , pp. 435-441
    • Flesch, F.M.1    Yu, J.W.2    Lemmon, M.A.3    Burger, K.N.4
  • 45
    • 34548483180 scopus 로고    scopus 로고
    • Structural and membrane binding analysis of the Phox homology domain of Bem1p: Basis of phosphatidylinositol 4-phosphate specificity
    • Stahelin, R.V., Karathanassis, D., Murray, D., Williams, R.L. & Cho, W. Structural and membrane binding analysis of the Phox homology domain of Bem1p: basis of phosphatidylinositol 4-phosphate specificity. J. Biol. Chem. 282, 25737-25747 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 25737-25747
    • Stahelin, R.V.1    Karathanassis, D.2    Murray, D.3    Williams, R.L.4    Cho, W.5
  • 46
    • 8144228588 scopus 로고    scopus 로고
    • Structural insights into the regulation of PDK1 by phosphoinositides and inositol phosphates
    • Komander, D. et al. Structural insights into the regulation of PDK1 by phosphoinositides and inositol phosphates. EMBO J. 23, 3918-3928 (2004).
    • (2004) EMBO J. , vol.23 , pp. 3918-3928
    • Komander, D.1
  • 47
    • 0033561252 scopus 로고    scopus 로고
    • Structure of the PH domain from Bruton?s tyrosine kinase in complex with inositol 1 3 4,5-tetrakisphosphate
    • Baraldi, E. et al. Structure of the PH domain from Bruton?s tyrosine kinase in complex with inositol 1,3,4,5-tetrakisphosphate. Structure 7, 449-460 (1999).
    • (1999) Structure , vol.7 , pp. 449-460
    • Baraldi, E.1
  • 48
    • 36249015526 scopus 로고    scopus 로고
    • Structural basis and mechanism of autoregulation in 3-phosphoinositide- dependent Grp1 family Arf GTPase exchange factors
    • DiNitto, J.P. et al. Structural basis and mechanism of autoregulation in 3-phosphoinositide-dependent Grp1 family Arf GTPase exchange factors. Mol. Cell 28, 569-583 (2007).
    • (2007) Mol. Cell , vol.28 , pp. 569-583
    • Dinitto, J.P.1
  • 49
    • 0037162293 scopus 로고    scopus 로고
    • High-resolution structure of the pleckstrin homology domain of protein kinase b/akt bound to phosphatidylinositol 3, 4,5)-trisphosphate
    • Thomas, C.C., Deak, M., Alessi, D.R. & van Aalten, D.M. High-resolution structure of the pleckstrin homology domain of protein kinase b/akt bound to phosphatidylinositol (3,4,5)-trisphosphate. Curr. Biol. 12, 1256-1262 (2002).
    • (2002) Curr. Biol. , vol.12 , pp. 1256-1262
    • Thomas, C.C.1    Deak, M.2    Alessi, D.R.3    Van Aalten, D.M.4
  • 50
    • 0242468741 scopus 로고    scopus 로고
    • Binding of phosphatidylinositol 3,4,5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change
    • Milburn, C.C. et al. Binding of phosphatidylinositol 3,4,5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change. Biochem. J. 375, 531-538 (2003).
    • (2003) Biochem. J. , vol.375 , pp. 531-538
    • Milburn, C.C.1
  • 51
    • 34547172596 scopus 로고    scopus 로고
    • A transforming mutation in the pleckstrin homology domain of AKT1 in cancer
    • Carpten, J.D. et al. A transforming mutation in the pleckstrin homology domain of AKT1 in cancer. Nature 448, 439-444 (2007).
    • (2007) Nature , vol.448 , pp. 439-444
    • Carpten, J.D.1
  • 52
    • 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. & Sigler, P.B. Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell 83, 1037-1046 (1995).
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 53
    • 38349049373 scopus 로고    scopus 로고
    • Structural analysis of the carboxy terminal PH domain of pleckstrin bound to d-myo-inositol 1,2,3,5,6-pentakisphosphate
    • Jackson, S.G., Zhang, Y., Haslam, R.J. & Junop, M.S. Structural analysis of the carboxy terminal PH domain of pleckstrin bound to d-myo-inositol 1,2,3,5,6-pentakisphosphate. BMC Struct. Biol. 7, 80 (2007).
