메뉴 건너뛰기




Volumn 80, Issue 3, 2012, Pages 1252-1266

Identification of components of the host type IA phosphoinositide 3-kinase pathway that promote internalization of Listeria monocytogenes

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CENTAURIN DELTA 1; CYTOSKELETON PROTEIN; DAPP1 PROTEIN; GIT1 PROTEIN; MAMMALIAN TARGET OF RAPAMYCIN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE 1; PROTEIN KINASE C ZETA; PSCD2 PROTEIN; RAB PROTEIN; RAB5C PROTEIN; SMALL INTERFERING RNA; SWAP70 PROTEIN; UNCLASSIFIED DRUG;

EID: 84863251100     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.06082-11     Document Type: Article
Times cited : (32)

References (97)
  • 1
    • 4544261701 scopus 로고    scopus 로고
    • The adaptor protein Bam32 regulates Rac1 activation and actin remodeling through a phosphorylation-dependent mechanism
    • Allam A, Niiro H, Clark EA, Marshall AJ. 2004. The adaptor protein Bam32 regulates Rac1 activation and actin remodeling through a phosphorylation-dependent mechanism. J. Biol. Chem. 279:39775-39782.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39775-39782
    • Allam, A.1    Niiro, H.2    Clark, E.A.3    Marshall, A.J.4
  • 2
    • 77956927514 scopus 로고    scopus 로고
    • Integrin receptors play a role in the internalin B-dependent entry of Listeria monocytogenes into host cells
    • Auriemma C, et al. 2010. Integrin receptors play a role in the internalin B-dependent entry of Listeria monocytogenes into host cells. Cell. Mol. Biol. Lett. 15:496-506.
    • (2010) Cell. Mol. Biol. Lett. , vol.15 , pp. 496-506
    • Auriemma, C.1
  • 3
    • 79952110243 scopus 로고    scopus 로고
    • PDK1: the major transducer of PI 3-kinase actions
    • Bayascas JR. 2010. PDK1: the major transducer of PI 3-kinase actions. Curr. Top. Microbiol. Immunol. 346:9-29.
    • (2010) Curr. Top. Microbiol. Immunol. , vol.346 , pp. 9-29
    • Bayascas, J.R.1
  • 4
    • 0035494442 scopus 로고    scopus 로고
    • A role for cofilin and LIM kinase in Listeria-induced phagocytosis
    • Bierne H, et al. 2001. A role for cofilin and LIM kinase in Listeria-induced phagocytosis. J. Cell Biol. 155:101-112.
    • (2001) J. Cell Biol. , vol.155 , pp. 101-112
    • Bierne, H.1
  • 5
    • 17844363005 scopus 로고    scopus 로고
    • WASP-related proteins, Abi and Ena/VASP are required for Listeria invasion induced by the Met receptor
    • Bierne H, et al. 2005. WASP-related proteins, Abi and Ena/VASP are required for Listeria invasion induced by the Met receptor. J. Cell Sci. 118:1537-1547.
    • (2005) J. Cell Sci. , vol.118 , pp. 1537-1547
    • Bierne, H.1
  • 6
    • 64049117000 scopus 로고    scopus 로고
    • Listeria monocytogenes internalin and E-cadherin: from structure to pathogenesis
    • Bonazzi M, Lecuit M, Cossart P. 2009. Listeria monocytogenes internalin and E-cadherin: from structure to pathogenesis. Cell. Microbiol. 11:693-702.
    • (2009) Cell. Microbiol. , vol.11 , pp. 693-702
    • Bonazzi, M.1    Lecuit, M.2    Cossart, P.3
  • 7
    • 0034774069 scopus 로고    scopus 로고
    • Activation of protein kinase Cζ induces serine phosphorylation of VAMP2 in the GLUT4 compartment and increases glucose transport in skeletal muscle
    • Braiman L, et al. 2001. Activation of protein kinase Cζ induces serine phosphorylation of VAMP2 in the GLUT4 compartment and increases glucose transport in skeletal muscle. Mol. Cell. Biol. 21:7852-7861.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7852-7861
    • Braiman, L.1
  • 8
    • 33644785944 scopus 로고    scopus 로고
    • Linking exocytosis and endocytosis during phagocytosis
    • Braun V, Niedergang F. 2006. Linking exocytosis and endocytosis during phagocytosis. Biol. Cell 98:195-201.
    • (2006) Biol. Cell , vol.98 , pp. 195-201
    • Braun, V.1    Niedergang, F.2
  • 9
    • 0035802108 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate and Arf6-regulated membrane traffic
    • Brown FD, Rozelle AL, Yin HL, Balla R, Donaldson JG. 2001. Phosphatidylinositol 4,5-bisphosphate and Arf6-regulated membrane traffic. J. Cell Biol. 154:1007-1017.
