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Volumn 1804, Issue 3, 2010, Pages 533-540

Somatic mutations in PI3Kα: Structural basis for enzyme activation and drug design

Author keywords

Gain of function; H1047R mutant; p110 p85; PI3K; Somatic mutation

Indexed keywords

1 (1 CYANO 1 METHYLETHYL) 3 METHYL 8 (3 QUINOLINYL)IMIDAZO[4,5 C]QUINOLIN 2(1H,3H) ONE; 2 MORPHOLINO 8 PHENYLCHROMONE; 4 DIALLYLAMINOMETHYLENE 1,3,4,7,10,11,12,13,14,15,16,17 DODECAHYDRO 6 HYDROXY 1 METHOXYMETHYL 10,13 DIMETHYL 3,7,17 TRIOXO 2 OXACYCLOPENTA[A]PHENANTHREN 11 YL ACETATE; 5 (6 QUINOXALINYLMETHYLENE) 2,4 THIAZOLIDINEDIONE; 5 [5 (4 FLUORO 2 HYDROXYPHENYL)FURFURYLIDENE] 2,4 THIAZOLIDINEDIONE; [1 (4 OXO 8 PHENYL 4H 1 BENZOPYRAN 2 YL)MORPHOLINIO]METHOXYSUCCINYLARGINYLGLYCYLASPARTYLSERINE ACETATE; CAL 101; HYDROGEN SULFITE REDUCTASE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3 KINASE ALPHA; PHOSPHATIDYLINOSITOL 3 KINASE INHIBITOR; PHOSPHOTRANSFERASE; PROTEIN P110; UNCLASSIFIED DRUG; WORTMANNIN; ANTINEOPLASTIC AGENT; ENZYME INHIBITOR; ISOENZYME;

EID: 75349088737     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.11.020     Document Type: Review
Times cited : (17)

