메뉴 건너뛰기




Volumn 289, Issue 33, 2014, Pages 23112-23122

A novel interaction between the SH2 domain of signaling adaptor protein Nck-1 and the upstream regulator of the Rho family GTPase Rac1 Engulfment and Cell Motility 1 (ELMO1) promotes Rac1 activation and cell motility

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELLS; CHEMICAL ACTIVATION; CYTOLOGY; PROTEINS;

EID: 84905963094     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.549550     Document Type: Article
Times cited : (9)

References (43)
  • 1
    • 0034193568 scopus 로고    scopus 로고
    • Protein-protein interactions define specificity in signal transduction
    • Pawson, T., and Nash, P. (2000) Protein-protein interactions define specificity in signal transduction. Genes Dev. 14, 1027-1047 (Pubitemid 30324418)
    • (2000) Genes and Development , vol.14 , Issue.9 , pp. 1027-1047
    • Pawson, T.1    Nash, P.2
  • 2
    • 84862659868 scopus 로고    scopus 로고
    • History of protein-protein interactions: From egg-white to complex networks
    • Braun, P., and Gingras, A. C. (2012) History of protein-protein interactions: from egg-white to complex networks. Proteomics 12, 1478-1498
    • (2012) Proteomics , vol.12 , pp. 1478-1498
    • Braun, P.1    Gingras, A.C.2
  • 3
    • 0032213509 scopus 로고    scopus 로고
    • The Nck SH2/SH3 adaptor protein: A regulator of multiple intracellular signal transduction events
    • McCarty, J. H. (1998) The Nck SH2/SH3 adaptor protein: a regulator of multiple intracellular signal transduction events. BioEssays 20, 913-921
    • (1998) BioEssays , vol.20 , pp. 913-921
    • McCarty, J.H.1
  • 4
    • 0036015163 scopus 로고    scopus 로고
    • The Nck family of adapter proteins: Regulators of actin cytoskeleton
    • DOI 10.1016/S0898-6568(02)00027-X, PII S089865680200027X
    • Buday, L., Wunderlich, L., and Tamás, P. (2002) The Nck family of adapter proteins: regulators of actin cytoskeleton. Cell. Signal. 14, 723-731 (Pubitemid 34597179)
    • (2002) Cellular Signalling , vol.14 , Issue.9 , pp. 723-731
    • Buday, L.1    Wunderlich, L.2    Tamas, P.3
  • 5
    • 0035473460 scopus 로고    scopus 로고
    • Nck/Dock: An adapter between cell surface receptors and the actin cytoskeleton
    • DOI 10.1038/sj.onc.1204782
    • Li, W., Fan, J., and Woodley, D. T. (2001) Nck/Dock: an adapter between cell surface receptors and the actin cytoskeleton. Oncogene 20, 6403-6417 (Pubitemid 32977847)
    • (2001) Oncogene , vol.20 , Issue.44 REV. ISS. 5 , pp. 6403-6417
    • Li, W.1    Fan, J.2    Woodley, D.T.3
  • 6
    • 84905991491 scopus 로고    scopus 로고
    • Integration of signaling and cytoskeletal remodeling by Nck in directional cell migration
    • Chaki, S. P., and Rivera, G. M. (2013) Integration of signaling and cytoskeletal remodeling by Nck in directional cell migration. Bioarchitecture 3, 57-63
    • (2013) Bioarchitecture , vol.3 , pp. 57-63
    • Chaki, S.P.1    Rivera, G.M.2
  • 8
    • 33745478846 scopus 로고    scopus 로고
    • Dissecting Nck/Dock signaling pathways in Drosophila visual system
    • Rao, Y. (2005) Dissecting Nck/Dock signaling pathways in Drosophila visual system. Int. J. Biol. Sci. 1, 80-86
    • (2005) Int. J. Biol. Sci. , vol.1 , pp. 80-86
    • Rao, Y.1
  • 10
    • 75149162463 scopus 로고    scopus 로고
    • Nck- and N-WASP-dependent actin-based motility is conserved in divergent vertebrate poxviruses
    • Dodding, M. P., and Way, M. (2009) Nck- and N-WASP-dependent actin-based motility is conserved in divergent vertebrate poxviruses. Cell Host Microbe 6, 536-550
    • (2009) Cell Host Microbe , vol.6 , pp. 536-550
    • Dodding, M.P.1    Way, M.2
  • 11
    • 79954612462 scopus 로고    scopus 로고
    • Identification of Dermcidin as a novel binding protein of Nck1 and characterization of its role in promoting cell migration
