메뉴 건너뛰기




Volumn 1812, Issue 6, 2011, Pages 703-710

Identification of Dermcidin as a novel binding protein of Nck1 and characterization of its role in promoting cell migration

Author keywords

Cell migration; Dermcidin; Hepatocellular carcinoma; Nck1; SH2 domain; Tyrosine phosphorylation

Indexed keywords

DERMCIDIN; NCK PROTEIN; PHOSPHOTYROSINE; PROTEIN CDC42; PROTEIN NCK1; PROTEIN SH2; RAC1 PROTEIN; UNCLASSIFIED DRUG;

EID: 79954612462     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2011.03.004     Document Type: Article
Times cited : (27)

References (28)
  • 1
    • 28844480321 scopus 로고    scopus 로고
    • Management of hepatocellular carcinoma
    • Bruix J., Sherman M. Management of hepatocellular carcinoma. Hepatology 2005, 42:1208-1236.
    • (2005) Hepatology , vol.42 , pp. 1208-1236
    • Bruix, J.1    Sherman, M.2
  • 2
    • 0037530573 scopus 로고    scopus 로고
    • Recurrence and metastasis of hepatocellular carcinoma: progress and prospects
    • Zhou X.D. Recurrence and metastasis of hepatocellular carcinoma: progress and prospects. Hepatobiliary Pancreat. Dis. Int. 2002, 1:35-41.
    • (2002) Hepatobiliary Pancreat. Dis. Int. , vol.1 , pp. 35-41
    • Zhou, X.D.1
  • 4
    • 34247468876 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton in cancer cell migration and invasion
    • Yamaguchi H., Condeelis J. Regulation of the actin cytoskeleton in cancer cell migration and invasion. Biochim. Biophys. Acta 2007, 1773:642-652.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 642-652
    • Yamaguchi, H.1    Condeelis, J.2
  • 5
    • 0038383014 scopus 로고    scopus 로고
    • The murine Nck SH2/SH3 adaptors are important for the development of mesoderm-derived embryonic structures and for regulating the cellular actin network
    • Bladt F., Aippersbach E., Gelkop S., Strasser G.A., Nash P., Tafuri A., Gertler F.B., Pawson T. The murine Nck SH2/SH3 adaptors are important for the development of mesoderm-derived embryonic structures and for regulating the cellular actin network. Mol. Cell. Biol. 2003, 23:4586-4597.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4586-4597
    • Bladt, F.1    Aippersbach, E.2    Gelkop, S.3    Strasser, G.A.4    Nash, P.5    Tafuri, A.6    Gertler, F.B.7    Pawson, T.8
  • 6
    • 4544387829 scopus 로고    scopus 로고
    • The adaptor protein Nck1 mediates endothelin A receptor-regulated cell migration through the Cdc42-dependent c-Jun N-terminal kinase pathway
    • Miyamoto Y., Yamauchi J., Mizuno N., Itoh H. The adaptor protein Nck1 mediates endothelin A receptor-regulated cell migration through the Cdc42-dependent c-Jun N-terminal kinase pathway. J. Biol. Chem. 2004, 279:34336-34342.
    • (2004) J. Biol. Chem. , vol.279 , pp. 34336-34342
    • Miyamoto, Y.1    Yamauchi, J.2    Mizuno, N.3    Itoh, H.4
  • 9
    • 0034082699 scopus 로고    scopus 로고
    • Interaction between PAK and nck: a template for Nck targets and role of PAK autophosphorylation
    • Zhao Z.S., Manser E., Lim L. Interaction between PAK and nck: a template for Nck targets and role of PAK autophosphorylation. Mol. Cell. Biol. 2000, 20:3906-3917.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3906-3917
    • Zhao, Z.S.1    Manser, E.2    Lim, L.3
  • 10
    • 0035473460 scopus 로고    scopus 로고
    • Nck/Dock: an adapter between cell surface receptors and the actin cytoskeleton
    • Li W., Fan J., Woodley D.T. Nck/Dock: an adapter between cell surface receptors and the actin cytoskeleton. Oncogene 2001, 20:6403-6417.
    • (2001) Oncogene , vol.20 , pp. 6403-6417
    • Li, W.1    Fan, J.2    Woodley, D.T.3
  • 11
    • 77950672269 scopus 로고    scopus 로고
    • Targeting multiple kinase pathways: a change in paradigm
    • Gossage L., Eisen T. Targeting multiple kinase pathways: a change in paradigm. Clin. Cancer Res. 2010, 16:1973-1978.
    • (2010) Clin. Cancer Res. , vol.16 , pp. 1973-1978
    • Gossage, L.1    Eisen, T.2
  • 12
    • 39149135251 scopus 로고    scopus 로고
    • Downregulation of Par-3 expression and disruption of Par complex integrity by TGF-beta during the process of epithelial to mesenchymal transition in rat proximal epithelial cells
    • Wang X., Nie J., Zhou Q., Liu W., Zhu F., Chen W., Mao H., Luo N., Dong X., Yu X. Downregulation of Par-3 expression and disruption of Par complex integrity by TGF-beta during the process of epithelial to mesenchymal transition in rat proximal epithelial cells. Biochim. Biophys. Acta 2008, 1782:51-59.
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 51-59