    • (2001) J. Cell Biol. , vol.154 , pp. 1007-1017
    • Brown, F.D.1    Rozelle, A.L.2    Yin, H.L.3    Balla, R.4    Donaldson, J.G.5
  • 11
    • 77951568703 scopus 로고    scopus 로고
    • Phosphoinositide signalling in cancer: beyond PI3K and PTEN
    • Bunney TD, Katan M. 2010. Phosphoinositide signalling in cancer: beyond PI3K and PTEN. Nat. Rev. Cancer 10:342-352.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 342-352
    • Bunney, T.D.1    Katan, M.2
  • 12
    • 79960055459 scopus 로고    scopus 로고
    • Ras interaction with PI3K: more than just another effector pathway
    • Castellano E, Downward J. 2011. Ras interaction with PI3K: more than just another effector pathway. Genes Cancer 2:261-274.
    • (2011) Genes Cancer , vol.2 , pp. 261-274
    • Castellano, E.1    Downward, J.2
  • 13
    • 34250361914 scopus 로고    scopus 로고
    • Non-canonical interaction of phosphoinositides with pleckstrin homology domains of Tiam1 and ARHGAP9
    • Ceccarelli DFJ, et al. 2007. Non-canonical interaction of phosphoinositides with pleckstrin homology domains of Tiam1 and ARHGAP9. J. Biol. Chem. 282:13864-13874.
    • (2007) J. Biol. Chem. , vol.282 , pp. 13864-13874
    • Ceccarelli, D.F.J.1
  • 14
    • 33746160962 scopus 로고    scopus 로고
    • Regulation of EGFR endocytic trafficking by rab proteins
    • Ceresa BP. 2006. Regulation of EGFR endocytic trafficking by rab proteins. Histol. Histopathol. 21:987-993.
    • (2006) Histol. Histopathol. , vol.21 , pp. 987-993
    • Ceresa, B.P.1
  • 15
    • 10344232033 scopus 로고    scopus 로고
    • The p85a subunit of phosphatidylinositol 3-kinase binds to and stimulates the GTPase activity of Rab proteins
    • Chamberlain MD, Berry TR, Pastor MC, Anderson DH. 2004. The p85a subunit of phosphatidylinositol 3-kinase binds to and stimulates the GTPase activity of Rab proteins. J. Biol. Chem. 279:48607-48614.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48607-48614
    • Chamberlain, M.D.1    Berry, T.R.2    Pastor, M.C.3    Anderson, D.H.4
  • 16
    • 79960917675 scopus 로고    scopus 로고
    • Unraveling the enigma: progress towards understanding the coronin family of actin regulators
    • Chan KT, Creed SJ, Bear JE. 2011. Unraveling the enigma: progress towards understanding the coronin family of actin regulators. Trends Cell Biol. 21:481-488.
    • (2011) Trends Cell Biol. , vol.21 , pp. 481-488
    • Chan, K.T.1    Creed, S.J.2    Bear, J.E.3
  • 17
    • 0029979722 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase
    • Chen HC, Appenddu PA, Isoda H, Guan JL. 1996. Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase. J. Biol. Chem. 271:26329-26334.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26329-26334
    • Chen, H.C.1    Appenddu, P.A.2    Isoda, H.3    Guan, J.L.4
  • 18
    • 0033174034 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-OH kinases are Rab5 effectors
    • Christoforidis S, et al. 1999. Phosphatidylinositol 3-OH kinases are Rab5 effectors. Nat. Cell Biol. 1:249-252.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 249-252
    • Christoforidis, S.1
  • 19
    • 0036326980 scopus 로고    scopus 로고
    • Identification of MEK- and phosphoinositide 3-kinase-dependent signalling as essential events during Chlamydia pneumoniae invasion of HEp2 cells
    • Coombes BK, Mahony JB. 2002. Identification of MEK- and phosphoinositide 3-kinase-dependent signalling as essential events during Chlamydia pneumoniae invasion of HEp2 cells. Cell. Microbiol. 4:447-460.
    • (2002) Cell. Microbiol. , vol.4 , pp. 447-460
    • Coombes, B.K.1    Mahony, J.B.2
  • 20
    • 23144450821 scopus 로고    scopus 로고
    • A novel and evolutionarily conserved PtdIns(3,4,5)P3-binding domain is necessary for Dock180 signalling
    • Cote JF, Motoyama AB, Bush JA, Vuori K. 2005. A novel and evolutionarily conserved PtdIns(3,4,5)P3-binding domain is necessary for Dock180 signalling. Nat. Cell Biol. 7:797-807.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 797-807
    • Cote, J.F.1    Motoyama, A.B.2    Bush, J.A.3    Vuori, K.4
  • 21
    • 0036304226 scopus 로고    scopus 로고
    • Myosin X is a downstream effector of PI(3)K during phagocytosis
    • Cox D, et al. 2002. Myosin X is a downstream effector of PI(3)K during phagocytosis. Nat. Cell Biol. 4:469-476.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 469-476
    • Cox, D.1
  • 22
    • 33747799289 scopus 로고    scopus 로고
    • Enhancing and confirming the specificity of RNAi experiments
    • Cullen BR. 2006. Enhancing and confirming the specificity of RNAi experiments. Nat. Methods 3:677-681.