    • Shen, S. L., Qiu, F. H., Dayarathna, T. K., Wu, J., Kuang, M., Li, S. S., Peng, B. G., and Nie, J. (2011) Identification of Dermcidin as a novel binding protein of Nck1 and characterization of its role in promoting cell migration. Biochim. Biophys. Acta 1812, 703-710
    • (2011) Biochim. Biophys. Acta , vol.1812 , pp. 703-710
    • Shen, S.L.1    Qiu, F.H.2    Dayarathna, T.K.3    Wu, J.4    Kuang, M.5    Li, S.S.6    Peng, B.G.7    Nie, J.8
  • 13
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • DOI 10.1042/0264-6021:3480241
    • Bishop, A. L., and Hall, A. (2000) Rho GTPases and their effector proteins. Biochem. J. 348, 241-255 (Pubitemid 30345195)
    • (2000) Biochemical Journal , vol.348 , Issue.2 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 14
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • DOI 10.1038/nature01148
    • Etienne-Manneville, S., and Hall, A. (2002) Rho GTPases in cell biology. Nature 420, 629-635 (Pubitemid 36764489)
    • (2002) Nature , vol.420 , Issue.6916 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 15
  • 16
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D., and Hall, A. (1995) Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81, 53-62
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 17
    • 0042674398 scopus 로고    scopus 로고
    • RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo
    • DOI 10.1038/nature01817
    • Katoh, H., and Negishi, M. (2003) RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo. Nature 424, 461-464 (Pubitemid 36917498)
    • (2003) Nature , vol.424 , Issue.6947 , pp. 461-464
    • Katoh, H.1    Negishi, M.2
  • 18
    • 31644445194 scopus 로고    scopus 로고
    • Activation of Rac1 by RhoG regulates cell migration
    • DOI 10.1242/jcs.02720
    • Katoh, H., Hiramoto, K., and Negishi, M. (2006) Activation of Rac1 by RhoG regulates cell migration. J. Cell Sci. 119, 56-65 (Pubitemid 43169298)
    • (2006) Journal of Cell Science , vol.119 , Issue.1 , pp. 56-65
    • Katoh, H.1    Hiramoto, K.2    Negishi, M.3
  • 19
    • 0037008772 scopus 로고    scopus 로고
    • Identification of novel SH3 domain ligands for the SRC family kinase Hck. Wiskott-Aldrich syndrome protein (WASP), WASP-interacting protein (WIP), and ELMO1
    • DOI 10.1074/jbc.M202783200
    • Scott, M. P., Zappacosta, F., Kim, E. Y., Annan, R. S., and Miller, W. T. (2002) Identification of novel SH3 domain ligands for the Src family kinase Hck. Wiskott-Aldrich syndrome protein (WASP), WASP-interacting protein (WIP), and ELMO1. J. Biol. Chem. 277, 28238-28246 (Pubitemid 34966778)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.31 , pp. 28238-28246
    • Scott, M.P.1    Zappacosta, F.2    Kim, E.Y.3    Annan, R.S.4    Todd, M.W.5
  • 20
    • 20544462391 scopus 로고    scopus 로고
    • Identification of tyrosine residues on ELMO1 that are phosphorylated by the Src-family kinase Hck
    • DOI 10.1021/bi0500832
    • Yokoyama, N., deBakker, C. D., Zappacosta, F., Huddleston, M. J., Annan, R. S., Ravichandran, K. S., and Miller, W. T. (2005) Identification of tyrosine residues on ELMO1 that are phosphorylated by the Src-family kinase Hck. Biochemistry 44, 8841-8849 (Pubitemid 40840449)
    • (2005) Biochemistry , vol.44 , Issue.24 , pp. 8841-8849
    • Yokoyama, N.1    Debakker, C.D.2    Zappacosta, F.3    Huddleston, M.J.4    Annan, R.S.5    Ravichandran, K.S.6    Miller, W.T.7
  • 22
    • 80655125028 scopus 로고    scopus 로고
    • The Arf family GTPase Arl4A complexes with ELMO proteins to promote actin cytoskeleton remodeling and reveals a versatile Ras-binding domain in the ELMO proteins family
    • Patel, M., Chiang, T. C., Tran, V., Lee, F. J., and Côté, J. F. (2011) The Arf family GTPase Arl4A complexes with ELMO proteins to promote actin cytoskeleton remodeling and reveals a versatile Ras-binding domain in the ELMO proteins family. J. Biol. Chem. 286, 38969-38979
    • (2011) J. Biol. Chem. , vol.286 , pp. 38969-38979
    • Patel, M.1    Chiang, T.C.2    Tran, V.3    Lee, F.J.4    Côté, J.F.5
  • 25
