메뉴 건너뛰기




Volumn 15, Issue 22, 1996, Pages 6241-6250

Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase

Author keywords

Bruton's tyrosine kinase; Dynamin; PH domain; Phosphoinositides; Surface plasmon resonance

Indexed keywords

DYNAMIN; GUANOSINE TRIPHOSPHATASE; INOSITOL POLYPHOSPHATE; LIPOSOME; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PLECKSTRIN; PROTEIN TYROSINE KINASE;

EID: 10544219605     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb01014.x     Document Type: Article
Times cited : (504)

References (55)
  • 1
    • 0029055503 scopus 로고
    • Pleckstrin inhibits phosphoinositide hydrolysis initiated by G-protein-coupled and growth factor receptors. A role for pleckstrin's PH domains
    • Abrams, C.S., Wu, H., Zhao, W., Belmonte, E., White, D. and Brass, L.F. (1995) Pleckstrin inhibits phosphoinositide hydrolysis initiated by G-protein-coupled and growth factor receptors. A role for pleckstrin's PH domains. J. Biol. Chem., 270, 14485-14492.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14485-14492
    • Abrams, C.S.1    Wu, H.2    Zhao, W.3    Belmonte, E.4    White, D.5    Brass, L.F.6
  • 3
    • 0028902269 scopus 로고
    • Insights into lymphocyte development from X-linked immune deficiencies
    • Belmont, J.W. (1995) Insights into lymphocyte development from X-linked immune deficiencies. Trends Genet., 11, 112-116.
    • (1995) Trends Genet. , vol.11 , pp. 112-116
    • Belmont, J.W.1
  • 4
    • 45449126184 scopus 로고
    • Toward complete H-1-NMR spectra in proteins
    • Brown, S.C., Weber, P.L. and Mueller, L. (1988) Toward complete H-1-NMR spectra in proteins. J. Magn. Reson., 77, 166-169.
    • (1988) J. Magn. Reson. , vol.77 , pp. 166-169
    • Brown, S.C.1    Weber, P.L.2    Mueller, L.3
  • 5
    • 0029160069 scopus 로고
    • Protein kinase B (c-AKT) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering, B.M.T. and Coffer, P.J. (1995) Protein kinase B (c-AKT) in phosphatidylinositol-3-OH kinase signal transduction. Nature, 17, 599-602.
    • (1995) Nature , vol.17 , pp. 599-602
    • Burgering, B.M.T.1    Coffer, P.J.2
  • 7
    • 0028063861 scopus 로고
    • Mutation analysis of the Bruton's tyrosine kinase gene in X-linked agammaglobulinemia: Identification of a mutation which affects the same codon as is altered in immunodeficient xid mice
    • deWeers, M., Mensink, R.G.J., Kraakman, M.E.M., Schuurman, R.K.B. and Hendriks, R.W. (1994) Mutation analysis of the Bruton's tyrosine kinase gene in X-linked agammaglobulinemia: identification of a mutation which affects the same codon as is altered in immunodeficient xid mice. Hum. Mol. Genet., 3, 161-166.
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 161-166
    • DeWeers, M.1    Mensink, R.G.J.2    Kraakman, M.E.M.3    Schuurman, R.K.B.4    Hendriks, R.W.5
  • 9
    • 0030010590 scopus 로고    scopus 로고
    • Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor
    • Eck, M.J., Dhe-Paganon, S., Trub, J., Nolte, R.T. and Shoelson, S.E. (1996) Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor. Cell, 85, 695-705.
    • (1996) Cell , vol.85 , pp. 695-705
    • Eck, M.J.1    Dhe-Paganon, S.2    Trub, J.3    Nolte, R.T.4    Shoelson, S.E.5
  • 10
    • 0027945789 scopus 로고
    • Crystal structure at 2.2 Å resolution of the pleckstrin homology domain from human dynamin
    • Ferguson, K.M., Lemmon, M.A., Schlessinger, J. and Cowburn, D. (1994) Crystal structure at 2.2 Å resolution of the pleckstrin homology domain from human dynamin. Cell, 79, 199-209.
    • (1994) Cell , vol.79 , pp. 199-209
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Cowburn, D.4
  • 11
    • 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. (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    Schlessinger, J.3    Sigler, P.B.4
  • 12
    • 0029079275 scopus 로고
    • The protein kinase encoded by the AKT proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
    • Franke, T.F., Yang, S., Chan, T.O., Datta, K., Kazlauskas, A., Morrison, D.K., Kaplan, D.R. and Tsichlis, P.N. (1995) The protein kinase encoded by the AKT proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell, 81, 727-738.
