메뉴 건너뛰기




Volumn 265, Issue 1, 1999, Pages 481-490

Involvement of EF hand motifs in the Ca2+-dependent binding of the pleckstrin homology domain to phosphoinositides

Author keywords

Calcium; EF hand motif; Inositol trisphosphate; Phosphoinositide; Phospholipase C ; Pleckstrin homology domain

Indexed keywords

PHOSPHATIDYLINOSITIDE; PHOSPHOLIPASE C; PLECKSTRIN;

EID: 0033214251     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00786.x     Document Type: Article
Times cited : (36)

References (56)
  • 1
    • 0031006326 scopus 로고    scopus 로고
    • Regulatory recruitment of signalling molecules to the cell membrane by pleckstrin homology domains
    • 1. Lemmon, M.A., Falsca, M., Ferguson, K.M. & Schlessinger, J. (1997) Regulatory recruitment of signalling molecules to the cell membrane by pleckstrin homology domains. Trends Cell Biol. 7, 237-242.
    • (1997) Trends Cell Biol. , vol.7 , pp. 237-242
    • Lemmon, M.A.1    Falsca, M.2    Ferguson, K.M.3    Schlessinger, J.4
  • 3
    • 0031831780 scopus 로고    scopus 로고
    • Pleckstrin homology domains: A common fold with diverse functions
    • 3. Rebecchi, M.J. & Scarlata, S. (1998) Pleckstrin homology domains: a common fold with diverse functions. Annu. Rev. Biophys. Miomol. Struc. 27, 503-528.
    • (1998) Annu. Rev. Biophys. Miomol. Struc. , vol.27 , pp. 503-528
    • Rebecchi, M.J.1    Scarlata, S.2
  • 5
    • 0028246440 scopus 로고
    • Binding of G protein βγ-subunits to pleckstrin homology domains
    • 5. Touhara, K., Inglese, J., Pitcher, J.A., Shaw, G. & Lefkowitz, R.J. (1994) Binding of G protein βγ-subunits to pleckstrin homology domains. J. Biol. Chem. 269, 10217-10220.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10217-10220
    • Touhara, K.1    Inglese, J.2    Pitcher, J.A.3    Shaw, G.4    Lefkowitz, R.J.5
  • 6
    • 0027481032 scopus 로고
    • The binding site for the βγ subunits of heterotrimeric G proteins on the β-adrenergic receptor kinase
    • 6. Koch, W.J., Inglese, J., Stone, W.C. & Lefkowitz, R.J. (1993) The binding site for the βγ subunits of heterotrimeric G proteins on the β-adrenergic receptor kinase. J. Biol. Chem. 268, 8256-8260.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8256-8260
    • Koch, W.J.1    Inglese, J.2    Stone, W.C.3    Lefkowitz, R.J.4
  • 7
    • 0028173394 scopus 로고
    • Binding of βγ subunits of heterotrimeric G proteins to the PH domain of Bruton tyrosine kinase
    • 7. Tsukada, S., Simon, M.I., Witte, O.N. & Katz, A. (1994) Binding of βγ subunits of heterotrimeric G proteins to the PH domain of Bruton tyrosine kinase. Proc. Natl Acad. Sci. USA 91, 11256-11260.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 11256-11260
    • Tsukada, S.1    Simon, M.I.2    Witte, O.N.3    Katz, A.4
  • 8
    • 0028564915 scopus 로고
    • The pleckstrin homology domain of Bruton tyrosine kinase interacts with protein kinase C
    • 8. Yao, L., Kawakami, Y. & Kawakami, T. (1994) The pleckstrin homology domain of Bruton tyrosine kinase interacts with protein kinase C. Proc. Natl Acad. Sci. USA 91, 9175-9179.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9175-9179
    • Yao, L.1    Kawakami, Y.2    Kawakami, T.3
  • 9
    • 0028670203 scopus 로고
    • The pleckstrin homology domain of RAC protein kinase associates with the regulatory domain of protein kinase C
    • 9. Konishi, H., Kuroda, S. & Kikkawa, U. (1994) The pleckstrin homology domain of RAC protein kinase associates with the regulatory domain of protein kinase C. Biochem. Biophys. Res. Commun. 205, 1770-1775.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1770-1775
    • Konishi, H.1    Kuroda, S.2    Kikkawa, U.3
  • 11
    • 0029939448 scopus 로고    scopus 로고
    • PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface
    • 11. Lemmon, L.A., Ferguson, K.M. & Schlessinger, J. (1996) PH domains: diverse sequences with a common fold recruit signaling molecules to the cell surface. Cell 85, 621-624.