    • (2007) BMC Struct. Biol. , vol.7 , pp. 80
    • Jackson, S.G.1    Zhang, Y.2    Haslam, R.J.3    Junop, M.S.4
  • 54
    • 34250361914 scopus 로고    scopus 로고
    • Non-canonical interaction of phosphoinositides with pleckstrin homology domains of Tiam1 and ArhGAP9
    • Ceccarelli, D.F. et al. Non-canonical interaction of phosphoinositides with pleckstrin homology domains of Tiam1 and ArhGAP9. J. Biol. Chem. 282, 13864-13874 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 13864-13874
    • Ceccarelli, D.F.1
  • 55
    • 0029096888 scopus 로고
    • Structure of the binding site for inositol phosphates in a PH domain
    • Hyvönen, M. et al. Structure of the binding site for inositol phosphates in a PH domain. EMBO J. 14, 4676-4685 (1995).
    • (1995) EMBO J. , vol.14 , pp. 4676-4685
    • Hyvönen, M.1
  • 56
    • 33748461590 scopus 로고    scopus 로고
    • The Phox (PX) domain proteins and membrane traffic
    • Seet, L.F. & Hong, W. The Phox (PX) domain proteins and membrane traffic. Biochim. Biophys. Acta 1761, 878-896 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 878-896
    • Seet, L.F.1    Hong, W.2
  • 57
    • 0029850711 scopus 로고    scopus 로고
    • Novel domains in NADPH oxidase subunits, sorting nexins, and PtdIns 3-kinases: Binding partners of SH3 domains?
    • Ponting, C.P. et al. Novel domains in NADPH oxidase subunits, sorting nexins, and PtdIns 3-kinases: binding partners of SH3 domains? Protein Sci. 5, 2353-2357 (1996).
    • (1996) Protein Sci. , vol.5 , pp. 2353-2357
    • Ponting, C.P.1
  • 58
    • 0035941208 scopus 로고    scopus 로고
    • All phox homology (PX) domains from Saccharomyces cerevisiae specifically recognize phosphatidylinositol-3-phosphate
    • Yu, J.W. & Lemmon, M.A. All phox homology (PX) domains from Saccharomyces cerevisiae specifically recognize phosphatidylinositol-3- phosphate. J. Biol. Chem. 276, 44179-44184 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 44179-44184
    • Yu, J.W.1    Lemmon, M.A.2
  • 59
    • 0034946472 scopus 로고    scopus 로고
    • The PX domains of p47phox and p40phox bind to lipid products of PI(3)K
    • Kanai, F. et al. The PX domains of p47phox and p40phox bind to lipid products of PI(3)K. Nat. Cell Biol. 3, 675-678 (2001).
    • (2001) Nat. Cell Biol. , vol.3 , pp. 675-678
    • Kanai, F.1
  • 60
    • 0034944422 scopus 로고    scopus 로고
    • SNX3 regulates endosomal function through its PX-domain-mediated interaction with PtdIns(3)P
    • Xu, Y., Hortsman, H., Seet, L., Wong, S.H. & Hong, W. SNX3 regulates endosomal function through its PX-domain-mediated interaction with PtdIns(3)P. Nat. Cell Biol. 3, 658-666 (2001).
    • (2001) Nat. Cell Biol. , vol.3 , pp. 658-666
    • Xu, Y.1    Hortsman, H.2    Seet, L.3    Wong, S.H.4    Hong, W.5
  • 61
    • 0034947026 scopus 로고    scopus 로고
    • Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes
    • Cheever, M.L. et al. Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes. Nat. Cell Biol. 3, 613-618 (2001).
    • (2001) Nat. Cell Biol. , vol.3 , pp. 613-618
    • Cheever, M.L.1
  • 62
    • 0034743311 scopus 로고    scopus 로고
    • PtdIns(3)P regulates the neutrophil oxidase complex by binding to the PX domain of p40(phox)
    • Ellson, C.D. et al. PtdIns(3)P regulates the neutrophil oxidase complex by binding to the PX domain of p40(phox). Nat. Cell Biol. 3, 679-682 (2001).
    • (2001) Nat. Cell Biol. , vol.3 , pp. 679-682
    • Ellson, C.D.1
  • 63
    • 0035979372 scopus 로고    scopus 로고
    • Phox homology domains specifically bind phosphatidylinositol phosphates
    • Song, X. et al. Phox homology domains specifically bind phosphatidylinositol phosphates. Biochemistry 40, 8940-8944 (2001).
