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Volumn 7, Issue 4, 2007, Pages 320-328

Novel monoclonal antibodies for the investigation of PCH family proteins

Author keywords

Monoclonal antibodies; PCH protein family; Signal transduction; T lymphocytes; Vesicular transport

Indexed keywords

CD2 BINDING PROTEIN; CELL PROTEIN; DEATH RECEPTOR; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY CD2BP1; MONOCLONAL ANTIBODY CIP4; MONOCLONAL ANTIBODY PACSIN1; POMBE CDC15 HOMOLOGY; PROLINE; PROTEIN CD178; PROTEIN CDC42; PROTEIN KINASE C AND CASEIN KINASE SUBSTRATE IN NEURONS 1; PROTEIN SH3; UNCLASSIFIED DRUG;

EID: 34548294257     PISSN: 16154053     EISSN: 16154061     Source Type: Journal    
DOI: 10.1002/sita.200600130     Document Type: Article
Times cited : (3)

References (27)
  • 1
    • 0034656215 scopus 로고    scopus 로고
    • Involvement of PCH family proteins in cytokinesis and actin distribution
    • Lippincott, J., Li, R. (2000) Involvement of PCH family proteins in cytokinesis and actin distribution. Microsc. Res. Tech. 49: 168-172.
    • (2000) Microsc. Res. Tech , vol.49 , pp. 168-172
    • Lippincott, J.1    Li, R.2
  • 2
    • 4344619558 scopus 로고    scopus 로고
    • The syndapin protein family: Linking membrane trafficking with the cytoskeleton
    • Kessels, M.M., Qualmann, B. (2004) The syndapin protein family: linking membrane trafficking with the cytoskeleton. J. Cell Sci. 117: 3077-3086.
    • (2004) J. Cell Sci , vol.117 , pp. 3077-3086
    • Kessels, M.M.1    Qualmann, B.2
  • 3
    • 33751204126 scopus 로고    scopus 로고
    • Pombe Cdc15 homology proteins: Regulators of membrane dynamics and the actin cytoskeleton
    • Aspenstrom, P., Fransson, A., Richnau, N. (2006) Pombe Cdc15 homology proteins: regulators of membrane dynamics and the actin cytoskeleton. Trends Biochem. Sci. 31: 670-679.
    • (2006) Trends Biochem. Sci , vol.31 , pp. 670-679
    • Aspenstrom, P.1    Fransson, A.2    Richnau, N.3
  • 4
    • 0031194076 scopus 로고    scopus 로고
    • A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton
    • Aspenstrom, P. (1997) A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton. Curr. Biol. 7: 479-487.
    • (1997) Curr. Biol , vol.7 , pp. 479-487
    • Aspenstrom, P.1
  • 5
    • 28444452974 scopus 로고    scopus 로고
    • Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins
    • Itoh, T., Erdmann, K.S., Roux, A., Habermann, B., et al. (2005) Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Dev. Cell 9: 791-804.
    • (2005) Dev. Cell , vol.9 , pp. 791-804
    • Itoh, T.1    Erdmann, K.S.2    Roux, A.3    Habermann, B.4
  • 6
    • 30944435279 scopus 로고    scopus 로고
    • Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis
    • Tsujita, K., Suetsugu, S., Sasaki, N., Furutani, M., et al. (2006) Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis. J. Cell Biol. 172: 269-279.
    • (2006) J. Cell Biol , vol.172 , pp. 269-279
    • Tsujita, K.1    Suetsugu, S.2    Sasaki, N.3    Furutani, M.4
  • 7
    • 1442317538 scopus 로고    scopus 로고
    • BAR domains as sensors of membrane curvature: The amphiphysin BAR structure
    • Peter, B.J., Kent, H.M., Mills, I.G., Vallis, Y., et al. (2004) BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. Science 303: 495-499.
    • (2004) Science , vol.303 , pp. 495-499
    • Peter, B.J.1    Kent, H.M.2    Mills, I.G.3    Vallis, Y.4
  • 8
    • 4544251239 scopus 로고    scopus 로고
    • A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis
    • Kamioka, Y., Fukuhara, S., Sawa, H., Nagashima, K. et al. (2004) A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis. J. Biol. Chem. 279: 40091-40099.
    • (2004) J. Biol. Chem , vol.279 , pp. 40091-40099
    • Kamioka, Y.1    Fukuhara, S.2    Sawa, H.3    Nagashima, K.4
