메뉴 건너뛰기




Volumn 47, Issue 47, 2008, Pages 12260-12269

Molecular mechanism of an oncogenic mutation that alters membrane targeting: Glu17Lys modifies the PIP lipid specificity of the AKT1 PH domain

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL CELL CULTURE; DISSOCIATION; MEMBRANES; MODULATION; PHOSPHOLIPIDS; PLASMAS; RATE CONSTANTS;

EID: 56749168073     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801683k     Document Type: Article
Times cited : (78)

References (39)
  • 3
    • 20544475665 scopus 로고    scopus 로고
    • Membrane-protein interactions in cell signaling and membrane trafficking
    • Cho, W., and Stahelin, R. V. (2005) Membrane-protein interactions in cell signaling and membrane trafficking. Annu. Rev. Biophys. Biomol. Struct. 34, 119-151.
    • (2005) Annu. Rev. Biophys. Biomol. Struct , vol.34 , pp. 119-151
    • Cho, W.1    Stahelin, R.V.2
  • 4
    • 0034663568 scopus 로고    scopus 로고
    • Signal-dependent membrane targeting by pleckstrin homology (PH) domains
    • Lemmon, M. A., and Ferguson, K. M. (2000) Signal-dependent membrane targeting by pleckstrin homology (PH) domains. Biochem. J. 350 (Part 1), 1-18.
    • (2000) Biochem. J , vol.350 , Issue.PART 1 , pp. 1-18
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 5
    • 0035313710 scopus 로고    scopus 로고
    • Subcellular targeting by membrane lipids
    • Hurley, J. H., and Meyer, T. (2001) Subcellular targeting by membrane lipids. Curr. Opin. Cell Biol. 13, 146-152.
    • (2001) Curr. Opin. Cell Biol , vol.13 , pp. 146-152
    • Hurley, J.H.1    Meyer, T.2
  • 7
    • 0025731596 scopus 로고
    • Pathway of phosphatidylinositol(3,4,5)-trisphosphate synthesis in activated neutrophils
    • Stephens, L. R., Hughes, K. T., and Irvine, R. F. (1991) Pathway of phosphatidylinositol(3,4,5)-trisphosphate synthesis in activated neutrophils. Nature 351, 33-39.
    • (1991) Nature , vol.351 , pp. 33-39
    • Stephens, L.R.1    Hughes, K.T.2    Irvine, R.F.3
  • 8
    • 0032530384 scopus 로고    scopus 로고
    • Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast
    • Isakoff, S. J., Cardozo, T., Andreev, J., Li, Z., Ferguson, K. M., Abagyan, R., Lemmon, M. A., Aronheim, A., and Skolnik, E. Y. (1998) Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast. EMBO J. 17, 5374-5387.
    • (1998) EMBO J , vol.17 , pp. 5374-5387
    • Isakoff, S.J.1    Cardozo, T.2    Andreev, J.3    Li, Z.4    Ferguson, K.M.5    Abagyan, R.6    Lemmon, M.A.7    Aronheim, A.8    Skolnik, E.Y.9
  • 9
    • 84872115717 scopus 로고    scopus 로고
    • Pleckstrin homology (PH) domains and phosphoinositides
    • Lemmon, M. A. (2007) Pleckstrin homology (PH) domains and phosphoinositides. Biochem. Soc. Symp., 81-93.
    • (2007) Biochem. Soc. Symp , pp. 81-93
    • Lemmon, M.A.1
  • 10
    • 0034872365 scopus 로고    scopus 로고
    • Molecular determinants in pleckstrin homology domains that allow specific recognition of phosphoinositides
    • Lemmon, M. A., and Ferguson, K. M. (2001) Molecular determinants in pleckstrin homology domains that allow specific recognition of phosphoinositides. Biochem. Soc. Trans. 29, 377-384.
    • (2001) Biochem. Soc. Trans , vol.29 , pp. 377-384
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 13
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: Navigating downstream
    • Manning, B. D., and Cantley, L. C. (2007) AKT/PKB signaling: Navigating downstream. Cell 129, 1261-1274.
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 14
    • 0033551070 scopus 로고    scopus 로고
    • New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway
    • Cantley, L. C., and Neel, B. G. (1999) New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway. Proc. Natl. Acad. Sci. U.S.A. 96, 4240-4245.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 4240-4245
    • Cantley, L.C.1    Neel, B.G.2