    • (2001) Biochemistry , vol.40 , pp. 8940-8944
    • Song, X.1
  • 65
    • 0037853270 scopus 로고    scopus 로고
    • Membrane binding mechanisms of the PX domains of NADPH oxidase p40phox and p47phox
    • Stahelin, R.V., Burian, A., Bruzik, K.S., Murray, D. & Cho, W. Membrane binding mechanisms of the PX domains of NADPH oxidase p40phox and p47phox. J. Biol. Chem. 278, 14469-14479 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 14469-14479
    • Stahelin, R.V.1    Burian, A.2    Bruzik, K.S.3    Murray, D.4    Cho, W.5
  • 66
    • 33846000631 scopus 로고    scopus 로고
    • Molecular mechanism of membrane docking by the Vam7p PX domain
    • Lee, S.A. et al. Molecular mechanism of membrane docking by the Vam7p PX domain. J. Biol. Chem. 281, 37091-37101 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 37091-37101
    • Lee, S.A.1
  • 67
    • 17944367436 scopus 로고    scopus 로고
    • The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate
    • Bravo, J. et al. The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate. Mol. Cell 8, 829-839 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 829-839
    • Bravo, J.1
  • 68
    • 0036791737 scopus 로고    scopus 로고
    • Binding of the PX domain of p47(phox) to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction
    • Karathanassis, D. et al. Binding of the PX domain of p47(phox) to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction. EMBO J. 21, 5057-5068 (2002).
    • (2002) EMBO J. , vol.21 , pp. 5057-5068
    • Karathanassis, D.1
  • 69
    • 10744227963 scopus 로고    scopus 로고
    • Crystal structure of the yeast Phox homology (PX) domain protein Grd19p complexed to phosphatidylinositol-3-phosphate
    • Zhou, C.Z. et al. Crystal structure of the yeast Phox homology (PX) domain protein Grd19p complexed to phosphatidylinositol-3-phosphate. J. Biol. Chem. 278, 50371-50376 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 50371-50376
    • Zhou, C.Z.1
  • 71
    • 0034995037 scopus 로고    scopus 로고
    • Solution structure of the PX domain, a target of the SH3 domain
    • Hiroaki, H., Ago, T., Ito, T., Sumimoto, H. & Kohda, D. Solution structure of the PX domain, a target of the SH3 domain. Nat. Struct. Biol. 8, 526-530 (2001).
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 526-530
    • Hiroaki, H.1    Ago, T.2    Ito, T.3    Sumimoto, H.4    Kohda, D.5
  • 72
    • 3142655870 scopus 로고    scopus 로고
    • Structural basis of membrane targeting by the Phox homology domain of cytokine-independent survival kinase (CISK-PX)
    • Xing, Y. et al. Structural basis of membrane targeting by the Phox homology domain of cytokine-independent survival kinase (CISK-PX). J. Biol. Chem. 279, 30662-30669 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 30662-30669
    • Xing, Y.1
  • 73
    • 34748816375 scopus 로고    scopus 로고
    • Mechanistic similarities in docking of the FYVE and PX domains to phosphatidylinositol 3-phosphate containing membranes
    • Kutateladze, T.G. Mechanistic similarities in docking of the FYVE and PX domains to phosphatidylinositol 3-phosphate containing membranes. Prog. Lipid Res. 46, 315-327 (2007).
    • (2007) Prog. Lipid Res. , vol.46 , pp. 315-327
    • Kutateladze, T.G.1
  • 74
    • 11144237619 scopus 로고    scopus 로고
    • Mechanism of membrane binding of the phospholipase D1 PX domain
    • Stahelin, R.V. et al. Mechanism of membrane binding of the phospholipase D1 PX domain. J. Biol. Chem. 279, 54918-54926 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 54918-54926
    • Stahelin, R.V.1
  • 75
    • 33846010781 scopus 로고    scopus 로고
    • Structural and membrane binding analysis of the Phox homology domain of phosphoinositide 3-kinase-C2alpha
    • Stahelin, R.V. et al. Structural and membrane binding analysis of the Phox homology domain of phosphoinositide 3-kinase-C2alpha. J. Biol. Chem. 281, 39396-39406 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 39396-39406
    • Stahelin, R.V.1
  • 77
    • 34547768732 scopus 로고    scopus 로고
    • The structural basis of novel endosome anchoring activity of KIF16B kinesin
    • Blatner, N.R. et al. The structural basis of novel endosome anchoring activity of KIF16B kinesin. EMBO J. 26, 3709-3719 (2007).
    • (2007) EMBO J. , vol.26 , pp. 3709-3719
    • Blatner, N.R.1
  • 78
    • 33847200398 scopus 로고    scopus 로고
    • Full-length p40phox structure suggests a basis for regulation mechanism of its membrane binding
    • Honbou, K. et al. Full-length p40phox structure suggests a basis for regulation mechanism of its membrane binding. EMBO J. 26, 1176-1186 (2007).