    • (2006) Nat. Methods , vol.3 , pp. 677-681
    • Cullen, B.R.1
  • 24
    • 34548431321 scopus 로고    scopus 로고
    • The carboxylterminal SH3 domain of the mammalian adaptor CrkII promotes internalization of Listeria monocytogenes through activation of host phosphoinositide 3-kinase
    • Dokainish H, Gavicherla B, Shen Y, Ireton K. 2007. The carboxylterminal SH3 domain of the mammalian adaptor CrkII promotes internalization of Listeria monocytogenes through activation of host phosphoinositide 3-kinase. Cell. Microbiol. 9:2497-2516.
    • (2007) Cell. Microbiol. , vol.9 , pp. 2497-2516
    • Dokainish, H.1    Gavicherla, B.2    Shen, Y.3    Ireton, K.4
  • 25
    • 4143145447 scopus 로고    scopus 로고
    • P-Rex2, a new guanine nucleotide exchange factor for Rac
    • Donald S, et al. 2004. P-Rex2, a new guanine nucleotide exchange factor for Rac. FEBS Lett. 572:172-176.
    • (2004) FEBS Lett. , vol.572 , pp. 172-176
    • Donald, S.1
  • 26
    • 79957473559 scopus 로고    scopus 로고
    • ARF family G proteins and their regulators: roles in membrane transport, development, and disease
    • Donaldson JG, Jackson CL. 2011. ARF family G proteins and their regulators: roles in membrane transport, development, and disease. Nat. Rev. Mol. Cell Biol. 12:362-375.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 362-375
    • Donaldson, J.G.1    Jackson, C.L.2
  • 27
    • 0034306455 scopus 로고    scopus 로고
    • Identification of pleckstrin-homology domain containing proteins with novel phosphoinositide-binding specificities
    • Dowler S, et al. 2000. Identification of pleckstrin-homology domain containing proteins with novel phosphoinositide-binding specificities. Biochem. J. 351:19-31.
    • (2000) Biochem. J. , vol.351 , pp. 19-31
    • Dowler, S.1
  • 28
    • 0033567293 scopus 로고    scopus 로고
    • DAPP1: a dual adaptor for phosphotyrosine and 3-phosphoinositides
    • Dowler S, Currie RA, Downes CP, Alessi DR. 1999. DAPP1: a dual adaptor for phosphotyrosine and 3-phosphoinositides. Biochem. J. 342:7-12.
    • (1999) Biochem. J. , vol.342 , pp. 7-12
    • Dowler, S.1    Currie, R.A.2    Downes, C.P.3    Alessi, D.R.4
  • 29
    • 0029063839 scopus 로고
    • Entry of Listeria monocytogenes into hepatocytes requires expression of InlB, a surface protein of the internalin multigene family
    • Dramsi S, et al. 1995. Entry of Listeria monocytogenes into hepatocytes requires expression of InlB, a surface protein of the internalin multigene family. Mol. Microbiol. 16:251-261.
    • (1995) Mol. Microbiol. , vol.16 , pp. 251-261
    • Dramsi, S.1
  • 31
    • 33746257209 scopus 로고    scopus 로고
    • The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism
    • Engelman JA, Luo J, Cantley LC. 2006. The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism. Nat. Rev. Genet. 7:606-619.
    • (2006) Nat. Rev. Genet. , vol.7 , pp. 606-619
    • Engelman, J.A.1    Luo, J.2    Cantley, L.C.3
  • 32
    • 0032518666 scopus 로고    scopus 로고
    • Activation of phospholipase Cγ by PI 3-kinaseinduced PH domain-mediated membrane targeting
    • Falasca M, et al. 1998. Activation of phospholipase Cγ by PI 3-kinaseinduced PH domain-mediated membrane targeting. EMBO J. 15:414-422.
    • (1998) EMBO J. , vol.15 , pp. 414-422
    • Falasca, M.1
  • 33
    • 77952007543 scopus 로고    scopus 로고
    • Mammalian target of rapamycin (mTor): conducting the cellular signaling symphony
    • Foster KG, Fingar DC. 2010. Mammalian target of rapamycin (mTor): conducting the cellular signaling symphony. J. Biol. Chem. 285:14071-14077.
    • (2010) J. Biol. Chem. , vol.285 , pp. 14071-14077
    • Foster, K.G.1    Fingar, D.C.2
  • 34
    • 78049425330 scopus 로고    scopus 로고
    • Critical role for the host GTPase-activating protein ARAP2 in InlB-mediated entry of Listeria monocytogenes
    • Gavicherla B, et al. 2010. Critical role for the host GTPase-activating protein ARAP2 in InlB-mediated entry of Listeria monocytogenes. Infect. Immun. 78:4532-4541.
