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Volumn 139, Issue 2, 1997, Pages 339-349

Phosphatidylinositol 3-kinase is required for the formation of constitutive transport vesicles from the TGN

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; IMMUNOGLOBULIN A; IMMUNOGLOBULIN RECEPTOR; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOPROTEIN; WORTMANNIN;

EID: 0030720512     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.139.2.339     Document Type: Article
Times cited : (78)

References (64)
  • 3
    • 0025094319 scopus 로고
    • An essential role for a phospholipid transfer protein in yeast Golgi function
    • Bankaitis, V.A., J.R. Aitken, A.E. Cleves, and W. Dowhan. 1990. An essential role for a phospholipid transfer protein in yeast Golgi function. Nature (Lond.). 347:561-562.
    • (1990) Nature (Lond.) , vol.347 , pp. 561-562
    • Bankaitis, V.A.1    Aitken, J.R.2    Cleves, A.E.3    Dowhan, W.4
  • 4
    • 0024095176 scopus 로고
    • Organelle assembly in yeast: Characterization of yeast mutants defective in vacuolar biogenesis and protein sorting
    • Banta, L.M., J.S. Robinson, D.J. Kliosky, and S.D. Emr. 1988. Organelle assembly in yeast: characterization of yeast mutants defective in vacuolar biogenesis and protein sorting. J. Cell Biol. 107:1369-1383.
    • (1988) J. Cell Biol. , vol.107 , pp. 1369-1383
    • Banta, L.M.1    Robinson, J.S.2    Kliosky, D.J.3    Emr, S.D.4
  • 6
    • 0027159260 scopus 로고
    • TGN38 is maintained in the trans-Golgi network by a tyrosine-containing motif in the cytoplasmic domain
    • Bos, K., C. Wraight, and K.K. Stanley. 1993. TGN38 is maintained in the trans-Golgi network by a tyrosine-containing motif in the cytoplasmic domain. EMBO (Eur. Mol. Biol. Organ.) J. 12:2219-2228.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 2219-2228
    • Bos, K.1    Wraight, C.2    Stanley, K.K.3
  • 7
    • 0029148577 scopus 로고
    • Role for phosphatidylinositol 3-kinase in the sorting and transport of newly synthesized lysosomal enzymes in mammalian cells
    • Brown, W.J., D.B. DeWald, S.D. Emr, H. Plutner, and W.E. Balch. 1995. Role for phosphatidylinositol 3-kinase in the sorting and transport of newly synthesized lysosomal enzymes in mammalian cells. J. Cell Biol. 130:781-790.
    • (1995) J. Cell Biol. , vol.130 , pp. 781-790
    • Brown, W.J.1    DeWald, D.B.2    Emr, S.D.3    Plutner, H.4    Balch, W.E.5
  • 8
    • 0029831167 scopus 로고    scopus 로고
    • Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002
    • Brunn, G.J., J. Williams, C. Sabers, G. Wiederrecht, J.C. Lawrence, Jr., and R.T. Abraham. 1996. Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002. EMBO (Eur. Mol. Biol. Organ.) J. 15:5256-5267.
    • (1996) EMBO (Eur. Mol. Biol. Organ.) J. , vol.15 , pp. 5256-5267
    • Brunn, G.J.1    Williams, J.2    Sabers, C.3    Wiederrecht, G.4    Lawrence Jr., J.C.5    Abraham, R.T.6
  • 9
    • 0030575539 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase and the regulation of cell growth
    • Carpenter, C.L., and L.C. Cantley. 1996. Phosphoinositide 3-kinase and the regulation of cell growth. Biochim. Biophys. Acta. 1288:11-16.
    • (1996) Biochim. Biophys. Acta , vol.1288 , pp. 11-16
    • Carpenter, C.L.1    Cantley, L.C.2
  • 10
    • 0029123267 scopus 로고
    • Wortmannin causes mistargeting of procathepsin D. Evidence for the involvement of a phosphatidylinositol 3-kinase in vesicular transport to lysosomes
    • Davidson, H. 1995. Wortmannin causes mistargeting of procathepsin D. Evidence for the involvement of a phosphatidylinositol 3-kinase in vesicular transport to lysosomes. J. Cell Biol. 130:797-805.