    • (1995) Cell , vol.81 , pp. 727-738
    • Franke, T.F.1    Yang, S.2    Chan, T.O.3    Datta, K.4    Kazlauskas, A.5    Morrison, D.K.6    Kaplan, D.R.7    Tsichlis, P.N.8
  • 13
    • 0028836020 scopus 로고
    • Solution structure of pleckstrin homology domain of dynamin by heteronuclear NMR spectroscopy
    • Fushman, D., Cahill, S., Lemmon, M.A., Schlessinger, J. and Cowburn, D. (1995) Solution structure of pleckstrin homology domain of dynamin by heteronuclear NMR spectroscopy. Proc. Natl Acad. Sci. USA, 92, 816-820.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 816-820
    • Fushman, D.1    Cahill, S.2    Lemmon, M.A.3    Schlessinger, J.4    Cowburn, D.5
  • 14
    • 0027362241 scopus 로고
    • The GTPase dynamin binds to and is activated by a subset of SH3 domains
    • Gout, J. et al. (1993) The GTPase dynamin binds to and is activated by a subset of SH3 domains. Cell, 75, 25-36.
    • (1993) Cell , vol.75 , pp. 25-36
    • Gout, J.1
  • 15
    • 0000088628 scopus 로고
    • Processing of multidimensional NMR data with the new software PROSA
    • Guntert, P., Dotsch, V., Wider, G. and Wuthrich, K. (1992) Processing of multidimensional NMR data with the new software PROSA. J. Biomol. NMK, 2, 619-629.
    • (1992) J. Biomol. NMK , vol.2 , pp. 619-629
    • Guntert, P.1    Dotsch, V.2    Wider, G.3    Wuthrich, K.4
  • 16
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
    • Harlan, J.E., Hajduk, P.J., Yoon, H.S. and Fesik, S.W. (1994) Pleckstrin homology domains bind to phosphatidylinositol-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
  • 17
    • 0028898261 scopus 로고
    • Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding
    • Hinshaw, J.E. and Schmid, S.L. (1995) Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding. Nature, 374, 190-192.
    • (1995) Nature , vol.374 , pp. 190-192
    • Hinshaw, J.E.1    Schmid, S.L.2
  • 19
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K. and Pease, L.R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene, 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 21
    • 0029993517 scopus 로고    scopus 로고
    • Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation
    • James, S.R., Downes, P.C., Gigg, R., Grove, S.J.A., Holmes, A.B. and 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, P.C.2    Gigg, R.3    Grove, S.J.A.4    Holmes, A.B.5    Alessi, D.R.6
  • 23
    • 0028986998 scopus 로고
    • 2 hydrolysis and regulation of phospholipase C isozymes
    • 2 hydrolysis and regulation of phospholipase C isozymes. Curr. Opin. Cell Biol., 7, 183-189.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 183-189
    • Lee, S.B.1
  • 24
    • 0028874438 scopus 로고
    • Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain
    • Lemmon, M.A., Ferguson, K.M., O'Brian, R., Sigler, P.B. and Schlessinger, J. (1995) Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain. Proc. Natl Acad. Sci. USA, 92, 10472-10476.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10472-10476
    • Lemmon, M.A.1    Ferguson, K.M.2    O'Brian, R.3    Sigler, P.B.4    Schlessinger, J.5
  • 25
    • 0029939448 scopus 로고    scopus 로고
    • PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface
    • Lemmon, M.A., Ferguson, K.M. and 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, M.A.1    Ferguson, K.M.2    Schlessinger, J.3
  • 26
    • 0028805690 scopus 로고
    • Dynamin and endocytosis
    • Liu, J.-P. and Robinson, P.J. (1995) Dynamin and endocytosis. Endocr. Rev., 16, 590-607.
    • (1995) Endocr. Rev. , vol.16 , pp. 590-607
    • Liu, J.-P.1    Robinson, P.J.2
  • 28
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase-cycling. Application to the study of hydrogen exchange in proteins
    • Marion, D., Ikura, M., Tschudin, R. and Bax, A. (1989) Rapid recording of 2D NMR spectra without phase-cycling. Application to the study of hydrogen exchange in proteins. J. Magn. Reson., 85, 393-399.
    • (1989) J. Magn. Reson. , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 30