  • 9
    • 0034677932 scopus 로고    scopus 로고
    • Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules
    • Tian, L., Nelson, D.L., Stewart, D.M. (2000) Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules. J. Biol. Chem. 275: 7854-7861.
    • (2000) J. Biol. Chem , vol.275 , pp. 7854-7861
    • Tian, L.1    Nelson, D.L.2    Stewart, D.M.3
  • 10
    • 3242671847 scopus 로고    scopus 로고
    • Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex
    • Ho, H.Y., Rohatgi, R., Lebensohn, A.M., Le, M., et al. (2004) Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex. Cell 118: 203-216.
    • (2004) Cell , vol.118 , pp. 203-216
    • Ho, H.Y.1    Rohatgi, R.2    Lebensohn, A.M.3    Le, M.4
  • 11
    • 0032535449 scopus 로고    scopus 로고
    • A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion
    • Li, J., Nishizawa, K., An, W., Hussey, R.E., et al. (1998) A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion. EMBO J. 17: 7320-7336.
    • (1998) EMBO J , vol.17 , pp. 7320-7336
    • Li, J.1    Nishizawa, K.2    An, W.3    Hussey, R.E.4
  • 12
    • 33646492488 scopus 로고    scopus 로고
    • CD2BP1 modulates CD2-dependent T cell activation via linkage to protein tyrosine phosphatase (PTP)-PEST
    • Yang, H., Reinherz, E.L. (2006) CD2BP1 modulates CD2-dependent T cell activation via linkage to protein tyrosine phosphatase (PTP)-PEST. J. Immunol. 176: 5898-5907.
    • (2006) J. Immunol , vol.176 , pp. 5898-5907
    • Yang, H.1    Reinherz, E.L.2
  • 13
    • 0037241232 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome protein acts downstream of CD2 and the CD2AP and PSTPIP1 adaptors to promote formation of the immunological synapse
    • Badour, K., Zhang, J., Shi, F., McGavin, M.K., et al. (2003) The Wiskott-Aldrich syndrome protein acts downstream of CD2 and the CD2AP and PSTPIP1 adaptors to promote formation of the immunological synapse. Immunity. 18: 141-154.
    • (2003) Immunity , vol.18 , pp. 141-154
    • Badour, K.1    Zhang, J.2    Shi, F.3    McGavin, M.K.4
  • 14
    • 0032489515 scopus 로고    scopus 로고
    • Tyrosine phosphorylation regulates the SH3-mediated binding of the Wiskott-Aldrich syndrome protein to PSTPIP, a cytoskeletal-associated protein
    • Wu, Y., Spencer, S.D., Lasky, L.A. (1998) Tyrosine phosphorylation regulates the SH3-mediated binding of the Wiskott-Aldrich syndrome protein to PSTPIP, a cytoskeletal-associated protein. J. Biol. Chem. 273: 5765-5770.
    • (1998) J. Biol. Chem , vol.273 , pp. 5765-5770
    • Wu, Y.1    Spencer, S.D.2    Lasky, L.A.3
  • 15
    • 0032919866 scopus 로고    scopus 로고
    • Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein
    • Qualmann, B., Roos, J., DiGregorio, P.J., Kelly, R.B. (1999) Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein. Mol. Biol. Cell 10: 501-513.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 501-513
    • Qualmann, B.1    Roos, J.2    DiGregorio, P.J.3    Kelly, R.B.4
  • 16
    • 0034526495 scopus 로고    scopus 로고
    • Dynamin and its role in membrane fission
    • Hinshaw, J.E. (2000) Dynamin and its role in membrane fission. Annu. Rev. Cell Dev. Biol. 16: 483-519.
    • (2000) Annu. Rev. Cell Dev. Biol , vol.16 , pp. 483-519
    • Hinshaw, J.E.1
  • 17
    • 0034605101 scopus 로고    scopus 로고
    • Dynamim:GTP controls the formation of constricted coated pits, the rate limiting step in clathrin-mediated endocytosis
    • Sever, S., Damke, H., Schmid, S.L. (2000) Dynamim:GTP controls the formation of constricted coated pits, the rate limiting step in clathrin-mediated endocytosis. J. Cell Biol. 150: 1137-1148.
    • (2000) J. Cell Biol , vol.150 , pp. 1137-1148
    • Sever, S.1    Damke, H.2    Schmid, S.L.3
  • 18
    • 0037157139 scopus 로고    scopus 로고