    • (1995) J. Cell Biol. , vol.130 , pp. 797-805
    • Davidson, H.1
  • 12
    • 0030790548 scopus 로고    scopus 로고
    • Using structure to define the function of phosphoinositide 3 kinase family members
    • Domin, J., and M.D. Waterfield. 1997. Using structure to define the function of phosphoinositide 3 kinase family members. FEBS (Fed. Eur. Biochem. Soc.) Lett. 410:91-95.
    • (1997) FEBS (Fed. Eur. Biochem. Soc.) Lett. , vol.410 , pp. 91-95
    • Domin, J.1    Waterfield, M.D.2
  • 13
    • 0025727594 scopus 로고
    • cDNA cloning of a novel 85 kD protein that has SH2 domains and regulates binding of PI3-kinase to the PDGF β-receptor
    • Escobedo, J.A., S. Navankasattusas, W.M. Kavanaugh, D. Milfay, V.A. Fried, and L.T. Williams. 1991. cDNA cloning of a novel 85 kD protein that has SH2 domains and regulates binding of PI3-kinase to the PDGF β-receptor. Cell. 65:75-82.
    • (1991) Cell , vol.65 , pp. 75-82
    • Escobedo, J.A.1    Navankasattusas, S.2    Kavanaugh, W.M.3    Milfay, D.4    Fried, V.A.5    Williams, L.T.6
  • 14
    • 0028263636 scopus 로고
    • Golgi coatomer binds, and forms K(+)-selective channels gated by, inositol polyphosphates
    • Fleischer, B., J. Xie, M. Mayrleitner, S.B. Shears, D.J. Palmer, and S. Fleischer. 1994. Golgi coatomer binds, and forms K(+)-selective channels gated by, inositol polyphosphates. J. Biol. Chem. 269:17826-17832.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17826-17832
    • Fleischer, B.1    Xie, J.2    Mayrleitner, M.3    Shears, S.B.4    Palmer, D.J.5    Fleischer, S.6
  • 15
    • 0024534135 scopus 로고
    • MG-160. A novel sialoglycoprotein of the medial cisternae of the Golgi apparatus
    • Gonatas, J.O., S.G. Mezitis, A. Stieber, B. Fleischer, and N.K. Gonatas. 1989. MG-160. A novel sialoglycoprotein of the medial cisternae of the Golgi apparatus. J. Biol. Chem. 264:646-653.
    • (1989) J. Biol. Chem. , vol.264 , pp. 646-653
    • Gonatas, J.O.1    Mezitis, S.G.2    Stieber, A.3    Fleischer, B.4    Gonatas, N.K.5
  • 16
    • 0028232868 scopus 로고
    • Okadaic acid treatment leads to a fragmentation of the trans-Golgi network and an increase in expression of TGN38 at the cell surface
    • Horn, M., and G. Banting. 1994. Okadaic acid treatment leads to a fragmentation of the trans-Golgi network and an increase in expression of TGN38 at the cell surface. Biochem. J. 301:68-73.
    • (1994) Biochem. J. , vol.301 , pp. 68-73
    • Horn, M.1    Banting, G.2
  • 17
    • 2642704526 scopus 로고
    • Magnetic solid supports for cell-free analysis of vesicular transport
    • M. Uhlén, E. Hornes, and Ø. Olsvik, editors. Eaton Publishing, Natick, MA
    • Howell, K.E., J.R. Crosby, M.S. Ladinsky, S.M. Jones, R. Schmid, and J. Ugelstad. 1994. Magnetic solid supports for cell-free analysis of vesicular transport. In Advances in Biomagnetic Separation. M. Uhlén, E. Hornes, and Ø. Olsvik, editors. Eaton Publishing, Natick, MA. 195-204.
    • (1994) Advances in Biomagnetic Separation , pp. 195-204
    • Howell, K.E.1    Crosby, J.R.2    Ladinsky, M.S.3    Jones, S.M.4    Schmid, R.5    Ugelstad, J.6
  • 18
    • 0027395956 scopus 로고
    • Localization of TGN38 to the trans-Golgi network: Involvement of a cytoplasmic tryosine-containing sequence
    • Humphrey, J.S., P.J. Peters, L.C. Yuan, and J.S. Bonifacino. 1993. Localization of TGN38 to the trans-Golgi network: involvement of a cytoplasmic tryosine-containing sequence. J. Cell Biol. 120:1123-1135.
