메뉴 건너뛰기




Volumn 315, Issue 10, 2009, Pages 1734-1744

CD148/DEP-1 association with areas of cytoskeletal organisation in macrophages

Author keywords

Cytoskeleton; Macrophage; Tyrosine phosphatase

Indexed keywords

CD148 PROTEIN; COLONY STIMULATING FACTOR 1; DEP 1 PROTEIN; PROTEIN KINASE B; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE; UNCLASSIFIED DRUG;

EID: 67349225653     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2009.02.023     Document Type: Article
Times cited : (11)

References (44)
  • 1
    • 0032322136 scopus 로고    scopus 로고
    • The role of the macrophage in immune regulation
    • Gordon S. The role of the macrophage in immune regulation. Res. Immunol. 149 (1998) 685-688
    • (1998) Res. Immunol. , vol.149 , pp. 685-688
    • Gordon, S.1
  • 3
    • 0000172885 scopus 로고
    • Identification and subcellular localization of proteins that are rapidly phosphorylated in tyrosine in response to colony-stimulating factor 1
    • Sengupta A., Liu W.K., Yeung Y.G., Yeung D.C., Frackelton Jr. A.R., and Stanley E.R. Identification and subcellular localization of proteins that are rapidly phosphorylated in tyrosine in response to colony-stimulating factor 1. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 8062-8066
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 8062-8066
    • Sengupta, A.1    Liu, W.K.2    Yeung, Y.G.3    Yeung, D.C.4    Frackelton Jr., A.R.5    Stanley, E.R.6
  • 4
    • 32344441627 scopus 로고    scopus 로고
    • Proteomic approaches to the analysis of early events in colony-stimulating factor-1 signal transduction
    • Yeung Y.G., and Stanley E.R. Proteomic approaches to the analysis of early events in colony-stimulating factor-1 signal transduction. Mol. Cell. Proteomics 2 (2003) 1143-1155
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1143-1155
    • Yeung, Y.G.1    Stanley, E.R.2
  • 5
    • 0033782189 scopus 로고    scopus 로고
    • ets-2 is a target for an akt (Protein kinase B)/jun N-terminal kinase signaling pathway in macrophages of motheaten-viable mutant mice
    • Smith J.L., Schaffner A.E., Hofmeister J.K., Hartman M., Wei G., Forsthoefel D., Hume D.A., and Ostrowski M.C. ets-2 is a target for an akt (Protein kinase B)/jun N-terminal kinase signaling pathway in macrophages of motheaten-viable mutant mice. Mol. Cell. Biol. 20 (2000) 8026-8034
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8026-8034
    • Smith, J.L.1    Schaffner, A.E.2    Hofmeister, J.K.3    Hartman, M.4    Wei, G.5    Forsthoefel, D.6    Hume, D.A.7    Ostrowski, M.C.8
  • 6
    • 0030954854 scopus 로고    scopus 로고
    • Abnormal development and differentiation of macrophages and dendritic cells in viable motheaten mutant mice deficient in haematopoietic cell phosphatase
    • Nakayama K.I., Takahashi K., Shultz L.D., Miyakawa K., and Tomita K. Abnormal development and differentiation of macrophages and dendritic cells in viable motheaten mutant mice deficient in haematopoietic cell phosphatase. Int. J. Exp. Pathol. 78 (1997) 245-257
    • (1997) Int. J. Exp. Pathol. , vol.78 , pp. 245-257
    • Nakayama, K.I.1    Takahashi, K.2    Shultz, L.D.3    Miyakawa, K.4    Tomita, K.5
  • 7
    • 0030764557 scopus 로고    scopus 로고
    • Severe defects in immunity and hematopoiesis caused by SHP-1 protein-tyrosine-phosphatase deficiency
    • Shultz L.D., Rajan T.V., and Greiner D.L. Severe defects in immunity and hematopoiesis caused by SHP-1 protein-tyrosine-phosphatase deficiency. Trends Biotechnol. 15 (1997) 302-307
    • (1997) Trends Biotechnol. , vol.15 , pp. 302-307
    • Shultz, L.D.1    Rajan, T.V.2    Greiner, D.L.3
  • 8
    • 3543036342 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion
    • Yu D.H., Qu C.K., Henegariu O., Lu X., and Feng G.S. Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion. J. Biol. Chem. 273 (1998) 21125-21131
    • (1998) J. Biol. Chem. , vol.273 , pp. 21125-21131
    • Yu, D.H.1    Qu, C.K.2    Henegariu, O.3    Lu, X.4    Feng, G.S.5
  • 9
    • 33748068089 scopus 로고    scopus 로고
    • New concepts regarding focal adhesion kinase promotion of cell migration and proliferation