  • 18
    • 0037102153 scopus 로고    scopus 로고
    • High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site
    • Biondi, R. M., Komander, D., Thomas, C. C., Lizcano, J. M., Deak, M., Alessi, D. R., and van Aalten, D. M. (2002) High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site. EMBO J. 21, 4219-4228.
    • (2002) EMBO J , vol.21 , pp. 4219-4228
    • Biondi, R.M.1    Komander, D.2    Thomas, C.C.3    Lizcano, J.M.4    Deak, M.5    Alessi, D.R.6    van Aalten, D.M.7
  • 19
    • 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
    • Frech, M., Andjelkovic, M., Ingley, E., Reddy, K. K., Falck, J. R., and 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
  • 20
    • 15644381754 scopus 로고    scopus 로고
    • Andjelkovic, M., Alessi, D. R., Meier, R., Fernandez, A., Lamb, N. J., Freeh, M., Cron, P., Cohen, P., Lucocq, J. M., and Hemmings, B. A. (1997) Role of translocation in the activation and function of protein kinase B. J. Biol. Chem. 272, 31515-31524.
    • Andjelkovic, M., Alessi, D. R., Meier, R., Fernandez, A., Lamb, N. J., Freeh, M., Cron, P., Cohen, P., Lucocq, J. M., and Hemmings, B. A. (1997) Role of translocation in the activation and function of protein kinase B. J. Biol. Chem. 272, 31515-31524.
  • 22
    • 0031127305 scopus 로고    scopus 로고
    • Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα
    • Alessi, D. R., James, S. R., Downes, C. P., Holmes, A. B., Gaffney, P. R., Reese, C. B., and Cohen, P. (1997) Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα. Curr. Biol. 7, 261-269.
    • (1997) Curr. Biol , vol.7 , pp. 261-269
    • Alessi, D.R.1    James, S.R.2    Downes, C.P.3    Holmes, A.B.4    Gaffney, P.R.5    Reese, C.B.6    Cohen, P.7
  • 23
    • 0032482374 scopus 로고    scopus 로고
    • Translocation of PDK-1 to the plasma membrane is important in allowing PDK-1 to activate protein kinase B
    • Anderson, K. E., Coadwell, J., Stephens, L. R., and Hawkins, P. T. (1998) Translocation of PDK-1 to the plasma membrane is important in allowing PDK-1 to activate protein kinase B. Curr. Biol. 8, 684-691.
    • (1998) Curr. Biol , vol.8 , pp. 684-691
    • Anderson, K.E.1    Coadwell, J.2    Stephens, L.R.3    Hawkins, P.T.4
  • 25
    • 0028787055 scopus 로고
    • The pleckstrin homology domain of phospholipase C-δ1 binds with high affinity to phosphatidylinositol 4,5-bisphosphate in bilayer membranes
    • Garcia, P., Gupta, R., Shah, S., Morris, A. J., Rudge, S. A., Scarlata, S., Petrova, V., McLaughlin, S., and 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    Morris, A.J.4    Rudge, S.A.5    Scarlata, S.6    Petrova, V.7    McLaughlin, S.8    Rebecchi, M.J.9
  • 26
    • 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
  • 27
    • 11144292734 scopus 로고    scopus 로고
    • GRP1 pleckstrin homology domain: Activation parameters and novel search mechanism for rare target lipid
    • Corbin, J. A., Dirkx, R. A., and Falke, J. J. (2004) GRP1 pleckstrin homology domain: Activation parameters and novel search mechanism for rare target lipid. Biochemistry 43, 16161-16173.
    • (2004) Biochemistry , vol.43 , pp. 16161-16173
    • Corbin, J.A.1    Dirkx, R.A.2    Falke, J.J.3
  • 28
    • 36049032519 scopus 로고    scopus 로고
    • 2+ influx is an essential component of the positive-feedback loop that maintains leading-edge structure and activity in macrophages
    • 2+ influx is an essential component of the positive-feedback loop that maintains leading-edge structure and activity in macrophages. Proc. Natl. Acad. Sci. U.S.A. 104, 16176-16181.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 16176-16181
    • Evans, J.H.1    Falke, J.J.2
  • 29
    • 33748333139 scopus 로고    scopus 로고
    • Live cell imaging of phosphoinositide dynamics with fluorescent protein domains