    • (1996) Cell , vol.85 , pp. 621-624
    • Lemmon, L.A.1    Ferguson, K.M.2    Schlessinger, J.3
  • 14
    • 0031565953 scopus 로고    scopus 로고
    • Distinct specificity in the binding of inositol phosphates by pleckstrin homology domains of pleckstrin, RAC-protein kinase, diacylglycerol kinase and a new 130-kDa protein
    • 14. Takeuchi, H., Kanematsu, T., Misumi, Y., Sakane, F., Konishi, H., Kikkawa, U., Watanabe, Y., Katan, M. & Hirata, M. (1997) Distinct specificity in the binding of inositol phosphates by pleckstrin homology domains of pleckstrin, RAC-protein kinase, diacylglycerol kinase and a new 130-kDa protein. Biochim. Biophys. Acta 1359, 275-285.
    • (1997) Biochim. Biophys. Acta , vol.1359 , pp. 275-285
    • Takeuchi, H.1    Kanematsu, T.2    Misumi, Y.3    Sakane, F.4    Konishi, H.5    Kikkawa, U.6    Watanabe, Y.7    Katan, M.8    Hirata, M.9
  • 16
    • 0032518666 scopus 로고    scopus 로고
    • Activation of phospholipase Cγ by PI 3-kinase-induced PH domain-mediated membrane targeting
    • 16. Falasca, M., Logan, S.K., Lehto, V.P., Baccante, G., Lemmon, M.A. & Schlessinger, J. (1998) Activation of phospholipase Cγ by PI 3-kinase-induced PH domain-mediated membrane targeting. EMBO J. 17, 414-422.
    • (1998) EMBO J. , vol.17 , pp. 414-422
    • Falasca, M.1    Logan, S.K.2    Lehto, V.P.3    Baccante, G.4    Lemmon, M.A.5    Schlessinger, J.6
  • 17
    • 0033514366 scopus 로고    scopus 로고
    • Differential association of the pleckstrin homology domains of phospholipases C-β1, C-β2, and C-δ1 with lipid bilayers and the βγ subunits of heterotrimeric G proteins
    • 17. Wang, T., Pentyala, S., Rebecchi, M.J. & Scarlata, S. (1999) Differential association of the pleckstrin homology domains of phospholipases C-β1, C-β2, and C-δ1 with lipid bilayers and the βγ subunits of heterotrimeric G proteins. Biochemistry 38, 1517-1524.
    • (1999) Biochemistry , vol.38 , pp. 1517-1524
    • Wang, T.1    Pentyala, S.2    Rebecchi, M.J.3    Scarlata, S.4
  • 21
    • 0029838615 scopus 로고    scopus 로고
    • Localization of a high affinity inositol 1,4,5-trisphosphate/inositol 1,4,5,6-tetrakisphosphate binding domain to the pleckstrin homology module of a new 130-kDa protein: Characterization of the determinants of structural specificity
    • 21. Takeuchi, H., Kanematsu, T., Misumi, Y., Yaakob, H.B., Yagisawa, H., Ikehara, Y., Watanabe, Y., Tan, Z., Shears, S.B. & Hirata, M. (1996) Localization of a high affinity inositol 1,4,5-trisphosphate/inositol 1,4,5,6-tetrakisphosphate binding domain to the pleckstrin homology module of a new 130-kDa protein: characterization of the determinants of structural specificity. Biochem. J. 318, 561-568.