    • Cox B.D., Natarajan M., Stettner M.R., and Gladson C.L. New concepts regarding focal adhesion kinase promotion of cell migration and proliferation. J. Cell. Biochem. 99 (2006) 35-52
    • (2006) J. Cell. Biochem. , vol.99 , pp. 35-52
    • Cox, B.D.1    Natarajan, M.2    Stettner, M.R.3    Gladson, C.L.4
  • 11
    • 0035136875 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase phi regulates paxillin tyrosine phosphorylation and mediates colony-stimulating factor 1-induced morphological changes in macrophages
    • Pixley F.J., Lee P.S., Condeelis J.S., and Stanley E.R. Protein tyrosine phosphatase phi regulates paxillin tyrosine phosphorylation and mediates colony-stimulating factor 1-induced morphological changes in macrophages. Mol. Cell. Biol. 21 (2001) 1795-1809
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1795-1809
    • Pixley, F.J.1    Lee, P.S.2    Condeelis, J.S.3    Stanley, E.R.4
  • 12
    • 0028051306 scopus 로고
    • Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density
    • Ostman A., Yang Q., and Tonks N.K. Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 9680-9684
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 9680-9684
    • Ostman, A.1    Yang, Q.2    Tonks, N.K.3
  • 14
    • 4043107043 scopus 로고    scopus 로고
    • Regulated expression of the receptor-like tyrosine phosphatase CD148 on hemopoietic cells
    • Lin J., Zhu J.W., Baker J.E., and Weiss A. Regulated expression of the receptor-like tyrosine phosphatase CD148 on hemopoietic cells. J. Immunol. 173 (2004) 2324-2330
    • (2004) J. Immunol. , vol.173 , pp. 2324-2330
    • Lin, J.1    Zhu, J.W.2    Baker, J.E.3    Weiss, A.4
  • 16
    • 0029789246 scopus 로고    scopus 로고
    • The protein tyrosine phosphatase DEP-1 is induced during differentiation and inhibits growth of breast cancer cells
    • Keane M.M., Lowrey G.A., Ettenberg S.A., Dayton M.A., and Lipkowitz S. The protein tyrosine phosphatase DEP-1 is induced during differentiation and inhibits growth of breast cancer cells. Cancer Res. 56 (1996) 4236-4243
    • (1996) Cancer Res. , vol.56 , pp. 4236-4243
    • Keane, M.M.1    Lowrey, G.A.2    Ettenberg, S.A.3    Dayton, M.A.4    Lipkowitz, S.5
  • 17
    • 21044452876 scopus 로고    scopus 로고
    • The rat tyrosine phosphatase eta increases cell adhesion by activating c-Src through dephosphorylation of its inhibitory phosphotyrosine residue
    • Pera I.L., Iuliano R., Florio T., Susini C., Trapasso F., Santoro M., Chiariotti L., Schettini G., Viglietto G., and Fusco A. The rat tyrosine phosphatase eta increases cell adhesion by activating c-Src through dephosphorylation of its inhibitory phosphotyrosine residue. Oncogene 24 (2005) 3187-3195
    • (2005) Oncogene , vol.24 , pp. 3187-3195
    • Pera, I.L.1    Iuliano, R.2    Florio, T.3    Susini, C.4    Trapasso, F.5    Santoro, M.6    Chiariotti, L.7    Schettini, G.8    Viglietto, G.9    Fusco, A.10
  • 18
    • 0034717163 scopus 로고    scopus 로고
    • Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1
    • Kovalenko M., Denner K., Sandstrom J., Persson C., Gross S., Jandt E., Vilella R., Bohmer F., and Ostman A. Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1. J. Biol. Chem. 275 (2000) 16219-16226
    • (2000) J. Biol. Chem. , vol.275 , pp. 16219-16226
    • Kovalenko, M.1    Denner, K.2    Sandstrom, J.3    Persson, C.4    Gross, S.5    Jandt, E.6    Vilella, R.7    Bohmer, F.8    Ostman, A.9
  • 19
    • 0037458646 scopus 로고    scopus 로고
    • Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1
    • Palka H.L., Park M., and Tonks N.K. Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1. J. Biol. Chem. 278 (2003) 5728-5735
    • (2003) J. Biol. Chem. , vol.278 , pp. 5728-5735
    • Palka, H.L.1    Park, M.2    Tonks, N.K.3
  • 20
    • 33747165872 scopus 로고    scopus 로고
    • Vascular endothelial cadherin controls VEGFR-2 internalization and signaling from intracellular compartments
    • Lampugnani M.G., Orsenigo F., Gagliani M.C., Tacchetti C., and Dejana E. Vascular endothelial cadherin controls VEGFR-2 internalization and signaling from intracellular compartments. J.Cell Biol. 174 (2006) 593-604