    • 0035793946 scopus 로고    scopus 로고
    • Identification and kinetic analysis of the interaction between Nck-2 and DOCK180
    • DOI 10.1016/S0014-5793(01)02195-0, PII S0014579301021950
    • Tu, Y., Kucik, D. F., and Wu, C. (2001) Identification and kinetic analysis of the interaction between Nck-2 and DOCK180. FEBS Letters 491, 193-199 (Pubitemid 32193795)
    • (2001) FEBS Letters , vol.491 , Issue.3 , pp. 193-199
    • Tu, Y.1    Kucik, D.F.2    Wu, C.3
  • 27
    • 0035969559 scopus 로고    scopus 로고
    • Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication
    • DOI 10.1038/35107009
    • Nash, P., Tang, X., Orlicky, S., Chen, Q., Gertler, F. B., Mendenhall, M. D., Sicheri, F., Pawson, T., and Tyers, M. (2001) Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication. Nature 414, 514-521 (Pubitemid 33131529)
    • (2001) Nature , vol.414 , Issue.6863 , pp. 514-521
    • Nash, P.1    Tang, X.2    Orlicky, S.3    Chen, Q.4    Gertler, F.B.5    Mendenhall, M.D.6    Sicheri, F.7    Pawson, T.8    Tyers, M.9
  • 30
    • 0033518296 scopus 로고    scopus 로고
    • Novel mode of ligand binding by the SH2 domain of the human XLP disease gene product SAP/SH2D1A
    • Li, S. C., Gish, G., Yang, D., Coffey, A. J., Forman-Kay, J. D., Ernberg, I., Kay, L. E., and Pawson, T. (1999) Novel mode of ligand binding by the SH2 domain of the human XLP disease gene product SAP/SH2D1A. Curr. Biol. 9, 1355-1362
    • (1999) Curr. Biol. , vol.9 , pp. 1355-1362
    • Li, S.C.1    Gish, G.2    Yang, D.3    Coffey, A.J.4    Forman-Kay, J.D.5    Ernberg, I.6    Kay, L.E.7    Pawson, T.8
  • 31
    • 0033974061 scopus 로고    scopus 로고
    • Regulatory and signaling properties of the Vav family
    • Bustelo, X. R. (2000) Regulatory and signaling properties of the Vav family. Mol. Cell. Biol. 20, 1461-1477
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1461-1477
    • Bustelo, X.R.1
  • 32
    • 0031033292 scopus 로고    scopus 로고
    • Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product
    • DOI 10.1038/385169a0
    • Crespo, P., Schuebel, K. E., Ostrom, A. A., Gutkind, J. S., and Bustelo, X. R. (1997) Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product. Nature 385, 169-172 (Pubitemid 27034219)
    • (1997) Nature , vol.385 , Issue.6612 , pp. 169-172
    • Crespo, P.1    Schuebel, K.E.2    Ostrom, A.A.3    Gutkind, J.S.4    Bustelo, X.R.5
  • 33
    • 33644539533 scopus 로고    scopus 로고
    • Targeting and activation of Rac1 are mediated by the exchange factor beta-Pix
    • ten Klooster, J. P., Jaffer, Z. M., Chernoff, J., and Hordijk, P. L. (2006) Targeting and activation of Rac1 are mediated by the exchange factor beta-Pix. J. Cell Biol. 172, 759-769
    • (2006) J. Cell Biol. , vol.172 , pp. 759-769
    • Ten Klooster, J.P.1    Jaffer, Z.M.2    Chernoff, J.3    Hordijk, P.L.4
  • 34
    • 0034008403 scopus 로고    scopus 로고
    • Induction of Rac-guanine nucleotide exchange activity of Ras- GRF1/CDC25(Mm) following phosphorylation by the nonreceptor tyrosine kinase Src
    • DOI 10.1074/jbc.275.8.5441
    • Kiyono, M., Kaziro, Y., and Satoh, T. (2000) Induction of rac-guanine nucleotide exchange activity of Ras-GRF1/CDC25(Mm) following phosphorylation by the nonreceptor tyrosine kinase Src. J. Biol. Chem. 275, 5441-5446 (Pubitemid 30115176)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.8 , pp. 5441-5446
    • Kiyono, M.1    Kaziro, Y.2    Satoh, T.3
  • 35
    • 52649094451 scopus 로고    scopus 로고
    • Phosphorylation and activation of the Rac1 and Cdc42 GEF Asef in A431 cells stimulated by EGF
    • Itoh, R. E., Kiyokawa, E., Aoki, K., Nishioka, T., Akiyama, T., and Matsuda, M. (2008) Phosphorylation and activation of the Rac1 and Cdc42 GEF Asef in A431 cells stimulated by EGF. J. Cell Sci. 121, 2635-2642
    • (2008) J. Cell Sci. , vol.121 , pp. 2635-2642
    • Itoh, R.E.1    Kiyokawa, E.2    Aoki, K.3    Nishioka, T.4    Akiyama, T.5    Matsuda, M.6