    • (2010) Infect. Immun. , vol.78 , pp. 4532-4541
    • Gavicherla, B.1
  • 35
    • 0029143549 scopus 로고
    • Physical association and functional relationship between protein kinase Cζ and the actin cytoskeleton
    • Gomez J, et al. 1995. Physical association and functional relationship between protein kinase Cζ and the actin cytoskeleton. Eur. J. Immunol. 25:2673-2678.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 2673-2678
    • Gomez, J.1
  • 36
    • 15144353776 scopus 로고    scopus 로고
    • Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav
    • Han J, et al. 1998. Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav. Science 279:558-560.
    • (1998) Science , vol.279 , pp. 558-560
    • Han, J.1
  • 37
    • 80051553821 scopus 로고    scopus 로고
    • InlB-mediated Listeria monocyotogenes internalization requires a balanced phospholipase D activity maintained through phospho-cofilin
    • Han X, et al. 2011. InlB-mediated Listeria monocyotogenes internalization requires a balanced phospholipase D activity maintained through phospho-cofilin. Mol. Microbiol. 81:860-880.
    • (2011) Mol. Microbiol. , vol.81 , pp. 860-880
    • Han, X.1
  • 38
    • 34249660635 scopus 로고    scopus 로고
    • Integrin-linked kinase at the heart of cardiac contractility, repair, and disease
    • Hannigan GE, Coles JG, Dedhar S. 2007. Integrin-linked kinase at the heart of cardiac contractility, repair, and disease. Circ. Res. 100:1408-1414.
    • (2007) Circ. Res. , vol.100 , pp. 1408-1414
    • Hannigan, G.E.1    Coles, J.G.2    Dedhar, S.3
  • 39
    • 0642376906 scopus 로고    scopus 로고
    • Protein kinase Cζ (PKCζ): activation mechanisms and cellular functions
    • Hirai T, Chida K. 2003. Protein kinase Cζ (PKCζ): activation mechanisms and cellular functions. J. Biochem. 133:1-7.
    • (2003) J. Biochem. , vol.133 , pp. 1-7
    • Hirai, T.1    Chida, K.2
  • 41
    • 33646705915 scopus 로고    scopus 로고
    • The multifunctional GIT family of proteins
    • Hoefen RJ, Berk BC. 2006. The multifunctional GIT family of proteins. J. Cell Sci. 119:1469-1475.
    • (2006) J. Cell Sci. , vol.119 , pp. 1469-1475
    • Hoefen, R.J.1    Berk, B.C.2
  • 42
    • 32344447753 scopus 로고    scopus 로고
    • Signal transduction events involved in human epithelial cell invasion by Campylobacter jejuni 81-176
    • Hu L, McDaniel JP, Kopecko DJ. 2006. Signal transduction events involved in human epithelial cell invasion by Campylobacter jejuni 81-176. Microb. Pathog. 40:91-100.
    • (2006) Microb. Pathog. , vol.40 , pp. 91-100
    • Hu, L.1    McDaniel, J.P.2    Kopecko, D.J.3
  • 43
    • 0033593322 scopus 로고    scopus 로고
    • Fyn associates with Cbl and phosphorylates tyrosine 731 in Cbl, a binding site for phosphatidylinositol 3-kinase
    • Hunter S, Burton EA, Wu SC, Anderson SM. 1999. Fyn associates with Cbl and phosphorylates tyrosine 731 in Cbl, a binding site for phosphatidylinositol 3-kinase. J. Biol. Chem. 274:2097-2106.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2097-2106
    • Hunter, S.1    Burton, E.A.2    Wu, S.C.3    Anderson, S.M.4
  • 44
    • 34248645155 scopus 로고    scopus 로고
    • Entry of the bacterial pathogen Listeria monocytogenes into mammalian cells
    • Ireton K. 2007. Entry of the bacterial pathogen Listeria monocytogenes into mammalian cells. Cell. Microbiol. 9:1365-1375.
    • (2007) Cell. Microbiol. , vol.9 , pp. 1365-1375
    • Ireton, K.1
  • 45
    • 0029958304 scopus 로고    scopus 로고
    • A role for phosphoinositide 3-kinase in bacterial invasion
    • Ireton K, et al. 1996. A role for phosphoinositide 3-kinase in bacterial invasion. Science 274:780-782.