    • (1996) Biochem. J. , vol.318 , pp. 561-568
    • Takeuchi, H.1    Kanematsu, T.2    Misumi, Y.3    Yaakob, H.B.4    Yagisawa, H.5    Ikehara, Y.6    Watanabe, Y.7    Tan, Z.8    Shears, S.B.9    Hirata, M.10
  • 22
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    • 22. Ferguson, K.M., Lemmon, M.A., Schlegginger, J. & Sigler, P.B. (1995) Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell 83, 1037-1046.
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlegginger, J.3    Sigler, P.B.4
  • 23
    • 0028874438 scopus 로고
    • Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain
    • 23. Lemmon, M.A., Ferguson, K.M., O'Brien, R., Sigler, P.B. & Schleginger, J. (1995) Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain. Proc. Natl Acad. Sci. USA 92, 10472-10471-476.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10472-10476
    • Lemmon, M.A.1    Ferguson, K.M.2    O'Brien, R.3    Sigler, P.B.4    Schleginger, J.5
  • 24
    • 0028787055 scopus 로고
    • The pleckstrin homology domain of phospholipase C-δ1 binds with high affinity to phosphatidylinositol 4,5-bisphosphate in bilayer membranes
    • 24. Garcia, P., Gupta, R., Shah, S., Mprris, A.J., Rudge, S.A., Scarlata, S., Petrova, V., McLaughlin, S. & Rebecchi, M.J. (1995) The pleckstrin homology domain of phospholipase C-δ1 binds with high affinity to phosphatidylinositol 4,5-bisphosphate in bilayer membranes. Biochemistry 34, 16228-16234.
    • (1995) Biochemistry , vol.34 , pp. 16228-16234
    • Garcia, P.1    Gupta, R.2    Shah, S.3    Mprris, A.J.4    Rudge, S.A.5    Scarlata, S.6    Petrova, V.7    McLaughlin, S.8    Rebecchi, M.J.9
  • 27
    • 0028040136 scopus 로고
    • D-myo-inositol 1,4,5-trisphosphate inhibits binding of phospholipase C-δ1 to bilayer membrane
    • 27. Cifuentes, M.E., Delaney, T. & Rebecchi, M.J. (1994) D-myo-inositol 1,4,5-trisphosphate inhibits binding of phospholipase C-δ1 to bilayer membrane. J. Biol. Chem. 269, 1945-1948.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1945-1948
    • Cifuentes, M.E.1    Delaney, T.2    Rebecchi, M.J.3
  • 28
    • 0031972511 scopus 로고    scopus 로고
    • Replacements of single basic amino acids in the pleckstrin homology domain of phospholipase C-δ1 alter the ligand binding, phospholipase activity and interaction with the plasma membrane
    • 28. Yagisawa, H., Sakuma, K., Paterson, H.F., Cheung, R., Allen, V., Hirata, H., Watanabe, Y., Hirata, M., Williams, R.L. & Katan, M. (1998) Replacements of single basic amino acids in the pleckstrin homology domain of phospholipase C-δ1 alter the ligand binding, phospholipase activity and interaction with the plasma membrane. J. Biol. Chem. 273, 417-424.
    • (1998) J. Biol. Chem. , vol.273 , pp. 417-424
    • Yagisawa, H.1    Sakuma, K.2    Paterson, H.F.3    Cheung, R.4    Allen, V.5    Hirata, H.6    Watanabe, Y.7    Hirata, M.8    Williams, R.L.9    Katan, M.10
  • 29
    • 0027366440 scopus 로고
    • Agonist-stimulated synthesis of phosphatidylinositol(3,4,5)-trisphosphate: A new intracellular signalling system?
    • 29. Stephens, L., Jackson, T. & Hawkins, P. (1993) Agonist-stimulated synthesis of phosphatidylinositol(3,4,5)-trisphosphate: a new intracellular signalling system? Biochim. Biophys. Acta 1179, 27-75.
    • (1993) Biochim. Biophys. Acta , vol.1179 , pp. 27-75
    • Stephens, L.1    Jackson, T.2    Hawkins, P.3
  • 30
    • 0027389279 scopus 로고
    • Comparison of the levels of inositol metabolites in transformed haematopoietic cells and their normal counterparts
    • 30. Bunce, C., French, P., Allen, P., Mountford, J., Moor, B., Greaves, M., Michell, R. & Brown, G. (1993) Comparison of the levels of inositol metabolites in transformed haematopoietic cells and their normal counterparts. Biochem. J. 289, 667-673.