    • (2007) EMBO J. , vol.26 , pp. 1176-1186
    • Honbou, K.1
  • 79
    • 42049122203 scopus 로고    scopus 로고
    • Crystal structures of PI3K-C2alpha PX domain indicate conformational change associated with ligand binding
    • Parkinson, G.N., Vines, D., Driscoll, P.C. & Djordjevic, S. Crystal structures of PI3K-C2alpha PX domain indicate conformational change associated with ligand binding. BMC Struct. Biol. 8, 13 (2008).
    • (2008) BMC Struct. Biol. , vol.8 , pp. 13
    • Parkinson, G.N.1    Vines, D.2    Driscoll, P.C.3    Djordjevic, S.4
  • 80
    • 16344377050 scopus 로고    scopus 로고
    • Determinants of the endosomal localization of sorting nexin 1
    • Zhong, Q. et al. Determinants of the endosomal localization of sorting nexin 1. Mol. Biol. Cell 16, 2049-2057 (2005).
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2049-2057
    • Zhong, Q.1
  • 82
    • 33748288113 scopus 로고    scopus 로고
    • F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature
    • Itoh, T. & De Camilli, P. BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature. Biochim. Biophys. Acta 1761, 897-912 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 897-912
    • Itoh, T.1    Bar, P.D.2
  • 83
    • 33748324514 scopus 로고    scopus 로고
    • Membrane binding and subcellular targeting of C2 domains
    • Cho, W. & Stahelin, R.V. Membrane binding and subcellular targeting of C2 domains. Biochim. Biophys. Acta 1761, 838-849 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 838-849
    • Cho, W.1    Stahelin, R.V.2
  • 84
    • 0034283003 scopus 로고    scopus 로고
    • Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain
    • Hamada, K., Shimizu, T., Matsui, T., Tsukita, S. & Hakoshima, T. Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. EMBO J. 19, 4449-4462 (2000).
    • (2000) EMBO J. , vol.19 , pp. 4449-4462
    • Hamada, K.1    Shimizu, T.2    Matsui, T.3    Tsukita, S.4    Hakoshima, T.5
  • 85
    • 70349835304 scopus 로고    scopus 로고
    • GOLPH3 bridges phosphatidylinositol-4-phosphate and actomyosin to stretch and shape the Golgi to promote budding
    • Dippold, H.C. et al. GOLPH3 bridges phosphatidylinositol-4-phosphate and actomyosin to stretch and shape the Golgi to promote budding. Cell 139, 337-351 (2009).
    • (2009) Cell , vol.139 , pp. 337-351
    • Dippold, H.C.1
  • 86
    • 76149142505 scopus 로고    scopus 로고
    • PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase signaling to retrograde Golgi trafficking
    • Wood, C.S. et al. PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase signaling to retrograde Golgi trafficking. J. Cell Biol. 187, 967-975 (2009).
    • (2009) J. Cell Biol. , vol.187 , pp. 967-975
    • Wood, C.S.1
  • 87
    • 33748313081 scopus 로고    scopus 로고
    • The prevalence and significance of PDZ domain-phosphoinositide interactions
    • Zimmermann, P. The prevalence and significance of PDZ domain-phosphoinositide interactions. Biochim. Biophys. Acta 1761, 947-956 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 947-956
    • Zimmermann, P.1
  • 88
    • 62749090535 scopus 로고    scopus 로고
    • Phosphatidylinositol 3,5-bisphosphate and Fab1p/PIKfyve underPPIn endo-lysosome function
    • Dove, S.K., Dong, K., Kobayashi, T., Williams, F.K. & Michell, R.H. Phosphatidylinositol 3,5-bisphosphate and Fab1p/PIKfyve underPPIn endo-lysosome function. Biochem. J. 419, 1-13 (2009).
    • (2009) Biochem. J. , vol.419 , pp. 1-13
    • Dove, S.K.1    Dong, K.2    Kobayashi, T.3    Williams, F.K.4    Michell, R.H.5
  • 89
    • 0035874921 scopus 로고    scopus 로고
    • G-protein signaling through tubby proteins
    • Santagata, S. et al. G-protein signaling through tubby proteins. Science 292, 2041-2050 (2001).
    • (2001) Science , vol.292 , pp. 2041-2050
    • Santagata, S.1
  • 90
    • 70449413105 scopus 로고    scopus 로고
    • Live cell imaging with protein domains capable of recognizing phosphatidylinositol 4,5-bisphosphate; A comparative study
    • Szentpetery, Z., Balla, A., Kim, Y.J., Lemmon, M.A. & Balla, T. Live cell imaging with protein domains capable of recognizing phosphatidylinositol 4,5-bisphosphate; a comparative study. BMC Cell Biol. 10, 67 (2009).