    • (1996) Science , vol.274 , pp. 780-782
    • Ireton, K.1
  • 46
    • 0033546175 scopus 로고    scopus 로고
    • The Listeria monocytogenes protein InlB is an agonist of mammalian phosphoinositide-3-kinase
    • Ireton K, Payrastre B, Cossart P. 1999. The Listeria monocytogenes protein InlB is an agonist of mammalian phosphoinositide-3-kinase. J. Biol. Chem. 274:17025-17032.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17025-17032
    • Ireton, K.1    Payrastre, B.2    Cossart, P.3
  • 47
    • 34547866453 scopus 로고    scopus 로고
    • Role of phospholipase C γ1 in cell spreading requires association with a β-PIX/GIT1-containing complex, leading to activation of Cdc42 and Rac1
    • Jones NP, Katan M. 2007. Role of phospholipase C γ1 in cell spreading requires association with a β-PIX/GIT1-containing complex, leading to activation of Cdc42 and Rac1. Mol. Cell. Biol. 27:5790-5805.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 5790-5805
    • Jones, N.P.1    Katan, M.2
  • 48
    • 18244410381 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase-protein kinase B/Akt pathway is critical for Pseudomonas aeuruginosa strain PAK internalization
    • Kierbel A, Gassama-Diagne A, Mostov K, Engel JN. 2005. The phosphatidylinositol 3-kinase-protein kinase B/Akt pathway is critical for Pseudomonas aeuruginosa strain PAK internalization. Mol. Biol. Cell 16:2577-2585.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2577-2585
    • Kierbel, A.1    Gassama-Diagne, A.2    Mostov, K.3    Engel, J.N.4
  • 49
    • 0037203546 scopus 로고    scopus 로고
    • Akt: versatile mediator of cell survival and beyond
    • Kim D, Chung J. 2002. Akt: versatile mediator of cell survival and beyond. J. Biochem. Mol. Biol. 35:106-115.
    • (2002) J. Biochem. Mol. Biol. , vol.35 , pp. 106-115
    • Kim, D.1    Chung, J.2
  • 50
    • 0030975196 scopus 로고    scopus 로고
    • Signaling by phosphoinositide 3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 domains
    • Klarlund J, et al. 1997. Signaling by phosphoinositide 3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 domains. Science 275:1927-1930.
    • (1997) Science , vol.275 , pp. 1927-1930
    • Klarlund, J.1
  • 51
    • 18244392475 scopus 로고    scopus 로고
    • Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices
    • Krugmann S, et al. 2002. Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices. Mol. Cell 9:95-108.
    • (2002) Mol. Cell , vol.9 , pp. 95-108
    • Krugmann, S.1
  • 52
    • 0034912213 scopus 로고    scopus 로고
    • Association of phosphatidylinositol 3-kinase composed of p110β-catalytic and p85-regulatory subunits with the small GTPase Rab5
    • Kurosu H, Katada T. 2001. Association of phosphatidylinositol 3-kinase composed of p110β-catalytic and p85-regulatory subunits with the small GTPase Rab5. J. Biochem. 130:73-78.
    • (2001) J. Biochem. , vol.130 , pp. 73-78
    • Kurosu, H.1    Katada, T.2
  • 53
    • 27844539756 scopus 로고    scopus 로고
    • Protein kinase C and the regulation of the actin cytoskeleton
    • Larsson C. 2006. Protein kinase C and the regulation of the actin cytoskeleton. Cell. Signal. 18:276-284.
    • (2006) Cell. Signal. , vol.18 , pp. 276-284
    • Larsson, C.1
  • 54
    • 0038281249 scopus 로고    scopus 로고
    • Phosphoinositide recognition domains
    • Lemmon MA. 2003. Phosphoinositide recognition domains. Traffic 4:201-213.
    • (2003) Traffic , vol.4 , pp. 201-213
    • Lemmon, M.A.1
  • 55
    • 0033634785 scopus 로고    scopus 로고
    • Structural basis of 3-phosphoinositide recognition by pleckstrin homology domains
    • Lietzke SE, et al. 2000. Structural basis of 3-phosphoinositide recognition by pleckstrin homology domains. Mol. Cell 6:385-394.
    • (2000) Mol. Cell , vol.6 , pp. 385-394
    • Lietzke, S.E.1
  • 56
    • 33745746346 scopus 로고    scopus 로고
    • Protein kinase zeta mediates insulin-induced glucose transport through actin remodeling in L6 muscle cells
    • Liu LZ, et al. 2006. Protein kinase zeta mediates insulin-induced glucose transport through actin remodeling in L6 muscle cells. Mol. Biol. Cell 17:2322-2330.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2322-2330
    • Liu, L.Z.1
  • 58
    • 34250788809 scopus 로고    scopus 로고
    • Akt/PKB signaling: navigating downstream
    • Manning BD, Cantley LC. 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
  • 59
    • 0029869384 scopus 로고    scopus 로고
    • E-cadherin is the receptor for internalin, a surface protein required for entry of L. monocytogenes into epithelial cells
    • Mengaud J, Ohayon H, Gounon P, Mege RM, Cossart P. 1996. E-cadherin is the receptor for internalin, a surface protein required for entry of L. monocytogenes into epithelial cells. Cell 84:923-932.
    • (1996) Cell , vol.84 , pp. 923-932
    • Mengaud, J.1    Ohayon, H.2    Gounon, P.3    Mege, R.M.4    Cossart, P.5
  • 60
    • 12744264409 scopus 로고    scopus 로고
    • Sorting nexin 5 is localized to a subdomain of the early endosomes and is recruited to the plasma membrane following EGF stimulation
    • Merino-Trigo A, et al. 2004. Sorting nexin 5 is localized to a subdomain of the early endosomes and is recruited to the plasma membrane following EGF stimulation. J. Cell Sci. 117:6413-6424.