    • (1993) J. Cell Biol. , vol.120 , pp. 1123-1135
    • Humphrey, J.S.1    Peters, P.J.2    Yuan, L.C.3    Bonifacino, J.S.4
  • 19
    • 0027240379 scopus 로고
    • A cytoplasmic complex of p62 and rab6 associates with TGN38/41 and is involved in budding of exocytic vesicles from the trans-Golgi network
    • Jones, S.M., J.R. Crosby, J. Salamero, and K.E. Howell. 1993. A cytoplasmic complex of p62 and rab6 associates with TGN38/41 and is involved in budding of exocytic vesicles from the trans-Golgi network. J. Cell Biol. 122:775-788.
    • (1993) J. Cell Biol. , vol.122 , pp. 775-788
    • Jones, S.M.1    Crosby, J.R.2    Salamero, J.3    Howell, K.E.4
  • 21
    • 0028084335 scopus 로고
    • Receptor tyrosine kinases and their targets
    • Kazlauskas, A. 1994. Receptor tyrosine kinases and their targets. Curr. Opin. Genet. Dev. 4:5-14.
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 5-14
    • Kazlauskas, A.1
  • 22
    • 0025042770 scopus 로고
    • Phosphorylation of the PDGF receptor β subunit creates a tight binding site for phosphatidylinositol 3 kinase
    • Kazlauskas, A., and J.A. Cooper. 1990. Phosphorylation of the PDGF receptor β subunit creates a tight binding site for phosphatidylinositol 3 kinase. EMBO (Eur. Mol. Biol. Organ.) J. 9:3279-3286.
    • (1990) EMBO (Eur. Mol. Biol. Organ.) J. , vol.9 , pp. 3279-3286
    • Kazlauskas, A.1    Cooper, J.A.2
  • 25
    • 0026472647 scopus 로고
    • The trans-Golgi network can be dissected structurally and functionally from the cisternae of the Golgi complex by brefeldin A
    • Ladinsky, M.S., and K.E. Howell. 1992. The trans-Golgi network can be dissected structurally and functionally from the cisternae of the Golgi complex by brefeldin A. Eur. J. Cell Biol. 59:92-105.
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 92-105
    • Ladinsky, M.S.1    Howell, K.E.2
  • 27
    • 0028265959 scopus 로고
    • Lipid second messengers
    • Liscovitch, M., and L.C. Cantley. 1994. Lipid second messengers. Cell. 77-329-334.
    • (1994) Cell , vol.77 , pp. 329-334
    • Liscovitch, M.1    Cantley, L.C.2
  • 28
    • 0029019442 scopus 로고
    • Signal transduction and membrane traffic: The PITP/phosphoinositide connection
    • Liscovitch, M., and L.C. Cantley. 1995. Signal transduction and membrane traffic: the PITP/phosphoinositide connection. Cell. 81:659-662.
    • (1995) Cell , vol.81 , pp. 659-662
    • Liscovitch, M.1    Cantley, L.C.2
  • 29
    • 14444287604 scopus 로고
    • Immunological approaches to the study of membrane features in adipocytes
    • Luzio, J.P. 1977. Immunological approaches to the study of membrane features in adipocytes. Methodol. Surv. Biochem. 6:131-142.
    • (1977) Methodol. Surv. Biochem. , vol.6 , pp. 131-142
    • Luzio, J.P.1
  • 30
    • 0025148186 scopus 로고
    • Identification, sequencing and expression of an integral membrane protein of the trans-Golgi network (TGN38)
    • Luzio, P.J., B. Brake, G. Banting, K.E. Howell, P. Braghetta, and K.K. Stanley. 1990. Identification, sequencing and expression of an integral membrane protein of the trans-Golgi network (TGN38). Biochem. J. 270:97-102.
    • (1990) Biochem. J. , vol.270 , pp. 97-102
    • Luzio, P.J.1    Brake, B.2    Banting, G.3    Howell, K.E.4    Braghetta, P.5    Stanley, K.K.6
  • 31
    • 0000923841 scopus 로고
    • Polyacrylamide electrophoresis of viral proteins
    • Maizel, J.V. 1971. Polyacrylamide electrophoresis of viral proteins. Methods Virol. 5:179-246.