    • (2009) BMC Cell Biol. , vol.10 , pp. 67
    • Szentpetery, Z.1    Balla, A.2    Kim, Y.J.3    Lemmon, M.A.4    Balla, T.5
  • 91
    • 0035895882 scopus 로고    scopus 로고
    • The effector domain of myristoylated alanine-rich C kinase substrate binds strongly to phosphatidylinositol 4,5-bisphosphate
    • Wang, J., Arbuzova, A., Hangyas-Mihalyne, G. & McLaughlin, S. The effector domain of myristoylated alanine-rich C kinase substrate binds strongly to phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 276, 5012-5019 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 5012-5019
    • Wang, J.1    Arbuzova, A.2    Hangyas-Mihalyne, G.3    McLaughlin, S.4
  • 92
    • 0035881755 scopus 로고    scopus 로고
    • New EMBO members' review: Actin cytoskeleton regulation through modulation of PI(4 5)P(2) rafts
    • Caroni, P. New EMBO members' review: actin cytoskeleton regulation through modulation of PI(4,5)P(2) rafts. EMBO J. 20, 4332-4336 (2001).
    • (2001) EMBO J. , vol.20 , pp. 4332-4336
    • Caroni, P.1
  • 93
    • 0032522719 scopus 로고    scopus 로고
    • Membrane-targeting sequences on AKAP79 bind phosphatidylinositol-4, 5-bisphosphate
    • Dell'Acqua, M.L., Faux, M.C., Thorburn, J., Thorburn, A. & Scott, J.D. Membrane-targeting sequences on AKAP79 bind phosphatidylinositol-4, 5-bisphosphate. EMBO J. 17, 2246-2260 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2246-2260
    • Dell'Acqua, M.L.1    Faux, M.C.2    Thorburn, J.3    Thorburn, A.4    Scott, J.D.5
  • 94
    • 0025308055 scopus 로고
    • The actin-binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C
    • Goldschmidt-Clermont, P.J., Machesky, L.M., Baldassare, J.J. & Pollard, T.D. The actin-binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C. Science 247, 1575-1578 (1990).
    • (1990) Science , vol.247 , pp. 1575-1578
    • Goldschmidt-Clermont, P.J.1    MacHesky, L.M.2    Baldassare, J.J.3    Pollard, T.D.4
  • 95
    • 0034683746 scopus 로고    scopus 로고
    • Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate
    • Rohatgi, R., Ho, H.Y. & Kirschner, M.W. Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate. J. Cell Biol. 150, 1299-1310 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 1299-1310
    • Rohatgi, R.1    Ho, H.Y.2    Kirschner, M.W.3
  • 96
    • 0035135419 scopus 로고    scopus 로고
    • Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes
    • Ford, M.G. et al. Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes. Science 291, 1051-1055 (2001).
    • (2001) Science , vol.291 , pp. 1051-1055
    • Ford, M.G.1
  • 97
    • 0037179662 scopus 로고    scopus 로고
    • Curvature of clathrin-coated pits driven by epsin
    • Ford, M.G. et al. Curvature of clathrin-coated pits driven by epsin. Nature 419, 361-366 (2002).
    • (2002) Nature , vol.419 , pp. 361-366
    • Ford, M.G.1
  • 98
    • 59849125052 scopus 로고    scopus 로고
    • Mutations in phosphoinositide metabolizing enzymes and human disease
    • McCrea, H.J. & De Camilli, P. Mutations in phosphoinositide metabolizing enzymes and human disease. Physiology (Bethesda) 24, 8-16 (2009).
    • (2009) Physiology (Bethesda) , vol.24 , pp. 8-16
    • McCrea, H.J.1    De Camilli, P.2
  • 99
    • 2642563771 scopus 로고    scopus 로고
    • Phosphoinositide signaling; From affinity probes to pharmaceutical targets
    • Prestwich, G.D. Phosphoinositide signaling; from affinity probes to pharmaceutical targets. Chem. Biol. 11, 619-637 (2004).
    • (2004) Chem. Biol. , vol.11 , pp. 619-637
    • Prestwich, G.D.1
  • 100
    • 33746257209 scopus 로고    scopus 로고
    • The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism
    • Engelman, J.A., Luo, J. & Cantley, L.C. The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism. Nat. Rev. Genet. 7, 606-619 (2006).
    • (2006) Nat. Rev. Genet. , vol.7 , pp. 606-619
    • Engelman, J.A.1    Luo, J.2    Cantley, L.C.3


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