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Volumn 358, Issue 3, 2007, Pages 931-937

STAP-2 regulates c-Fms/M-CSF receptor signaling in murine macrophage Raw 264.7 cells

Author keywords

Adaptor protein; c Fms; Macrophage; Migration; Signal transduction; Tyrosine phosphorylation

Indexed keywords

COLONY STIMULATING FACTOR RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE; SIGNAL TRANSDUCING ADAPTOR PROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN 2; UNCLASSIFIED DRUG;

EID: 34249050701     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.05.030     Document Type: Article
Times cited : (21)

References (25)
  • 1
    • 0024502040 scopus 로고
    • The molecular control of cell division, differentiation commitment and maturation in haemopoietic cells
    • Metcalf D. The molecular control of cell division, differentiation commitment and maturation in haemopoietic cells. Nature 339 (1989) 27-30
    • (1989) Nature , vol.339 , pp. 27-30
    • Metcalf, D.1
  • 2
    • 0022931543 scopus 로고
    • 125I-colony-stimulating factor-1 with bone marrow-derived macrophages
    • 125I-colony-stimulating factor-1 with bone marrow-derived macrophages. J. Biol. Chem. 261 (1986) 4024-4032
    • (1986) J. Biol. Chem. , vol.261 , pp. 4024-4032
    • Guilbert, L.J.1    Stanley, E.R.2
  • 3
    • 0019847979 scopus 로고
    • Distribution of cells bearing receptors for a colony-stimulating factor (CSF-1) in murine tissues
    • Byrne P.V., Guilbert L.J., and Stanley E.R. Distribution of cells bearing receptors for a colony-stimulating factor (CSF-1) in murine tissues. J. Cell Biol. 91 (1981) 848-853
    • (1981) J. Cell Biol. , vol.91 , pp. 848-853
    • Byrne, P.V.1    Guilbert, L.J.2    Stanley, E.R.3
  • 4
    • 0021933641 scopus 로고
    • The c-fms proto-oncogene product is related to the receptor for the mononuclear phagocyte growth factor, CSF-1
    • Sherr C.J., Rettenmier C.W., Sacca R., Roussel M.F., Look A.T., and Stanley E.R. The c-fms proto-oncogene product is related to the receptor for the mononuclear phagocyte growth factor, CSF-1. Cell 41 (1985) 665-676
    • (1985) Cell , vol.41 , pp. 665-676
    • Sherr, C.J.1    Rettenmier, C.W.2    Sacca, R.3    Roussel, M.F.4    Look, A.T.5    Stanley, E.R.6
  • 5
    • 0033525882 scopus 로고    scopus 로고
    • Expression of c-Myc in response to colony-stimulating factor-1 requires mitogen-activated protein kinase kinase-1
    • Cheng M., Wang D., and Roussel M.F. Expression of c-Myc in response to colony-stimulating factor-1 requires mitogen-activated protein kinase kinase-1. J. Biol. Chem. 274 (1999) 6553-6558
    • (1999) J. Biol. Chem. , vol.274 , pp. 6553-6558
    • Cheng, M.1    Wang, D.2    Roussel, M.F.3
  • 6
    • 0034629364 scopus 로고    scopus 로고
    • The differential time-course of extracellular-regulated kinase activity correlates with the macrophage response toward proliferation or activation
    • Valledor A.F., Comalada M., Xaus J., and Celada A. The differential time-course of extracellular-regulated kinase activity correlates with the macrophage response toward proliferation or activation. J. Biol. Chem. 275 (2000) 7403-7409
    • (2000) J. Biol. Chem. , vol.275 , pp. 7403-7409