    • (1971) Methods Virol. , vol.5 , pp. 179-246
    • Maizel, J.V.1
  • 33
    • 0028981718 scopus 로고
    • Different sensitivity to wortmannin of two vacuolar sorting signals indicates the presence of distinct sorting machineries in tobacco cells
    • Matsuoka, K., D.C. Bassham, N.V. Raikhel, and K. Nakamura. 1995. Different sensitivity to wortmannin of two vacuolar sorting signals indicates the presence of distinct sorting machineries in tobacco cells. J. Cell Biol. 130:1307-1318.
    • (1995) J. Cell Biol. , vol.130 , pp. 1307-1318
    • Matsuoka, K.1    Bassham, D.C.2    Raikhel, N.V.3    Nakamura, K.4
  • 34
    • 0027468686 scopus 로고
    • 2+ stores of rat cerebellum: Heterogeneity within and distinction from endoplasmic reticulum
    • 2+ stores of rat cerebellum: heterogeneity within and distinction from endoplasmic reticulum. Biochem. J. 291:199-204.
    • (1993) Biochem. J. , vol.291 , pp. 199-204
    • Nori, A.1    Villa, A.2    Podini, P.3    Witcher, D.R.4    Volpe, P.5
  • 35
    • 0027570012 scopus 로고
    • The assembly of signalling complexes by receptor tyrosine kinases
    • Panayotou, G., and M.D. Waterfield. 1993. The assembly of signalling complexes by receptor tyrosine kinases. Bioessays. 15:171-177.
    • (1993) Bioessays , vol.15 , pp. 171-177
    • Panayotou, G.1    Waterfield, M.D.2
  • 36
    • 0027447921 scopus 로고
    • TGN38/41 recycles between the cell surface and the TGN: Brefeldin a affects its rate of return to the TGN
    • Reaves, B., M. Horn, and G. Banting. 1993. TGN38/41 recycles between the cell surface and the TGN: brefeldin A affects its rate of return to the TGN. Mol. Biol. Cell. 4:93-105.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 93-105
    • Reaves, B.1    Horn, M.2    Banting, G.3
  • 37
    • 0029863528 scopus 로고    scopus 로고
    • The effect of wortmannin on the localisation of lysosomal type 1 integral membrane glycoprotein suggests a role for phosphoinositide 3-kinase activity in regulating membrane traffic late in the endocytic pathway
    • Reaves, B.J., N.A. Bright, B.M. Mullock, and J.P. Luzio. 1996. The effect of wortmannin on the localisation of lysosomal type 1 integral membrane glycoprotein suggests a role for phosphoinositide 3-kinase activity in regulating membrane traffic late in the endocytic pathway. J. Cell Sci. 109:744-762.
    • (1996) J. Cell Sci. , vol.109 , pp. 744-762
    • Reaves, B.J.1    Bright, N.A.2    Mullock, B.M.3    Luzio, J.P.4
  • 38
    • 11944260593 scopus 로고
    • Exocytic transport vesicles generated in vitro from the trans-Golgi network carry secretory and plasma membane proteins
    • Salamero, J., E.S. Sztul, and K.E. Howell. 1990. Exocytic transport vesicles generated in vitro from the trans-Golgi network carry secretory and plasma membane proteins. Proc. Natl. Acad. Sci. USA. 87:7717-7721.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7717-7721
    • Salamero, J.1    Sztul, E.S.2    Howell, K.E.3
  • 39
    • 0027905021 scopus 로고
    • Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene is essential for protein sorting
    • Schu, P.V., K. Takegawa, M.J. Fry, J.H. Stack, M.D. Waterfield, and S.D. Emr. 1993. Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene is essential for protein sorting. Science (Wash. DC). 260:88-91.
    • (1993) Science (Wash. DC) , vol.260 , pp. 88-91
    • Schu, P.V.1    Takegawa, K.2    Fry, M.J.3    Stack, J.H.4    Waterfield, M.D.5    Emr, S.D.6
  • 40
    • 0001718634 scopus 로고
    • Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions
    • Sheetz, M., and S. Singer. 1974. Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions. Proc. Natl. Acad. Sci. USA. 71:4457-4461.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4457-4461
    • Sheetz, M.1    Singer, S.2
  • 42
    • 0030027394 scopus 로고    scopus 로고
    • Potential sites of PI-3 kinase function in the endocytic pathway revealed by the PI-3 kinase inhibitor, wortmannin
    • Shpetner, H., M. Joly, D. Hartley, and S. Corvera. 1996. Potential sites of PI-3 kinase function in the endocytic pathway revealed by the PI-3 kinase inhibitor, wortmannin, J. Cell Biol. 132:595-605.