References (53)
  • 1
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley L.C. The phosphoinositide 3-kinase pathway. Science 296 (2002) 1655-1657
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 2
    • 0033104502 scopus 로고    scopus 로고
    • Autophosphorylation of p110delta phosphoinositide 3-kinase: a new paradigm for the regulation of lipid kinases in vitro and in vivo
    • Vanhaesebroeck B., Higashi K., Raven C., Welham M., Anderson S., Brennan P., Ward S.G., and Waterfield M.D. Autophosphorylation of p110delta phosphoinositide 3-kinase: a new paradigm for the regulation of lipid kinases in vitro and in vivo. Embo J. 18 (1999) 1292-1302
    • (1999) Embo J. , vol.18 , pp. 1292-1302
    • Vanhaesebroeck, B.1    Higashi, K.2    Raven, C.3    Welham, M.4    Anderson, S.5    Brennan, P.6    Ward, S.G.7    Waterfield, M.D.8
  • 4
    • 0034653608 scopus 로고    scopus 로고
    • The PI3K-PDK1 connection: more than just a road to PKB
    • Vanhaesebroeck B., and Alessi D.R. The PI3K-PDK1 connection: more than just a road to PKB. Biochem. J. 346 Pt. 3 (2000) 561-576
    • (2000) Biochem. J. , vol.346 , Issue.PART 3 , pp. 561-576
    • Vanhaesebroeck, B.1    Alessi, D.R.2
  • 5
    • 0033604577 scopus 로고    scopus 로고
    • Signaling by distinct classes of phosphoinositide 3-kinases
    • Vanhaesebroeck B., and Waterfield M.D. Signaling by distinct classes of phosphoinositide 3-kinases. Exp. Cell Res. 253 (1999) 239-254
    • (1999) Exp. Cell Res. , vol.253 , pp. 239-254
    • Vanhaesebroeck, B.1    Waterfield, M.D.2
  • 6
    • 0035190026 scopus 로고    scopus 로고
    • Cellular function of phosphoinositide 3-kinases: implications for development, homeostasis, and cancer
    • Katso R., Okkenhaug K., Ahmadi K., White S., Timms J., and Waterfield M.D. Cellular function of phosphoinositide 3-kinases: implications for development, homeostasis, and cancer. Annu. Rev. Cell Dev. Biol. 17 (2001) 615-675
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 615-675
    • Katso, R.1    Okkenhaug, K.2    Ahmadi, K.3    White, S.4    Timms, J.5    Waterfield, M.D.6
  • 10
    • 75349093632 scopus 로고    scopus 로고
    • http://www.sanger.ac.uk/perl/genetics/CGP/cosmic?action=bygene&ln=PIK3CA&start=1&end=1069&coords=AA:AA.
  • 11
    • 40649096375 scopus 로고    scopus 로고
    • Helical domain and kinase domain mutations in p110alpha of phosphatidylinositol 3-kinase induce gain of function by different mechanisms
    • Zhao L., and Vogt P.K. Helical domain and kinase domain mutations in p110alpha of phosphatidylinositol 3-kinase induce gain of function by different mechanisms. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 2652-2657
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 2652-2657
    • Zhao, L.1    Vogt, P.K.2
  • 12
    • 38649090091 scopus 로고    scopus 로고
    • PIK3CA mutations in the kinase domain (exon 20) of uterine endometrial adenocarcinomas are associated with adverse prognostic parameters.
    • Catasus L., Gallardo A., Cuatrecasas M., and Prat J. PIK3CA mutations in the kinase domain (exon 20) of uterine endometrial adenocarcinomas are associated with adverse prognostic parameters. Mod. Pathol. 21 (2008) 131-139
    • (2008) Mod. Pathol. , vol.21 , pp. 131-139
    • Catasus, L.1    Gallardo, A.2    Cuatrecasas, M.3    Prat, J.4
  • 14
    • 40549113364 scopus 로고    scopus 로고
    • PIK3CA exon 20 mutation is independently associated with a poor prognosis in breast cancer patients.
    • Lai Y., Mau B., Cheng W., Chen H., Chiu H., and Tzen C. PIK3CA exon 20 mutation is independently associated with a poor prognosis in breast cancer patients. Ann. Surg. Oncol. 15 (2008) 1064-1069
    • (2008) Ann. Surg. Oncol. , vol.15 , pp. 1064-1069
    • Lai, Y.1    Mau, B.2    Cheng, W.3    Chen, H.4    Chiu, H.5    Tzen, C.6
  • 18
    • 0029957987 scopus 로고    scopus 로고
    • Crystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85 alpha subunit