    • (2006) J.Cell Biol. , vol.174 , pp. 593-604
    • Lampugnani, M.G.1    Orsenigo, F.2    Gagliani, M.C.3    Tacchetti, C.4    Dejana, E.5
  • 21
    • 46249118646 scopus 로고    scopus 로고
    • The tyrosine phosphatase CD148 interacts with the p85 regulatory subunit of phosphoinositide 3-kinase
    • Tsuboi N., Utsunomiya T., Roberts R.L., Ito H., Takahashi K., Noda M., and Takahashi T. The tyrosine phosphatase CD148 interacts with the p85 regulatory subunit of phosphoinositide 3-kinase. Biochem. J. 413 (2008) 193-200
    • (2008) Biochem. J. , vol.413 , pp. 193-200
    • Tsuboi, N.1    Utsunomiya, T.2    Roberts, R.L.3    Ito, H.4    Takahashi, K.5    Noda, M.6    Takahashi, T.7
  • 22
    • 0035102841 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylation
    • Baker J.E., Majeti R., Tangye S.G., and Weiss A. Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylation. Mol. Cell. Biol. 21 (2001) 2393-2403
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2393-2403
    • Baker, J.E.1    Majeti, R.2    Tangye, S.G.3    Weiss, A.4
  • 23
    • 0041976988 scopus 로고    scopus 로고
    • The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling
    • Lin J., and Weiss A. The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling. J. Cell Biol. 162 (2003) 673-682
    • (2003) J. Cell Biol. , vol.162 , pp. 673-682
    • Lin, J.1    Weiss, A.2
  • 24
    • 0032194157 scopus 로고    scopus 로고
    • CD148: a receptor-type protein tyrosine phosphatase involved in the regulation of human T cell activation
    • Tangye S.G., Phillips J.H., Lanier L.L., de Vries J.E., and Aversa G. CD148: a receptor-type protein tyrosine phosphatase involved in the regulation of human T cell activation. J. Immunol. 161 (1998) 3249-3255
    • (1998) J. Immunol. , vol.161 , pp. 3249-3255
    • Tangye, S.G.1    Phillips, J.H.2    Lanier, L.L.3    de Vries, J.E.4    Aversa, G.5
  • 25
  • 27
    • 39149139617 scopus 로고    scopus 로고
    • Structurally distinct phosphatases CD45 and CD148 both regulate B cell and macrophage immunoreceptor signaling
    • Zhu J.W., Brdicka T., Katsumoto T.R., Lin J., and Weiss A. Structurally distinct phosphatases CD45 and CD148 both regulate B cell and macrophage immunoreceptor signaling. Immunity 28 (2008) 183-196
    • (2008) Immunity , vol.28 , pp. 183-196
    • Zhu, J.W.1    Brdicka, T.2    Katsumoto, T.R.3    Lin, J.4    Weiss, A.5
  • 28
    • 1242329400 scopus 로고    scopus 로고
    • The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation
    • Kellie S., Craggs G., Bird I.N., and Jones G.E. The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation. J. Cell. Sci. 117 (2004) 609-618
    • (2004) J. Cell. Sci. , vol.117 , pp. 609-618
    • Kellie, S.1    Craggs, G.2    Bird, I.N.3    Jones, G.E.4
  • 30
    • 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. Cytoskelet. 63 (2006) 132-140
    • (2006) Cell Motil. Cytoskelet. , vol.63 , pp. 132-140
    • Wheeler, A.P.1    Smith, S.D.2    Ridley, A.J.3
  • 31
    • 0034651941 scopus 로고    scopus 로고
    • Lipopolysaccharide induces actin reorganization and tyrosine phosphorylation of Pyk2 and paxillin in monocytes and macrophages
    • Williams L.M., and Ridley A.J. Lipopolysaccharide induces actin reorganization and tyrosine phosphorylation of Pyk2 and paxillin in monocytes and macrophages. J. Immunol. 164 (2000) 2028-2036
    • (2000) J. Immunol. , vol.164 , pp. 2028-2036
    • Williams, L.M.1    Ridley, A.J.2
  • 32
    • 0024361531 scopus 로고
    • Colony-stimulating factor-1 induces rapid behavioural responses in the mouse macrophage cell line, BAC1.2F5
    • Boocock C.A., Jones G.E., Stanley E.R., and Pollard J.W. Colony-stimulating factor-1 induces rapid behavioural responses in the mouse macrophage cell line, BAC1.2F5. J. Cell. Sci. 93 Pt 3 (1989) 447-456
    • (1989) J. Cell. Sci. , vol.93 , Issue.PART 3 , pp. 447-456
    • Boocock, C.A.1    Jones, G.E.2    Stanley, E.R.3    Pollard, J.W.4
  • 33
    • 29244432463 scopus 로고    scopus 로고
    • A WAVE2-Abi1 complex mediates CSF-1-induced F-actin-rich membrane protrusions and migration in macrophages