    • Varnai, P., and Balla, T. (2006) Live cell imaging of phosphoinositide dynamics with fluorescent protein domains. Biochim. Biophys. Acta 1761, 957-967.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 957-967
    • Varnai, P.1    Balla, T.2
  • 30
    • 0034635513 scopus 로고    scopus 로고
    • Polarization of chemoattractant receptor signaling during neutrophil Chemotaxis
    • Servant, G., Weiner, O. D., Herzmark, P., Balla, T., Sedat, J. W., and Bourne, H. R. (2000) Polarization of chemoattractant receptor signaling during neutrophil Chemotaxis. Science 287, 1037-1040.
    • (2000) Science , vol.287 , pp. 1037-1040
    • Servant, G.1    Weiner, O.D.2    Herzmark, P.3    Balla, T.4    Sedat, J.W.5    Bourne, H.R.6
  • 31
    • 0032510323 scopus 로고    scopus 로고
    • Receptor-induced transient reduction in plasma membrane PtdIns(4,5)P2 concentration monitored in living cells
    • Stauffer, T. P., Ahn, S., and Meyer, T. (1998) Receptor-induced transient reduction in plasma membrane PtdIns(4,5)P2 concentration monitored in living cells. Curr. Biol. 8, 343-346.
    • (1998) Curr. Biol , vol.8 , pp. 343-346
    • Stauffer, T.P.1    Ahn, S.2    Meyer, T.3
  • 32
    • 0035805510 scopus 로고    scopus 로고
    • Monitoring agonist-induced phospholipase C activation in live cells by fluorescence resonance energy transfer
    • van der Wal, J., Habets, R., Varnai, P., Balla, T., and Jalink, K. (2001) Monitoring agonist-induced phospholipase C activation in live cells by fluorescence resonance energy transfer. J. Biol. Chem. 276, 15337-15344.
    • (2001) J. Biol. Chem , vol.276 , pp. 15337-15344
    • van der Wal, J.1    Habets, R.2    Varnai, P.3    Balla, T.4    Jalink, K.5
  • 33
    • 0041510168 scopus 로고    scopus 로고
    • Molecular modeling of the membrane targeting of phospholipase C pleckstrin homology domains
    • Singh, S. M., and Murray, D. (2003) Molecular modeling of the membrane targeting of phospholipase C pleckstrin homology domains. Protein Sci. 12, 1934-1953.
    • (2003) Protein Sci , vol.12 , pp. 1934-1953
    • Singh, S.M.1    Murray, D.2
  • 35
    • 44949238672 scopus 로고    scopus 로고
    • Diffusion Coefficient of Fluorescent Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane of Cells
    • Golebiewska, U., Nyako, M., Woturski, W., Zaitseva, I., and McLaughlin, S. (2008) Diffusion Coefficient of Fluorescent Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane of Cells. Mol. Biol. Cell 19, 1663-1669.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1663-1669
    • Golebiewska, U.1    Nyako, M.2    Woturski, W.3    Zaitseva, I.4    McLaughlin, S.5
  • 38
    • 0345561543 scopus 로고    scopus 로고
    • Phosphatidylinositol-3- kinase dependent membrane association of the Bruton's tyrosine kinase pleckstrin homology domain visualized in single living cells
    • Varnai, P., Rother, K. I., and Balla, T. (1999) Phosphatidylinositol-3- kinase dependent membrane association of the Bruton's tyrosine kinase pleckstrin homology domain visualized in single living cells. J. Biol. Chem. 274, 10983-10989.
    • (1999) J. Biol. Chem , vol.274 , pp. 10983-10989
    • Varnai, P.1    Rother, K.I.2    Balla, T.3
  • 39
    • 1242263882 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of the pleckstrin homology domain of the human protein kinase B (PKB/Akt). Interaction with inositol phosphates
    • Augin, D., Barthe, P., Auge-Senegas, M. T., Stern, M. H., Noguchi, M., and Roumestand, C. (2004) Solution structure and backbone dynamics of the pleckstrin homology domain of the human protein kinase B (PKB/Akt). Interaction with inositol phosphates. J. Biomol. NMR 28, 135-155.
    • (2004) J. Biomol. NMR , vol.28 , pp. 135-155
    • Augin, D.1    Barthe, P.2    Auge-Senegas, M.T.3    Stern, M.H.4    Noguchi, M.5    Roumestand, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.