    • 0027361390 scopus 로고
    • Experimental NMR techniques for studies of protein-ligand interactions
    • Otting, G. (1993) Experimental NMR techniques for studies of protein-ligand interactions. Curr. Opin. Struct. Biol., 3, 760-768.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 760-768
    • Otting, G.1
  • 31
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson, T. (1995) Protein modules and signalling networks. Nature, 373, 573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 32
    • 49049123785 scopus 로고
    • A very mild method allowing the encapsulation of very high amounts of macromolecules into very large (1000 nm) unilamellar liposomes
    • Philippot, J., Mataftschiev, S. and Liautard, J.P. (1983) A very mild method allowing the encapsulation of very high amounts of macromolecules into very large (1000 nm) unilamellar liposomes. Biochim. Biophys. Acta, 734, 134-143.
    • (1983) Biochim. Biophys. Acta , vol.734 , pp. 134-143
    • Philippot, J.1    Mataftschiev, S.2    Liautard, J.P.3
  • 33
    • 0029039613 scopus 로고
    • Pleckstrin homology domain-mediated membrane association and activation of the β-adrenergic receptor kinase requires coordinate interaction with βγ subunits and lipid
    • Pitcher, J.A., Touhara, K., Payne, E.S. and Lefkowitz, R.J. (1995) Pleckstrin homology domain-mediated membrane association and activation of the β-adrenergic receptor kinase requires coordinate interaction with βγ subunits and lipid. J. Biol. Chem., 270, 11707-11710.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11707-11710
    • Pitcher, J.A.1    Touhara, K.2    Payne, E.S.3    Lefkowitz, R.J.4
  • 34
    • 0028892253 scopus 로고
    • Phosphatidylinositol (3,4,5)P3 interacts with SH2 domains and modulates PI 3-kinase association with tyrosine-phosphorylated proteins
    • Rameh, L.E., Chen, C.-S. and Cantley, L.C. (1995) Phosphatidylinositol (3,4,5)P3 interacts with SH2 domains and modulates PI 3-kinase association with tyrosine-phosphorylated proteins. Cell, 83, 821-830.
    • (1995) Cell , vol.83 , pp. 821-830
    • Rameh, L.E.1    Chen, C.-S.2    Cantley, L.C.3
  • 35
    • 0027305921 scopus 로고
    • Mutation of unique region of Bruton's tyrosine kinase in immunodeficient XID mice
    • Rawlings, D.J. et al. (1993) Mutation of unique region of Bruton's tyrosine kinase in immunodeficient XID mice. Science, 261, 358-361.
    • (1993) Science , vol.261 , pp. 358-361
    • Rawlings, D.J.1
  • 36
    • 13444269041 scopus 로고
    • Computer-optimized decoupling scheme for wideband applications and low-level operation
    • Shaka, A.J., Barke, P.B. and Freeman, R. (1985) Computer-optimized decoupling scheme for wideband applications and low-level operation. J. Magn. Reson., 64, 547-552.
    • (1985) J. Magn. Reson. , vol.64 , pp. 547-552
    • Shaka, A.J.1    Barke, P.B.2    Freeman, R.3
  • 37
    • 0030040967 scopus 로고    scopus 로고
    • The pleckstrin homology domain: An intriguing multifunctional protein module
    • Shaw, G. (1996) The pleckstrin homology domain: an intriguing multifunctional protein module. BioEssays, 18, 35-46.
    • (1996) BioEssays , vol.18 , pp. 35-46
    • Shaw, G.1
  • 38
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusion with glutathione S-transferase
    • Smith, D.B. and Johnson, K.S. (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusion with glutathione S-transferase. Gene, 67, 31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 39
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals
    • Takei, K., McPherson, P.S., Schmid, S.L. and DeCamilli, P. (1995) Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals. Nature, 374, 186-190.
    • (1995) Nature , vol.374 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    DeCamilli, P.4
  • 40
    • 0027261447 scopus 로고
    • Colocalization of X-linked agammaglobulinemia and X-linked immunodeficiency genes
    • Thomas, J.D., Sideras, P., Smith, C.I.E., Vorechovsky, I., Chapman, V. and Paul, W.E. (1993) Colocalization of X-linked agammaglobulinemia and X-linked immunodeficiency genes. Science, 261, 355-358.