    • Wang, X.1    Nie, J.2    Zhou, Q.3    Liu, W.4    Zhu, F.5    Chen, W.6    Mao, H.7    Luo, N.8    Dong, X.9    Yu, X.10
  • 13
    • 58549113000 scopus 로고    scopus 로고
    • Ectopic expression of Ligand-of-Numb protein X promoted TGF-beta induced epithelial to mesenchymal transition of proximal tubular epithelial cells
    • Nie J., Wu Q., Liu W., Zhu F., Qiu F., Zhou Q., Fan J., Dong X., Yu X. Ectopic expression of Ligand-of-Numb protein X promoted TGF-beta induced epithelial to mesenchymal transition of proximal tubular epithelial cells. Biochim. Biophys. Acta 2009, 1792:122-131.
    • (2009) Biochim. Biophys. Acta , vol.1792 , pp. 122-131
    • Nie, J.1    Wu, Q.2    Liu, W.3    Zhu, F.4    Qiu, F.5    Zhou, Q.6    Fan, J.7    Dong, X.8    Yu, X.9
  • 15
    • 67650080520 scopus 로고    scopus 로고
    • Regulation of process retraction and cell migration by EphA3 is mediated by the adaptor protein Nck1
    • Hu T., Shi G., Larose L., Rivera G.M., Mayer B.J., Zhou R. Regulation of process retraction and cell migration by EphA3 is mediated by the adaptor protein Nck1. Biochemistry 2009, 48:6369-6378.
    • (2009) Biochemistry , vol.48 , pp. 6369-6378
    • Hu, T.1    Shi, G.2    Larose, L.3    Rivera, G.M.4    Mayer, B.J.5    Zhou, R.6
  • 16
    • 4444384629 scopus 로고    scopus 로고
    • Characterization of a human homologue of proteolysis-inducing factor and its role in cancer cachexia
    • Monitto C.L., Dong S.M., Jen J., Sidransky D. Characterization of a human homologue of proteolysis-inducing factor and its role in cancer cachexia. Clin. Cancer Res. 2004, 10:5862-5869.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 5862-5869
    • Monitto, C.L.1    Dong, S.M.2    Jen, J.3    Sidransky, D.4
  • 18
    • 33745230465 scopus 로고    scopus 로고
    • Dermcidin expression in hepatic cells improves survival without N-glycosylation, but requires asparagine residues
    • Lowrie A.G., Wigmore S.J., Wright D.J., Waddell I.D., Ross J.A. Dermcidin expression in hepatic cells improves survival without N-glycosylation, but requires asparagine residues. Br. J. Cancer 2006, 94:1663-1671.
    • (2006) Br. J. Cancer , vol.94 , pp. 1663-1671
    • Lowrie, A.G.1    Wigmore, S.J.2    Wright, D.J.3    Waddell, I.D.4    Ross, J.A.5
  • 19
    • 0035293048 scopus 로고    scopus 로고
    • Proteolysis-inducing factor regulates hepatic gene expression via the transcription factors NF-(kappa)B and STAT3
    • Watchorn T.M., Waddell I., Dowidar N., Ross J.A. Proteolysis-inducing factor regulates hepatic gene expression via the transcription factors NF-(kappa)B and STAT3. FASEB J. 2001, 15:562-564.
    • (2001) FASEB J. , vol.15 , pp. 562-564
    • Watchorn, T.M.1    Waddell, I.2    Dowidar, N.3    Ross, J.A.4
  • 22
    • 0027521783 scopus 로고
    • Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor
    • Nishimura R., Li W., Kashishian A., Mondino A., Zhou M., Cooper J., Schlessinger J. Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor. Mol. Cell. Biol. 1993, 13:6889-6896.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6889-6896
    • Nishimura, R.1    Li, W.2    Kashishian, A.3    Mondino, A.4    Zhou, M.5    Cooper, J.6    Schlessinger, J.7
  • 23
    • 0036015163 scopus 로고    scopus 로고
    • The Nck family of adapter proteins: regulators of actin cytoskeleton
    • Buday L., Wunderlich L., Tamas P. The Nck family of adapter proteins: regulators of actin cytoskeleton. Cell. Signal. 2002, 14:723-731.
    • (2002) Cell. Signal. , vol.14 , pp. 723-731
    • Buday, L.1    Wunderlich, L.2    Tamas, P.3
  • 25
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon M.A., Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell 2010, 141:1117-1134.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 26
    • 33745185987 scopus 로고    scopus 로고
    • The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling
    • Liu B.A., Jablonowski K., Raina M., Arce M., Pawson T., Nash P.D. The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling. Mol. Cell 2006, 22:851-868.
    • (2006) Mol. Cell , vol.22 , pp. 851-868
    • Liu, B.A.1    Jablonowski, K.2    Raina, M.3    Arce, M.4    Pawson, T.5    Nash, P.D.6
  • 28
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • Blagoev B., Kratchmarova I., Ong S.E., Nielsen M., Foster L.J., Mann M. A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat. Biotechnol. 2003, 21:315-318.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 315-318
    • Blagoev, B.1    Kratchmarova, I.2    Ong, S.E.3    Nielsen, M.4    Foster, L.J.5    Mann, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.