    • Kheir W.A., Gevrey J.C., Yamaguchi H., Isaac B., and Cox D. A WAVE2-Abi1 complex mediates CSF-1-induced F-actin-rich membrane protrusions and migration in macrophages. J. Cell. Sci. 118 (2005) 5369-5379
    • (2005) J. Cell. Sci. , vol.118 , pp. 5369-5379
    • Kheir, W.A.1    Gevrey, J.C.2    Yamaguchi, H.3    Isaac, B.4    Cox, D.5
  • 34
    • 0037165628 scopus 로고    scopus 로고
    • Primary sequence determinants responsible for site-selective dephosphorylation of the PDGF beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1
    • Persson C., Engstrom U., Mowbray S.L., and Ostman A. Primary sequence determinants responsible for site-selective dephosphorylation of the PDGF beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1. FEBS Lett. 517 (2002) 27-31
    • (2002) FEBS Lett. , vol.517 , pp. 27-31
    • Persson, C.1    Engstrom, U.2    Mowbray, S.L.3    Ostman, A.4
  • 35
    • 0034177683 scopus 로고    scopus 로고
    • Regulation of urokinase plasminogen activator gene transcription in the RAW264 murine macrophage cell line by macrophage colony-stimulating factor (CSF-1) is dependent upon the level of cell-surface receptor
    • Fowles L.F., Stacey K.J., Marks D., Hamilton J.A., and Hume D.A. Regulation of urokinase plasminogen activator gene transcription in the RAW264 murine macrophage cell line by macrophage colony-stimulating factor (CSF-1) is dependent upon the level of cell-surface receptor. Biochem. J. 347 (2000) 313-320
    • (2000) Biochem. J. , vol.347 , pp. 313-320
    • Fowles, L.F.1    Stacey, K.J.2    Marks, D.3    Hamilton, J.A.4    Hume, D.A.5
  • 37
    • 19644380374 scopus 로고    scopus 로고
    • The PCH family member MAYP/PSTPIP2 directly regulates F-actin bundling and enhances filopodia formation and motility in macrophages
    • Chitu V., Pixley F.J., Macaluso F., Larson D.R., Condeelis J., Yeung Y.G., and Stanley E.R. The PCH family member MAYP/PSTPIP2 directly regulates F-actin bundling and enhances filopodia formation and motility in macrophages. Mol. Biol. Cell 16 (2005) 2947-2959
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2947-2959
    • Chitu, V.1    Pixley, F.J.2    Macaluso, F.3    Larson, D.R.4    Condeelis, J.5    Yeung, Y.G.6    Stanley, E.R.7
  • 39
    • 0033743866 scopus 로고    scopus 로고
    • PYK2 is an adhesion kinase in macrophages, localized in podosomes and activated by beta(2)-integrin ligation
    • Duong L.T., and Rodan G.A. PYK2 is an adhesion kinase in macrophages, localized in podosomes and activated by beta(2)-integrin ligation. Cell Motil. Cytoskelet. 47 (2000) 174-188
    • (2000) Cell Motil. Cytoskelet. , vol.47 , pp. 174-188
    • Duong, L.T.1    Rodan, G.A.2
  • 42
    • 58149457090 scopus 로고    scopus 로고
    • New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival
    • Chabot C., Spring K., Gratton J.P., Elchebly M., and Royal I. New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival. Mol. Cell. Biol. 29 (2009) 241-253
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 241-253
    • Chabot, C.1    Spring, K.2    Gratton, J.P.3    Elchebly, M.4    Royal, I.5
  • 43
    • 0027266773 scopus 로고
    • Ligand-mediated negative regulation of a chimeric transmembrane receptor tyrosine phosphatase
    • Desai D.M., Sap J., Schlessinger J., and Weiss A. Ligand-mediated negative regulation of a chimeric transmembrane receptor tyrosine phosphatase. Cell 73 (1993) 541-554
    • (1993) Cell , vol.73 , pp. 541-554
    • Desai, D.M.1    Sap, J.2    Schlessinger, J.3    Weiss, A.4
  • 44
    • 0034704180 scopus 로고    scopus 로고
    • An inactivating point mutation in the inhibitory wedge of CD45 causes lymphoproliferation and autoimmunity
    • Majeti R., Xu Z., Parslow T.G., Olson J.L., Daikh D.I., Killeen N., and Weiss A. An inactivating point mutation in the inhibitory wedge of CD45 causes lymphoproliferation and autoimmunity. Cell 103 (2000) 1059-1070
    • (2000) Cell , vol.103 , pp. 1059-1070
    • Majeti, R.1    Xu, Z.2    Parslow, T.G.3    Olson, J.L.4    Daikh, D.I.5    Killeen, N.6    Weiss, A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.