    • (2004) J. Cell Sci. , vol.117 , pp. 6413-6424
    • Merino-Trigo, A.1
  • 61
    • 0033517348 scopus 로고    scopus 로고
    • Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an adaptor molecule that interacts with the oncoprotein-serine/threonine kinase Akt2
    • Mitsuuchi Y, et al. 1999. Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an adaptor molecule that interacts with the oncoprotein-serine/threonine kinase Akt2. Oncogene 18:4891-4898.
    • (1999) Oncogene , vol.18 , pp. 4891-4898
    • Mitsuuchi, Y.1
  • 62
    • 0036159033 scopus 로고    scopus 로고
    • ARAP1: a point of convergence for Arf and Rho signaling
    • Miura K, et al. 2002. ARAP1: a point of convergence for Arf and Rho signaling. Mol. Cell 9:109-119.
    • (2002) Mol. Cell , vol.9 , pp. 109-119
    • Miura, K.1
  • 63
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • Mosmann T. 1983. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 65:55-63.
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 64
    • 0037283966 scopus 로고    scopus 로고
    • The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC
    • Mukai H. 2003. The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC. J. Biochem. 133:17-27.
    • (2003) J. Biochem. , vol.133 , pp. 17-27
    • Mukai, H.1
  • 65
    • 3342977736 scopus 로고    scopus 로고
    • Convergence of non-clathrin- and clathrin-derived endosomes involves Arf6 inactivation and changes in phosphoinositides
    • Naslavsky N, Weigert R, Donaldson JG. 2004. Convergence of non-clathrin- and clathrin-derived endosomes involves Arf6 inactivation and changes in phosphoinositides. Mol. Biol. Cell 15:3542-3552.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3542-3552
    • Naslavsky, N.1    Weigert, R.2    Donaldson, J.G.3
  • 66
    • 77952004815 scopus 로고    scopus 로고
    • Differential effects of cytohesins 2 and 3 on β1 integrin recycling
    • Oh SJ, Santy LC. 2010. Differential effects of cytohesins 2 and 3 on β1 integrin recycling. J. Biol. Chem. 285:14610-14616.
    • (2010) J. Biol. Chem. , vol.285 , pp. 14610-14616
    • Oh, S.J.1    Santy, L.C.2
  • 67
    • 69549098037 scopus 로고    scopus 로고
    • CD14-Mac-1 interactions in Bacillus anthracis spore internalization by macrophages
    • Oliva C, Turnbaugh CL, Kearney JF. 2009. CD14-Mac-1 interactions in Bacillus anthracis spore internalization by macrophages. Proc. Natl. Acad. Sci. U. S. A. 106:13957-13962.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 13957-13962
    • Oliva, C.1    Turnbaugh, C.L.2    Kearney, J.F.3
  • 68
    • 46149125934 scopus 로고    scopus 로고
    • Endocytic trafficking of Rac is required for the spatial restriction of signaling in cell migration
    • Palamidessi A, et al. 2008. Endocytic trafficking of Rac is required for the spatial restriction of signaling in cell migration. Cell 134:135-147.
    • (2008) Cell , vol.134 , pp. 135-147
    • Palamidessi, A.1
  • 69
    • 77957874785 scopus 로고    scopus 로고
    • PtdIns(3,4,5)P3 is a regulator of myosin-X localization and filopodia formation
    • Plantard L, et al. 2010. PtdIns(3,4,5)P3 is a regulator of myosin-X localization and filopodia formation. J. Cell Sci. 123:3525-3534.
    • (2010) J. Cell Sci. , vol.123 , pp. 3525-3534
    • Plantard, L.1
  • 71
    • 0037201953 scopus 로고    scopus 로고
    • The regulation of phospholipase D by inositol phospholipids and small GTPases
    • Powner DJ, Wakelam MJO. 2002. The regulation of phospholipase D by inositol phospholipids and small GTPases. FEBS Lett. 531:62-64.
    • (2002) FEBS Lett. , vol.531 , pp. 62-64
    • Powner, D.J.1    Wakelam, M.J.O.2
  • 72
    • 0030820924 scopus 로고    scopus 로고
    • A comparative analysis of the phosphoinositide binding specificity of pleckstrin homology domains
    • Rameh LE, et al. 1997. A comparative analysis of the phosphoinositide binding specificity of pleckstrin homology domains. J. Biol. Chem. 272:22059-22066.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22059-22066
    • Rameh, L.E.1
  • 73
    • 72949116594 scopus 로고    scopus 로고
    • An aPKC-exocyst complex controls paxillin phosphorylation and migration through localised JNK activation
    • Rosse C, et al. 2009. An aPKC-exocyst complex controls paxillin phosphorylation and migration through localised JNK activation. PLoS Biol. 7:e1000235.