    • (1996) J. Cell Biol. , vol.132 , pp. 595-605
    • Shpetner, H.1    Joly, M.2    Hartley, D.3    Corvera, S.4
  • 44
    • 0028464361 scopus 로고
    • Profilin: At the crossroads of signal transduction and the actin cytoskeleton
    • Sohn, R.H., and P.J. Goldschmidt-Clermont. 1994. Profilin: at the crossroads of signal transduction and the actin cytoskeleton. Bioessays. 16:465-472.
    • (1994) Bioessays , vol.16 , pp. 465-472
    • Sohn, R.H.1    Goldschmidt-Clermont, P.J.2
  • 45
    • 0028110018 scopus 로고
    • Vps34 required for yeast vacuolar protein Sorting is a multiple specificity kinase that exhibits both protein kinase and phosphatidylinositol-specific PI3-kinase activities
    • Stack, J.H., and S.D Emr. 1994. Vps34 required for yeast vacuolar protein Sorting is a multiple specificity kinase that exhibits both protein kinase and phosphatidylinositol-specific PI3-kinase activities. J. Biol. Chem. 269:31552-31562.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31552-31562
    • Stack, J.H.1    Emr, S.D.2
  • 46
    • 0027256130 scopus 로고
    • A membrane-associated complex containing the Vps25 protein kinase and the Vps34 PI3-kinase is essential for protein sorting to the yeast lysosome like vacuole
    • Stack, J.H., P.K. Herman, P.V Schu, and S.D. Emr. 1993. A membrane-associated complex containing the Vps25 protein kinase and the Vps34 PI3-kinase is essential for protein sorting to the yeast lysosome like vacuole. EMBO (Eur. Mol. Biol. Organ.) J. 12:2195-2204.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 2195-2204
    • Stack, J.H.1    Herman, P.K.2    Schu, P.V.3    Emr, S.D.4
  • 47
    • 0028964232 scopus 로고
    • Vesicle-mediated protein transport: Regulatory interactions between the Vps15 protein kinase and the Vps34 Ptdlns 3-kinase essential for protein sorting to the vacuole in yeast
    • Stack, J.H., D. Wald, K. Takegawa, and S.D. Emr. 1995a. Vesicle-mediated protein transport: regulatory interactions between the Vps15 protein kinase and the Vps34 Ptdlns 3-kinase essential for protein sorting to the vacuole in yeast. J. Cell Biol. 129:321-334.
    • (1995) J. Cell Biol. , vol.129 , pp. 321-334
    • Stack, J.H.1    Wald, D.2    Takegawa, K.3    Emr, S.D.4
  • 48
    • 0029618201 scopus 로고
    • Receptor-mediated Protein sorting to the vacuole in yeast: Roles for protein kinase, a lipid kinase and GTP-binding proteins
    • Stack, J.H., B. Horazdovsky, and S.D. Emr. 1995b. Receptor-mediated Protein sorting to the vacuole in yeast: roles for protein kinase, a lipid kinase and GTP-binding proteins. Annu. Rev. Cell Dev. Biol. 11:1-33.
    • (1995) Annu. Rev. Cell Dev. Biol. , vol.11 , pp. 1-33
    • Stack, J.H.1    Horazdovsky, B.2    Emr, S.D.3
  • 51
    • 0022003393 scopus 로고
    • Biogenesis of the polymeric IgA-R in rat hepatocytes
    • Sztul, E.S., K.E Howell, and G.E. Palade. 1985. Biogenesis of the polymeric IgA-R in rat hepatocytes. J. Cell Biol. 100:1248-1254.
    • (1985) J. Cell Biol. , vol.100 , pp. 1248-1254
    • Sztul, E.S.1    Howell, K.E.2    Palade, G.E.3
  • 52
    • 0030822623 scopus 로고    scopus 로고
    • Characterization of the Golgi complex cleared of proteins in transit and examination of calcium uptake activities
    • Taylor, R.S., S.M. Jones, R.H. Dahl, M. Nordeen, and K.E. Howell. 1997a. Characterization of the Golgi complex cleared of proteins in transit and examination of calcium uptake activities. Mol. Biol. Cell. 8:1911-1931.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1911-1931
    • Taylor, R.S.1    Jones, S.M.2    Dahl, R.H.3    Nordeen, M.4    Howell, K.E.5
  • 53
    • 0031409582 scopus 로고    scopus 로고
    • 2D mapping of the endogenous proteins of the rat hepatocyte Golgi complex clear of proteins in transit
    • In press
    • Taylor, R.S., I. Fialka, S.M. Jones, L.A. Huber, and K.E. Howell. 1997b. 2D mapping of the endogenous proteins of the rat hepatocyte Golgi complex clear of proteins in transit. Electrophoresis. In press.