    • Valledor, A.F.1    Comalada, M.2    Xaus, J.3    Celada, A.4
  • 9
    • 33644856778 scopus 로고    scopus 로고
    • CSF-1 and PI 3-kinase regulate podosome distribution and assembly in macrophages
    • Wheeler A.P., Smith S.D., and Ridley A.J. CSF-1 and PI 3-kinase regulate podosome distribution and assembly in macrophages. Cell Motil. Cytoskeleton 63 (2006) 132-140
    • (2006) Cell Motil. Cytoskeleton , vol.63 , pp. 132-140
    • Wheeler, A.P.1    Smith, S.D.2    Ridley, A.J.3
  • 10
    • 0024272031 scopus 로고
    • A point mutation in the extracellular domain of the human CSF-1 receptor (c-fms proto-oncogene product) activates its transforming potential
    • Roussel M.F., Downing J.R., Rettenmier C.W., and Sherr C.J. A point mutation in the extracellular domain of the human CSF-1 receptor (c-fms proto-oncogene product) activates its transforming potential. Cell 55 (1988) 979-988
    • (1988) Cell , vol.55 , pp. 979-988
    • Roussel, M.F.1    Downing, J.R.2    Rettenmier, C.W.3    Sherr, C.J.4
  • 11
    • 0038175432 scopus 로고    scopus 로고
    • STAP-2/BKS, an adaptor/docking protein, modulates STAT3 activation in acute-phase response through its YXXQ motif
    • Minoguchi M., Minoguchi S., Aki D., Joo A., Yamamoto T., Yumioka T., Matsuda T., and Yoshimura A. STAP-2/BKS, an adaptor/docking protein, modulates STAT3 activation in acute-phase response through its YXXQ motif. J. Biol. Chem. 278 (2003) 11182-11189
    • (2003) J. Biol. Chem. , vol.278 , pp. 11182-11189
    • Minoguchi, M.1    Minoguchi, S.2    Aki, D.3    Joo, A.4    Yamamoto, T.5    Yumioka, T.6    Matsuda, T.7    Yoshimura, A.8
  • 12
    • 0034738966 scopus 로고    scopus 로고
    • A novel adaptor-like protein which is a substrate for the non-receptor tyrosine kinase, BRK
    • Mitchell P.J., Sara E.A., and Crompton M.R. A novel adaptor-like protein which is a substrate for the non-receptor tyrosine kinase, BRK. Oncogene 19 (2000) 4273-4282
    • (2000) Oncogene , vol.19 , pp. 4273-4282
    • Mitchell, P.J.1    Sara, E.A.2    Crompton, M.R.3
  • 16
    • 33947355024 scopus 로고    scopus 로고
    • Leukemia inhibitory factor-induced phosphorylation of STAP-2 on tyrosine-250 is involved in its STAT3-enhancing activity
    • Sekine Y., Tsuji S., Ikeda O., Kakisaka M., Sugiyama K., Yoshimura A., and Matsuda T. Leukemia inhibitory factor-induced phosphorylation of STAP-2 on tyrosine-250 is involved in its STAT3-enhancing activity. Biochem. Biophys. Res. Commun. 356 (2007) 517-522
    • (2007) Biochem. Biophys. Res. Commun. , vol.356 , pp. 517-522
    • Sekine, Y.1    Tsuji, S.2    Ikeda, O.3    Kakisaka, M.4    Sugiyama, K.5    Yoshimura, A.6    Matsuda, T.7
  • 17
    • 0033490109 scopus 로고    scopus 로고
    • Impaired integrin-mediated signal transduction, altered cytoskeletal structure and reduced motility in Hck/Fgr deficient macrophages
    • Suen P.W., Ilic D., Caveggion E., Berton G., Damsky C.H., and Lowell C.A. Impaired integrin-mediated signal transduction, altered cytoskeletal structure and reduced motility in Hck/Fgr deficient macrophages. J. Cell Sci. 112 (1999) 4067-4078
    • (1999) J. Cell Sci. , vol.112 , pp. 4067-4078
    • Suen, P.W.1    Ilic, D.2    Caveggion, E.3    Berton, G.4    Damsky, C.H.5    Lowell, C.A.6