    • (1993) Biochem. J. , vol.289 , pp. 667-673
    • Bunce, C.1    French, P.2    Allen, P.3    Mountford, J.4    Moor, B.5    Greaves, M.6    Michell, R.7    Brown, G.8
  • 32
  • 34
    • 0032547744 scopus 로고    scopus 로고
    • 3H]inositol-labeled phosphoinositide pools
    • 3H]inositol-labeled phosphoinositide pools. J. Cell Biol. 143, 501-510.
    • (1998) J. Cell Biol. , vol.143 , pp. 501-510
    • Varnai, P.1    Balla, T.2
  • 35
    • 0033582303 scopus 로고    scopus 로고
    • Real-time visualization of PH domain-dependent translocation of phospholipase C-δ1 in renal epithelial cels (MDCK): Response to hypo-osmotic stress
    • 35. Fujii, M., Ohtsubo, M., Ogawa, T., Kamata, H., Hirata, H. & Yagisawa, H. (1999) Real-time visualization of PH domain-dependent translocation of phospholipase C-δ1 in renal epithelial cels (MDCK): response to hypo-osmotic stress. Biochem. Biophys. Res. Commun. 254, 284-291.
    • (1999) Biochem. Biophys. Res. Commun. , vol.254 , pp. 284-291
    • Fujii, M.1    Ohtsubo, M.2    Ogawa, T.3    Kamata, H.4    Hirata, H.5    Yagisawa, H.6
  • 36
    • 0028357208 scopus 로고
    • Thrombin-mediated phosphoinositide hydrolysis in Chinese hamster ovary cells overexpressing phospholipase C-δ1
    • 36. Banno, Y., Okano, Y. & Nozawa, Y. (1994) Thrombin-mediated phosphoinositide hydrolysis in Chinese hamster ovary cells overexpressing phospholipase C-δ1. J. Biol. Chem. 269, 15846-15852.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15846-15852
    • Banno, Y.1    Okano, Y.2    Nozawa, Y.3
  • 38
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ
    • 38. Essen, L.O., Perisic, O., Cheung, R., Katan, M. & Williams, R.L. (1996) Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ. Nature 380, 595-602.
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 39
    • 0027979269 scopus 로고
    • Synthesis of a phosphatidylinositol 3,4,5-trisphosphate
    • 39. Watanabe, Y., Hirofuji, H. & Ozaki, S. (1994) Synthesis of a phosphatidylinositol 3,4,5-trisphosphate. Tetrahedron Lett. 35, 123-124.
    • (1994) Tetrahedron Lett. , vol.35 , pp. 123-124
    • Watanabe, Y.1    Hirofuji, H.2    Ozaki, S.3
  • 40
    • 0030039461 scopus 로고    scopus 로고
    • Regiospecific synthesis of 2,6- di-O-a-D-mannopyranosyl-phosphatidyl-D-myoinositol
    • 40. Watanabe, Y., Yamamoto, T. & Ozaki, S. (1996) Regiospecific synthesis of 2,6-di-O-a-D-mannopyranosyl-phosphatidyl-D-myoinositol. J. Org. Chem. 61, 14-15.
    • (1996) J. Org. Chem. , vol.61 , pp. 14-15
    • Watanabe, Y.1    Yamamoto, T.2    Ozaki, S.3
  • 42
    • 0029993517 scopus 로고    scopus 로고
    • Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation
    • 42. James, S.R., Downes, C.P., Gigg, R., Grove, S.J., Holmes, A.B. & Alessi, D.R. (1996) Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation. Biochem. J. 315, 709-713.
    • (1996) Biochem. J. , vol.315 , pp. 709-713
    • James, S.R.1    Downes, C.P.2    Gigg, R.3    Grove, S.J.4    Holmes, A.B.5    Alessi, D.R.6
  • 43
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of the Akt proto-oncogene product by phosphatidylinositol 3,4- bisphosphate
    • 43. Franke, T.F., Kaplan, D.R., Cantley, L.C. & Toker, A. (1997) Direct regulation of the Akt proto-oncogene product by phosphatidylinositol 3,4-bisphosphate. Science 275, 665-668.