    • (2009) PLoS Biol. , vol.7
    • Rosse, C.1
  • 74
    • 75149161903 scopus 로고    scopus 로고
    • PKC and the control of localized signal dynamics
    • Rosse C, et al. 2010. PKC and the control of localized signal dynamics. Nat. Rev. Mol. Cell Biol. 11:103-112.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 103-112
    • Rosse, C.1
  • 75
    • 79960761944 scopus 로고    scopus 로고
    • An emerging role for Tor signaling in mammalian tissue and stem cell physiology
    • Russell RC, Fang C, Guan KL. 2011. An emerging role for Tor signaling in mammalian tissue and stem cell physiology. Development 138:3343-3356.
    • (2011) Development , vol.138 , pp. 3343-3356
    • Russell, R.C.1    Fang, C.2    Guan, K.L.3
  • 77
    • 0031855010 scopus 로고    scopus 로고
    • Wortmannin blocks Yersinia invasin-triggered internalization, but not interleukin-8 production by epithelial cells
    • Schulte R, Zumbihl R, Kampik D, Fauconnier A, Autenrieth IB. 1998. Wortmannin blocks Yersinia invasin-triggered internalization, but not interleukin-8 production by epithelial cells. Med. Microbiol. Immunol. 187:53-60.
    • (1998) Med. Microbiol. Immunol. , vol.187 , pp. 53-60
    • Schulte, R.1    Zumbihl, R.2    Kampik, D.3    Fauconnier, A.4    Autenrieth, I.B.5
  • 78
    • 0034721647 scopus 로고    scopus 로고
    • InlB-dependent internalization of Listeria is mediated by the Met receptor tyrosine kinase
    • Shen Y, Naujokas M, Park M, Ireton K. 2000. InlB-dependent internalization of Listeria is mediated by the Met receptor tyrosine kinase. Cell 103:501-510.
    • (2000) Cell , vol.103 , pp. 501-510
    • Shen, Y.1    Naujokas, M.2    Park, M.3    Ireton, K.4
  • 79
    • 0037129193 scopus 로고    scopus 로고
    • SWAP-70 is a guanine nucleotide exchange factor that mediates signalling of membrane ruffling
    • Shinohara M, et al. 2002. SWAP-70 is a guanine nucleotide exchange factor that mediates signalling of membrane ruffling. Nature 416:759-763.
    • (2002) Nature , vol.416 , pp. 759-763
    • Shinohara, M.1
  • 80
    • 0001584969 scopus 로고    scopus 로고
    • The Tec family of cytoplasmic tyrosine kinases: mammalian Btk, Bmx, Itk, Tec, Txk and homologs in other species
    • Smith CIE, et al. 2001. The Tec family of cytoplasmic tyrosine kinases: mammalian Btk, Bmx, Itk, Tec, Txk and homologs in other species. Bioessays 23:436-446.
    • (2001) Bioessays , vol.23 , pp. 436-446
    • Smith, C.I.E.1
  • 82
    • 78649420006 scopus 로고    scopus 로고
    • Met signaling: principles and functions in development, organ regeneration, and cancer
    • Trusolino L, Bertotti A, Comoglio PM. 2010. Met signaling: principles and functions in development, organ regeneration, and cancer. Nat. Rev. Mol. Cell Biol. 11:834-848.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 834-848
    • Trusolino, L.1    Bertotti, A.2    Comoglio, P.M.3
  • 83
    • 0031964845 scopus 로고    scopus 로고
    • c-Cbl is tyrosine-phosphorylated by interleukin-4 and enhances mitogenic and survival signals of interleukin-4 receptor by linking with the phosphatidylinositol 3-kinase pathway
    • Ueno H, et al. 1998. c-Cbl is tyrosine-phosphorylated by interleukin-4 and enhances mitogenic and survival signals of interleukin-4 receptor by linking with the phosphatidylinositol 3-kinase pathway. Blood 91:46-53.
    • (1998) Blood , vol.91 , pp. 46-53
    • Ueno, H.1
  • 84
    • 0034934605 scopus 로고    scopus 로고
    • Listeria pathogenesis and molecular virulence determinants
    • Vazquez-Boland JA, et al. 2001. Listeria pathogenesis and molecular virulence determinants. Clin. Microbiol. Rev. 14:584-640.
    • (2001) Clin. Microbiol. Rev. , vol.14 , pp. 584-640
    • Vazquez-Boland, J.A.1
  • 85
    • 26944438047 scopus 로고    scopus 로고
    • Listeria hijacks the clathrin-dependent endocytic machinery to invade mammalian cells
    • Veiga E, Cossart P. 2005. Listeria hijacks the clathrin-dependent endocytic machinery to invade mammalian cells. Nat. Cell Biol. 7:894-900.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 894-900
    • Veiga, E.1    Cossart, P.2
  • 86
    • 0033584404 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of a human homologue of centaurin-α
    • Venkateswarlu K, Cullen PJ. 1999. Molecular cloning and functional characterization of a human homologue of centaurin-α. Biochem. Biophys. Res. Commun. 262:237-244.