    • Musacchio A., Cantley L.C., and Harrison S.C. Crystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85 alpha subunit. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 14373-14378
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 14373-14378
    • Musacchio, A.1    Cantley, L.C.2    Harrison, S.C.3
  • 20
    • 0029878266 scopus 로고    scopus 로고
    • Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes.
    • Nolte R., Eck M., Schlessinger J., Shoelson S., and Harrison S. Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes. Nat. Struct. Biol. 3 (1996) 364-374
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 364-374
    • Nolte, R.1    Eck, M.2    Schlessinger, J.3    Shoelson, S.4    Harrison, S.5
  • 22
    • 0033581886 scopus 로고    scopus 로고
    • Structural insights into phosphoinositide 3-kinase catalysis and signalling
    • Walker E.H., Perisic O., Ried C., Stephens L., and Williams R.L. Structural insights into phosphoinositide 3-kinase catalysis and signalling. Nature 402 (1999) 313-320
    • (1999) Nature , vol.402 , pp. 313-320
    • Walker, E.H.1    Perisic, O.2    Ried, C.3    Stephens, L.4    Williams, R.L.5
  • 26
    • 0033063429 scopus 로고    scopus 로고
    • Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor
    • Schindler T., Sicheri F., Pico A., Gazit A., Levitzki A., and Kuriyan J. Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor. Mol. Cell 3 (1999) 639-648
    • (1999) Mol. Cell , vol.3 , pp. 639-648
    • Schindler, T.1    Sicheri, F.2    Pico, A.3    Gazit, A.4    Levitzki, A.5    Kuriyan, J.6
  • 29
    • 0035877577 scopus 로고    scopus 로고
    • Activation loop sequences confer substrate specificity to phosphoinositide 3-kinase alpha (PI3Kalpha). Functions of lipid kinase-deficient PI3Kalpha in signaling
    • Pirola L., Zvelebil M.J., Bulgarelli-Leva G., Van Obberghen E., Waterfield M.D., and Wymann M.P. Activation loop sequences confer substrate specificity to phosphoinositide 3-kinase alpha (PI3Kalpha). Functions of lipid kinase-deficient PI3Kalpha in signaling. J. Biol. Chem. 276 (2001) 21544-21554
    • (2001) J. Biol. Chem. , vol.276 , pp. 21544-21554
    • Pirola, L.1    Zvelebil, M.J.2    Bulgarelli-Leva, G.3    Van Obberghen, E.4    Waterfield, M.D.5    Wymann, M.P.6
  • 31
    • 66149100073 scopus 로고    scopus 로고
    • PIK3CA somatic mutations in breast cancer: Mechanistic insights from Langevin dynamics simulations
    • Mankoo P.K., Sukumar S., and Karchin R. PIK3CA somatic mutations in breast cancer: Mechanistic insights from Langevin dynamics simulations. Proteins 75 (2009) 499-508
    • (2009) Proteins , vol.75 , pp. 499-508
    • Mankoo, P.K.1    Sukumar, S.2    Karchin, R.3
  • 33
    • 54549108740 scopus 로고    scopus 로고
    • Network, Comprehensive genomic characterization defines human glioblastoma genes and core pathways
    • Cancer G.A.R. Network, Comprehensive genomic characterization defines human glioblastoma genes and core pathways. Nature 455 (2008) 1061-1068
    • (2008) Nature , vol.455 , pp. 1061-1068
    • Cancer, G.A.R.1
  • 36
    • 3142679468 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of synthetic viridins derived from C(20)-heteroalkylation of the steroidal PI-3-kinase inhibitor wortmannin
    • Wipf P., Minion D.J., Halter R.J., Berggren M.I., Ho C.B., Chiang G.G., Kirkpatrick L., Abraham R., and Powis G. Synthesis and biological evaluation of synthetic viridins derived from C(20)-heteroalkylation of the steroidal PI-3-kinase inhibitor wortmannin. Org. Biomol. Chem. 2 (2004) 1911-1920
    • (2004) Org. Biomol. Chem. , vol.2 , pp. 1911-1920
    • Wipf, P.1    Minion, D.J.2    Halter, R.J.3    Berggren, M.I.4    Ho, C.B.5    Chiang, G.G.6    Kirkpatrick, L.7    Abraham, R.8    Powis, G.9
  • 37
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002)