    • (1997) Electrophoresis
    • Taylor, R.S.1    Fialka, I.2    Jones, S.M.3    Huber, L.A.4    Howell, K.E.5
  • 54
    • 0026730329 scopus 로고
    • Inositol polyphosphate receptor and clathrin assembly protein AP-2 are related proteins that form potassium-selective ion channels in planar lipid bilayers
    • Timerman, A.P., M. Mayrleitner, T.J. Lukas, C.C. Chadwick, A. Saito, D.M. Watterson, H. Schindler, and S. Fleischer. 1992. Inositol polyphosphate receptor and clathrin assembly protein AP-2 are related proteins that form potassium-selective ion channels in planar lipid bilayers. Proc. Natl. Acad. Sci. USA. 89:8976-8980.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8976-8980
    • Timerman, A.P.1    Mayrleitner, M.2    Lukas, T.J.3    Chadwick, C.C.4    Saito, A.5    Watterson, D.M.6    Schindler, H.7    Fleischer, S.8
  • 56
    • 0029023942 scopus 로고
    • Rho family GTPases bind to phosphoinositide kinases
    • Tolias, K.F., L.C. Cantley, and C.L. Carpenter. 1995. Rho family GTPases bind to phosphoinositide kinases. J. Biol. Chem. 270:17656-17659.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17656-17659
    • Tolias, K.F.1    Cantley, L.C.2    Carpenter, C.L.3
  • 57
    • 0027217188 scopus 로고
    • Activation of dynamin GTPase by acidic phospholipids and endogenous rat brain vesicles
    • Tuma, P.L., MC Stachniak, and C.A. Collins. 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
  • 59
    • 0029884657 scopus 로고    scopus 로고
    • Mouse p1770 is a novel phosphoinositide 3-kinase containing a C2 domain
    • Virbasius, J.V., A. Guilherme, and M.P. Czech. 1996. Mouse p1770 is a novel phosphoinositide 3-kinase containing a C2 domain. J. Biol. Chem. 271: 13304-13307.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13304-13307
    • Virbasius, J.V.1    Guilherme, A.2    Czech, M.P.3
  • 62
    • 0029965452 scopus 로고    scopus 로고
    • Wortmannin inactivates phosphoinositide 3-kinase by covalent modification of lys-802, a residue involved in the phosphate transfer reaction
    • Wymann, M.P., G. Bulgarella-Leva, M.J. Zvelebil, L. Pirola, B. Vanhaesenbroek, M.D. Waterfield, and G. Panayotou. 1996. Wortmannin inactivates phosphoinositide 3-kinase by covalent modification of lys-802, a residue involved in the phosphate transfer reaction. Mol. Cell. Biol. 16:1722-1733.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1722-1733
    • Wymann, M.P.1    Bulgarella-Leva, G.2    Zvelebil, M.J.3    Pirola, L.4    Vanhaesenbroek, B.5    Waterfield, M.D.6    Panayotou, G.7
  • 63
    • 0027374497 scopus 로고
    • Activation of platelet phosphatidylinositide 3-kinase requires the small GTP-binding protein Rho
    • Zhang, J., W.G. King, S. Dillon, A. Hall, L. Feig, and S.E. Rittenhouse. 1993. Activation of platelet phosphatidylinositide 3-kinase requires the small GTP-binding protein Rho. J. Biol. Chem. 268:22251-22254.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22251-22254
    • Zhang, J.1    King, W.G.2    Dillon, S.3    Hall, A.4    Feig, L.5    Rittenhouse, S.E.6
  • 64
    • 0028338545 scopus 로고
    • Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85
    • Zheng, Y., S. Bagrodia, and R. Cerione. 1994. Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85. J. Biol. Chem. 269:18727-18730.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18727-18730
    • Zheng, Y.1    Bagrodia, S.2    Cerione, R.3


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