  • 19
    • 27744543102 scopus 로고    scopus 로고
    • Inflammatory cells during wound repair: the good, the bad and the ugly
    • Martin P., and Leibovich S.J. Inflammatory cells during wound repair: the good, the bad and the ugly. Trends Cell Biol. 15 (2005) 599-607
    • (2005) Trends Cell Biol. , vol.15 , pp. 599-607
    • Martin, P.1    Leibovich, S.J.2
  • 20
    • 22044432145 scopus 로고    scopus 로고
    • p85alpha subunit of class IA PI-3 kinase is crucial for macrophage growth and migration
    • Munugalavadla V., Borneo J., Ingram D.A., and Kapur R. p85alpha subunit of class IA PI-3 kinase is crucial for macrophage growth and migration. Blood 106 (2005) 103-109
    • (2005) Blood , vol.106 , pp. 103-109
    • Munugalavadla, V.1    Borneo, J.2    Ingram, D.A.3    Kapur, R.4
  • 22
    • 0035933751 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling 1 interacts with the macrophage colony-stimulating factor receptor and negatively regulates its proliferation signal
    • Bourette R.P., De Sepulveda P., Arnaud S., Dubreuil P., Rottapel R., and Mouchiroud G. Suppressor of cytokine signaling 1 interacts with the macrophage colony-stimulating factor receptor and negatively regulates its proliferation signal. J. Biol. Chem. 276 (2001) 22133-22139
    • (2001) J. Biol. Chem. , vol.276 , pp. 22133-22139
    • Bourette, R.P.1    De Sepulveda, P.2    Arnaud, S.3    Dubreuil, P.4    Rottapel, R.5    Mouchiroud, G.6
  • 23
    • 0033169024 scopus 로고    scopus 로고
    • The Cbl protooncoprotein stimulates c-fms/M-CSFR multiubiquitination and endocytosis, and attenuates macrophage proliferation
    • Lee P.S., Wang Y., Dominguez M.G., Yeung Y.G., Murphy M.A., Bowtell D.D., and Stanley E.R. The Cbl protooncoprotein stimulates c-fms/M-CSFR multiubiquitination and endocytosis, and attenuates macrophage proliferation. EMBO J. 18 (1999) 3616-3628
    • (1999) EMBO J. , vol.18 , pp. 3616-3628
    • Lee, P.S.1    Wang, Y.2    Dominguez, M.G.3    Yeung, Y.G.4    Murphy, M.A.5    Bowtell, D.D.6    Stanley, E.R.7
  • 24
    • 0037034167 scopus 로고    scopus 로고
    • c-Cbl binds the c-fms/M-CSFR at tyrosine 973, a novel phosphorylation site in the receptor's carboxy-terminus
    • Wilhelmsen K., Burkhalter S., and van der Geer P. c-Cbl binds the c-fms/M-CSFR at tyrosine 973, a novel phosphorylation site in the receptor's carboxy-terminus. Oncogene 21 (2002) 1079-1089
    • (2002) Oncogene , vol.21 , pp. 1079-1089
    • Wilhelmsen, K.1    Burkhalter, S.2    van der Geer, P.3
  • 25
    • 0037177868 scopus 로고    scopus 로고
    • c-Cbl associates directly with the C-terminal tail of the receptor for the macrophage colony-stimulating factor, c-Fms, and down-modulates this receptor but not the viral oncogene v-Fms
    • Mancini A., Koch A., Wilms R., and Tamura T. c-Cbl associates directly with the C-terminal tail of the receptor for the macrophage colony-stimulating factor, c-Fms, and down-modulates this receptor but not the viral oncogene v-Fms. J. Biol. Chem. 277 (2002) 14635-14640
    • (2002) J. Biol. Chem. , vol.277 , pp. 14635-14640
    • Mancini, A.1    Koch, A.2    Wilms, R.3    Tamura, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.