    • Vlahos C.J., Matter W.F., Hui K.Y., and Brown R.F. A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002). J. Biol. Chem. 269 (1994) 5241-5248
    • (1994) J. Biol. Chem. , vol.269 , pp. 5241-5248
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.Y.3    Brown, R.F.4
  • 41
    • 0033634827 scopus 로고    scopus 로고
    • Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine
    • Walker E.H., Pacold M.E., Perisic O., Stephens L., Hawkins P.T., Wymann M.P., and Williams R.L. Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine. Mol. Cell 6 (2000) 909-919
    • (2000) Mol. Cell , vol.6 , pp. 909-919
    • Walker, E.H.1    Pacold, M.E.2    Perisic, O.3    Stephens, L.4    Hawkins, P.T.5    Wymann, M.P.6    Williams, R.L.7
  • 43
    • 0027191192 scopus 로고
    • Solution structure and ligand-binding site of the SH3 domain of the p85 alpha subunit of phosphatidylinositol 3-kinase
    • Booker G.W., Gout I., Downing A.K., Driscoll P.C., Boyd J., Waterfield M.D., and Campbell I.D. Solution structure and ligand-binding site of the SH3 domain of the p85 alpha subunit of phosphatidylinositol 3-kinase. Cell 73 (1993) 813-822
    • (1993) Cell , vol.73 , pp. 813-822
    • Booker, G.W.1    Gout, I.2    Downing, A.K.3    Driscoll, P.C.4    Boyd, J.5    Waterfield, M.D.6    Campbell, I.D.7
  • 44
    • 0141791276 scopus 로고    scopus 로고
    • Nuclear magnetic resonance structure of the P395S mutant of the N-SH2 domain of the p85 subunit of PI3 kinase: an SH2 domain with altered specificity
    • Gunther U.L., Weyrauch B., Zhang X., and Schaffhausen B. Nuclear magnetic resonance structure of the P395S mutant of the N-SH2 domain of the p85 subunit of PI3 kinase: an SH2 domain with altered specificity. Biochemistry 42 (2003) 11120-11127
    • (2003) Biochemistry , vol.42 , pp. 11120-11127
    • Gunther, U.L.1    Weyrauch, B.2    Zhang, X.3    Schaffhausen, B.4
  • 45
    • 0033214182 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal SH2 domain of the p85alpha regulatory subunit of phosphoinositide 3-kinase: an SH2 domain mimicking its own substrate
    • Hoedemaeker F.J., Siegal G., Roe S.M., Driscoll P.C., and Abrahams J.P. Crystal structure of the C-terminal SH2 domain of the p85alpha regulatory subunit of phosphoinositide 3-kinase: an SH2 domain mimicking its own substrate. J. Mol. Biol. 292 (1999) 763-770
    • (1999) J. Mol. Biol. , vol.292 , pp. 763-770
    • Hoedemaeker, F.J.1    Siegal, G.2    Roe, S.M.3    Driscoll, P.C.4    Abrahams, J.P.5
  • 47
    • 0029894672 scopus 로고    scopus 로고
    • Structure of a specific peptide complex of the carboxy-terminal SH2 domain from the p85 alpha subunit of phosphatidylinositol 3-kinase
    • Breeze A.L., Kara B.V., Barratt D.G., Anderson M., Smith J.C., Luke R.W., Best J.R., and Cartlidge S.A. Structure of a specific peptide complex of the carboxy-terminal SH2 domain from the p85 alpha subunit of phosphatidylinositol 3-kinase. EMBO J. 15 (1996) 3579-3589
    • (1996) EMBO J. , vol.15 , pp. 3579-3589
    • Breeze, A.L.1    Kara, B.V.2    Barratt, D.G.3    Anderson, M.4    Smith, J.C.5    Luke, R.W.6    Best, J.R.7    Cartlidge, S.A.8
  • 52
    • 44649150564 scopus 로고    scopus 로고
    • Structure-based design of an organoruthenium phosphatidyl-inositol-3-kinase inhibitor reveals a switch governing lipid kinase potency and selectivity
    • Xie P., Williams D.S., Atilla-Gokcumen G.E., Milk L., Xiao M., Smalley K.S., Herlyn M., Meggers E., and Marmorstein R. Structure-based design of an organoruthenium phosphatidyl-inositol-3-kinase inhibitor reveals a switch governing lipid kinase potency and selectivity. ACS Chem. Biol. 3 (2008) 305-316
    • (2008) ACS Chem. Biol. , vol.3 , pp. 305-316
    • Xie, P.1    Williams, D.S.2    Atilla-Gokcumen, G.E.3    Milk, L.4    Xiao, M.5    Smalley, K.S.6    Herlyn, M.7    Meggers, E.8    Marmorstein, R.9


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