    • (1993) Science , vol.261 , pp. 355-358
    • Thomas, J.D.1    Sideras, P.2    Smith, C.I.E.3    Vorechovsky, I.4    Chapman, V.5    Paul, W.E.6
  • 42
    • 0028246440 scopus 로고
    • Binding of G protein βγ-subunits to pleckstrin homology domains
    • Touhara, K., Inglese, J., Pitcher, J.A., Shaw, G. and 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
  • 43
    • 0028173394 scopus 로고
    • Binding of βγ-subunits of heterotrimeric G proteins to the PH domain of Bruton's tyrosine kinase
    • Tsukada, S., Simon, M.I., Witte, O.N. and Katz, A. (1994) Binding of βγ-subunits of heterotrimeric G proteins to the PH domain of Bruton's 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
  • 44
    • 0027217188 scopus 로고
    • Activation of dynamin GTPase by acidic phospholipids and endogenous rat brain vesicles
    • Tuma, P.L., Stachniak, M.C. and Collins, C.A. (1993) Activation of dynamin GTPase by acidic phospholipids and endogenous rat brain vesicles. J. Biol. Chem., 268, 17240-17246.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17240-17246
    • Tuma, P.L.1    Stachniak, M.C.2    Collins, C.A.3
  • 45
    • 0027448054 scopus 로고
    • The NMR determination of the IIA(mtl) binding site on HPr of the E.coli phosphoenol pyruvate-dependent phosphotransferase system
    • Van Nuland, N.A., Kroon, G.J., Dijkstra, K., Wolters, G.K., Scheek, R.M. and Robillard, G.T. (1993) The NMR determination of the IIA(mtl) binding site on HPr of the E.coli phosphoenol pyruvate-dependent phosphotransferase system. FEBS Lett., 315, 11-15.
    • (1993) FEBS Lett. , vol.315 , pp. 11-15
    • Van Nuland, N.A.1    Kroon, G.J.2    Dijkstra, K.3    Wolters, G.K.4    Scheek, R.M.5    Robillard, G.T.6
  • 48
    • 0001074233 scopus 로고
    • Practical aspects of recording multi-dimensional NMR-spectra in water with flat base lines
    • Waltho, J.P. and Cavanagh, J. (1993) Practical aspects of recording multi-dimensional NMR-spectra in water with flat base lines. J. Magn. Reson., 103, 338-348.
    • (1993) J. Magn. Reson. , vol.103 , pp. 338-348
    • Waltho, J.P.1    Cavanagh, J.2
  • 49
    • 0028958660 scopus 로고
    • Dynamin GTPase is stimulated by crosslinking through the C-terminal proline-rich domain
    • Warnock, D.E., Terlecky, L.J. and Schmid, S.L. (1995) Dynamin GTPase is stimulated by crosslinking through the C-terminal proline-rich domain. EMBO J., 14, 1322-1328.
    • (1995) EMBO J. , vol.14 , pp. 1322-1328
    • Warnock, D.E.1    Terlecky, L.J.2    Schmid, S.L.3
  • 52
    • 0028541866 scopus 로고
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J. Biomol. NMR, 4, 845-858.
    • (1994) J. Biomol. NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4
  • 53
    • 0029645869 scopus 로고
    • Solution structure of the pleckstrin homology domain of Drosophila β-spectrin
    • Zhang, P., Talluri, S., Deng, H., Branton, D. and Wagner, G. (1995) Solution structure of the pleckstrin homology domain of Drosophila β-spectrin. Curr. Biol. Struct., 15, 1185-1195.
    • (1995) Curr. Biol. Struct. , vol.15 , pp. 1185-1195
    • Zhang, P.1    Talluri, S.2    Deng, H.3    Branton, D.4    Wagner, G.5
  • 54
    • 0029978885 scopus 로고    scopus 로고
    • Identification of the binding site for acidic phospholipids on the PH domain of dynamin: Implications for stimulation of GTPase activity
    • Zheng, J., Cahill, S.M., Lemmon, M.A., Fushman, D., Schlessinger, J. and Cowburn, D. (1996) Identification of the binding site for acidic phospholipids on the PH domain of dynamin: implications for stimulation of GTPase activity. J. Mol. Biol., 255, 14-21.
    • (1996) J. Mol. Biol. , vol.255 , pp. 14-21
    • Zheng, J.1    Cahill, S.M.2    Lemmon, M.A.3    Fushman, D.4    Schlessinger, J.5    Cowburn, D.6
  • 55
    • 0028860968 scopus 로고
    • Structure and ligand recognition of the phosphotyrosine binding domain of Shc
    • Zhou, M.-M. et al. (1995) Structure and ligand recognition of the phosphotyrosine binding domain of Shc. Nature, 378, 584-592.
    • (1995) Nature , vol.378 , pp. 584-592
    • Zhou, M.-M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.