    • (1997) Science , vol.275 , pp. 665-668
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 44
    • 0030991386 scopus 로고    scopus 로고
    • High affinity binding of inositol phosphates and phosphoinositides to the pleckstrin homology domain of RAC/protein kinase B and their influence on kinase activity
    • 44. Frech, M., Andjelkovic, M., Ingley, E., Reddy, K.K., Falck, J.R. & Hemmings, B.A. (1997) High affinity binding of inositol phosphates and phosphoinositides to the pleckstrin homology domain of RAC/protein kinase B and their influence on kinase activity. J. Biol. Chem. 272, 8474-8481.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8474-8481
    • Frech, M.1    Andjelkovic, M.2    Ingley, E.3    Reddy, K.K.4    Falck, J.R.5    Hemmings, B.A.6
  • 46
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylkinositol 4,5-bisphosphate
    • 46. Harlan, J.E., Hajduk, P.J., Yoon, H.S. & Fesik, S.W. (1994) Pleckstrin homology domains bind to phosphatidylkinositol 4,5-bisphosphate. Nature 371, 168-170.
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 47
    • 0032499031 scopus 로고    scopus 로고
    • Insulin-dependent translocation of ARNO to the plasma membrane of adipocytes requires phosphatidylinositol 3-kinase
    • 47. Venkateswarlu, K., Oatey, P.B., Tavare, J.M. & Cullen, P.J. (1998) Insulin-dependent translocation of ARNO to the plasma membrane of adipocytes requires phosphatidylinositol 3-kinase. Curr. Biol. 8, 463-466.
    • (1998) Curr. Biol. , vol.8 , pp. 463-466
    • Venkateswarlu, K.1    Oatey, P.B.2    Tavare, J.M.3    Cullen, P.J.4
  • 49
    • 15144349594 scopus 로고    scopus 로고
    • High affinity binding of the pleckstrin homology domain of mSos1 to phosphatidylinositol (4,5)-bisphosphate
    • 49. Kubieseski, T.J., Chook, Y.M., Parris, W.E., Rozakis-Adcock, M. & Pawson, T. (1997) High affinity binding of the pleckstrin homology domain of mSos1 to phosphatidylinositol (4,5)-bisphosphate. J. Biol. Chem. 272, 1799-1804.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1799-1804
    • Kubieseski, T.J.1    Chook, Y.M.2    Parris, W.E.3    Rozakis-Adcock, M.4    Pawson, T.5
  • 50
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: Structural and functional diversity
    • 50. Nalefski, E.A. & Falke, J.J. (1996) The C2 domain calcium-binding motif: structural and functional diversity. Protein Sci. 5, 2375-2390.
    • (1996) Protein Sci. , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 53
    • 0032558834 scopus 로고    scopus 로고
    • The G protein alpha12 stimulates Bruton's tyrosine kinase and a rasGAP through a conserved PH/BM domain
    • 53. Jiang, Y., Ma, W., Wan, Y., Kozaka, T., Hattori, S. & Huang, X.Y. (1998) The G protein alpha12 stimulates Bruton's tyrosine kinase and a rasGAP through a conserved PH/BM domain. Nature 395, 808-813.
    • (1998) Nature , vol.395 , pp. 808-813
    • Jiang, Y.1    Ma, W.2    Wan, Y.3    Kozaka, T.4    Hattori, S.5    Huang, X.Y.6
  • 55
    • 0032189381 scopus 로고    scopus 로고
    • Protein kinase B (c-Akt): A multifunctional mediator of phosphatidylinositol 3-kinase activation
    • 55. Coffer, P.J. & Woodgett, J.R. (1998) Protein kinase B (c-Akt): a multifunctional mediator of phosphatidylinositol 3-kinase activation. Biochem. J. 335, 1-13.
    • (1998) Biochem. J. , vol.335 , pp. 1-13
    • Coffer, P.J.1    Woodgett, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.