    • Identification of interaction partners of the cytosolic polyproline region of CD95 ligand (CD178)
    • Ghadimi, M.P., Sanzenbacher, R., Thiede, B., Wenzel, J., et al. (2002) Identification of interaction partners of the cytosolic polyproline region of CD95 ligand (CD178). FEBS Lett. 519: 50-58.
    • (2002) FEBS Lett , vol.519 , pp. 50-58
    • Ghadimi, M.P.1    Sanzenbacher, R.2    Thiede, B.3    Wenzel, J.4
  • 21
    • 33746289906 scopus 로고    scopus 로고
    • Qian.J., Chen, W., Lettau, M., Podda, G., et al. (2006) Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL. Cell. Signal. 18: 1327-1337.
    • Qian.J., Chen, W., Lettau, M., Podda, G., et al. (2006) Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL. Cell. Signal. 18: 1327-1337.
  • 22
    • 33845781550 scopus 로고    scopus 로고
    • Secretory lysosomes and their cargo in T and NK cells
    • Lettau, M., Schmidt, H., Kabelitz, D., Janssen, O. (2007) Secretory lysosomes and their cargo in T and NK cells. Immunol. Lett. 108: 10-19.
    • (2007) Immunol. Lett , vol.108 , pp. 10-19
    • Lettau, M.1    Schmidt, H.2    Kabelitz, D.3    Janssen, O.4
  • 23
    • 12144251368 scopus 로고    scopus 로고
    • Activation-dependent FasL expression in T lymphocytes and Natural Killer cells
    • Lettau, M., Qian, J., Kabelitz, D., Janssen, O. (2004) Activation-dependent FasL expression in T lymphocytes and Natural Killer cells. Signal Transduction 4: 206-211.
    • (2004) Signal Transduction , vol.4 , pp. 206-211
    • Lettau, M.1    Qian, J.2    Kabelitz, D.3    Janssen, O.4
  • 24
    • 33645829585 scopus 로고    scopus 로고
    • The adaptor protein Nck interacts with Fas ligand: Guiding the death factor to the cytotoxic immunological synapse
    • Lettau, M., Qian, J., Linkermann, A., Latreille, M. et al. (2006) The adaptor protein Nck interacts with Fas ligand: Guiding the death factor to the cytotoxic immunological synapse. Proc. Natl. Acad. Sci. U. S. A. 103: 5911-5916.
    • (2006) Proc. Natl. Acad. Sci. U. S. A , vol.103 , pp. 5911-5916
    • Lettau, M.1    Qian, J.2    Linkermann, A.3    Latreille, M.4
  • 25
    • 28844438238 scopus 로고    scopus 로고
    • Binding of the intracellular Fas ligand (FasL) domain to the adaptor protein PSTPIP results in a cytoplasmic localization of FasL
    • Baum, W., Kirkin, V., Fernandez, S.B., Pick, R., et al. (2005) Binding of the intracellular Fas ligand (FasL) domain to the adaptor protein PSTPIP results in a cytoplasmic localization of FasL. J. Biol. Chem. 280: 40012-40024.
    • (2005) J. Biol. Chem , vol.280 , pp. 40012-40024
    • Baum, W.1    Kirkin, V.2    Fernandez, S.B.3    Pick, R.4
  • 26
    • 0347915637 scopus 로고    scopus 로고
    • Fyn and PTP-PEST-mediated regulation of Wiskott-Aldrich syndrome protein (WASp) tyrosine phosphorylation is required for coupling T cell antigen receptor engagement to WASp effector function and T cell activation
    • Badour, K., Zhang, J., Shi, F., Leng, Y., et al. (2004) Fyn and PTP-PEST-mediated regulation of Wiskott-Aldrich syndrome protein (WASp) tyrosine phosphorylation is required for coupling T cell antigen receptor engagement to WASp effector function and T cell activation. J. Exp. Med. 199: 99-112.
    • (2004) J. Exp. Med , vol.199 , pp. 99-112
    • Badour, K.1    Zhang, J.2    Shi, F.3    Leng, Y.4
  • 27
    • 0030872948 scopus 로고    scopus 로고
    • PSTPIP: A tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for a PEST tyrosine phosphatase
    • Spencer, S., Dowbenko, D., Cheng, J., Li, W., et al. (1997) PSTPIP: a tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for a PEST tyrosine phosphatase. J. Cell Biol. 138: 845-860.
    • (1997) J. Cell Biol , vol.138 , pp. 845-860
    • Spencer, S.1    Dowbenko, D.2    Cheng, J.3    Li, W.4


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