    • (1999) Biochem. Biophys. Res. Commun. , vol.262 , pp. 237-244
    • Venkateswarlu, K.1    Cullen, P.J.2
  • 87
    • 0032499031 scopus 로고    scopus 로고
    • Insulindependent translocation of ARNO to the plasma membrane of adipocytes requires phosphatidylinositol 3-kinase
    • Venkateswarlu K, Oatey PB, Tavare JM, Cullen PJ. 1998. Insulindependent 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
  • 88
    • 0034607876 scopus 로고    scopus 로고
    • GIT proteins, a novel family of phosphatidylinositol 3,4,5-tris phosphate-stimulated GTPase-activating proteins for Arf6
    • Vitale N, et al. 2000. GIT proteins, a novel family of phosphatidylinositol 3,4,5-tris phosphate-stimulated GTPase-activating proteins for Arf6. J. Biol. Chem. 275:13901-13906.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13901-13906
    • Vitale, N.1
  • 89
    • 34249039680 scopus 로고    scopus 로고
    • Extending the host range of Listeria monocytogenes by rational protein design
    • Wollert T, et al. 2007. Extending the host range of Listeria monocytogenes by rational protein design. Cell 129:891-902.
    • (2007) Cell , vol.129 , pp. 891-902
    • Wollert, T.1
  • 90
    • 0035629458 scopus 로고    scopus 로고
    • The p85 subunit of phosphoinositide 3-kinase is associated with beta-catenin in the cadherin-based adhesion complex
    • Woodfield RJ, et al. 2001. The p85 subunit of phosphoinositide 3-kinase is associated with beta-catenin in the cadherin-based adhesion complex. Biochem. J. 360:335-344.
    • (2001) Biochem. J. , vol.360 , pp. 335-344
    • Woodfield, R.J.1
  • 91
    • 32044465506 scopus 로고    scopus 로고
    • Tor signaling in growth and metabolism
    • Wullschleger S, Loewith R, Hall MN. 2006. Tor signaling in growth and metabolism. Cell 124:471-484.
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 92
    • 33751264910 scopus 로고    scopus 로고
    • The GAP1 family of GTPase-activating proteins: spatial and temporal regulators of small GTPase signalling
    • Yarwood S, Bouyoucef-Cherchalli D, Cullen PJ, Kupzig S. 2006. The GAP1 family of GTPase-activating proteins: spatial and temporal regulators of small GTPase signalling. Biochem. Soc. Trans. 34:846-850.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 846-850
    • Yarwood, S.1    Bouyoucef-Cherchalli, D.2    Cullen, P.J.3    Kupzig, S.4
  • 93
    • 33845718110 scopus 로고    scopus 로고
    • ARAP2 effects on the actin cytoskeleton are dependent on Arf6-specific GTPase-activating-protein activity and binding to RhoA-GTP
    • Yoon HY, et al. 2006. ARAP2 effects on the actin cytoskeleton are dependent on Arf6-specific GTPase-activating-protein activity and binding to RhoA-GTP. J. Cell Sci. 119:4650-4666.
    • (2006) J. Cell Sci. , vol.119 , pp. 4650-4666
    • Yoon, H.Y.1
  • 94
    • 0033533613 scopus 로고    scopus 로고
    • Alpha-PIX nucleotide exchange factor is activated by interaction with phosphatidylinositol 3-kinase
    • Yoshii S, et al. 1999. Alpha-PIX nucleotide exchange factor is activated by interaction with phosphatidylinositol 3-kinase. Oncogene 18:5680-5690.
    • (1999) Oncogene , vol.18 , pp. 5680-5690
    • Yoshii, S.1
  • 95
    • 70350405643 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase-regulated adapters in lymphocyte activation
    • Zhang TT, et al. 2009. Phosphoinositide 3-kinase-regulated adapters in lymphocyte activation. Immunol. Rev. 232:255-272.
    • (2009) Immunol. Rev. , vol.232 , pp. 255-272
    • Zhang, T.T.1
  • 96
    • 0037076207 scopus 로고    scopus 로고
    • Endosomal localization and function of sorting nexin 1
    • Zhong Q, et al. 2002. Endosomal localization and function of sorting nexin 1. Proc. Natl. Acad. Sci. U. S. A. 99:6767-6772.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 6767-6772
    • Zhong, Q.1
  • 97
    • 34248149587 scopus 로고    scopus 로고
    • PI3K is negatively regulated by PIK3IP1, a novel p110 interacting protein
    • Zhu Z, et al. 2007. PI3K is negatively regulated by PIK3IP1, a novel p110 interacting protein. Biochem. Biophys. Res. Commun. 358:66-72.
    • (2007) Biochem. Biophys. Res. Commun. , vol.358 , pp. 66-72
    • Zhu, Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.