  • 36
    • 0031105660 scopus 로고    scopus 로고
    • Human p21-activated kinase (Pak1) regulates actin organization in mammalian cells
    • Sells, M. A., Knaus, U. G., Bagrodia, S., Ambrose, D. M., Bokoch, G. M., and Chernoff, J. (1997) Human p21-activated kinase (Pak1) regulates actin organization in mammalian cells. Curr. Biol. 7, 202-210 (Pubitemid 27164726)
    • (1997) Current Biology , vol.7 , Issue.3 , pp. 202-210
    • Sells, M.A.1    Knaus, U.G.2    Bagrodia, S.3    Ambrose, D.M.4    Bokoch, G.M.5    Chernoff, J.6
  • 37
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton
    • DOI 10.1016/S0955-0674(97)80156-1
    • Tapon, N., and Hall, A. (1997) Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr. Opin. Cell Biol. 9, 86-92 (Pubitemid 27065113)
    • (1997) Current Opinion in Cell Biology , vol.9 , Issue.1 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 38
    • 0033533613 scopus 로고    scopus 로고
    • αPIX nucleotide exchange factor is activated by interaction with phosphatidylinositol 3-kinase
    • DOI 10.1038/sj.onc.1202936
    • Yoshii, S., Tanaka, M., Otsuki, Y., Wang, D. Y., Guo, R. J., Zhu, Y., Takeda, R., Hanai, H., Kaneko, E., and Sugimura, H. (1999) αPIX nucleotide exchange factor is activated by interaction with phosphatidylinositol 3-kinase. Oncogene 18, 5680-5690 (Pubitemid 29497603)
    • (1999) Oncogene , vol.18 , Issue.41 , pp. 5680-5690
    • Yoshii, S.1    Tanaka, M.2    Otsuki, Y.3    Wang, D.-Y.4    Guo, R.-J.5    Zhu, Y.6    Takeda, R.7    Hanai, H.8    Kaneko, E.9    Sugimura, H.10
  • 39
    • 78649329795 scopus 로고    scopus 로고
    • An evolutionarily conserved autoin-hibitory molecular switch inELMOproteins regulates Rac signaling
    • Patel, M., Margaron, Y., Fradet, N., Yang, Q., Wilkes, B., Bouvier, M., Hofmann, K., and Côté, J. F. (2010) An evolutionarily conserved autoin-hibitory molecular switch inELMOproteins regulates Rac signaling. Curr. Biol. 20, 2021-2027
    • (2010) Curr. Biol. , vol.20 , pp. 2021-2027
    • Patel, M.1    Margaron, Y.2    Fradet, N.3    Yang, Q.4    Wilkes, B.5    Bouvier, M.6    Hofmann, K.7    Côté, J.F.8
  • 40
    • 80054098174 scopus 로고    scopus 로고
    • Opening up on ELMO regulation: New insights into the control of Rac signaling by the DOCK180/ELMO complex
    • Patel, M., Pelletier, A., and Côté, J. F. (2011) Opening up on ELMO regulation: New insights into the control of Rac signaling by the DOCK180/ELMO complex. Small GTPases 2, 268-275
    • (2011) Small GTPases , vol.2 , pp. 268-275
    • Patel, M.1    Pelletier, A.2    Côté, J.F.3
  • 41
    • 0034983715 scopus 로고    scopus 로고
    • WASP and WAVE family proteins: Key molecules for rapid rearrangement of cortical actin filaments and cell movement
    • Takenawa, T., and Miki, H. (2001) WASP and WAVE family proteins: key molecules for rapid rearrangement of cortical actin filaments and cell movement. J. Cell Sci. 114, 1801-1809 (Pubitemid 32530035)
    • (2001) Journal of Cell Science , vol.114 , Issue.10 , pp. 1801-1809
    • Takenawa, T.1    Miki, H.2
  • 42
    • 0037102301 scopus 로고    scopus 로고
    • Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck
    • Eden, S., Rohatgi, R., Podtelejnikov, A. V., Mann, M., and Kirschner, M. W. (2002) Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. Nature 418, 790-793
    • (2002) Nature , vol.418 , pp. 790-793
    • Eden, S.1    Rohatgi, R.2    Podtelejnikov, A.V.3    Mann, M.4    Kirschner, M.W.5
  • 43
    • 0035854732 scopus 로고    scopus 로고
    • Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway
    • Rohatgi, R., Nollau, P., Ho, H. Y., Kirschner, M. W., and Mayer, B. J. (2001) Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway. J. Biol. Chem. 276, 26448-26452
    • (2001) J. Biol. Chem. , vol.276 , pp. 26448-26452
    • Rohatgi, R.1    Nollau, P.2    Ho, H.Y.3    Kirschner, M.W.4    Mayer, B.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.