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Volumn 287, Issue 12, 2012, Pages 9013-9027

Novel roles for the E3 ubiquitin ligase atrophin-interacting protein 4 and signal transduction adaptor molecule 1 in G protein-coupled receptor signaling

Author keywords

[No Author keywords available]

Indexed keywords

CAVEOLAE; ENDOSOMAL SORTING COMPLEX REQUIRED FOR TRANSPORTS; G PROTEIN COUPLED RECEPTORS; HUMAN HEALTH; INACTIVE MUTANTS; LIGASE ACTIVITY; MICRO-DOMAINS; MOLECULAR MECHANISM; NOVEL FUNCTIONS; OVER-EXPRESSION; SIGNAL-TRANSDUCTION ADAPTOR MOLECULES; UBIQUITIN; UBIQUITIN LIGASES; UBIQUITINATION; WILD TYPES;

EID: 84858609378     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.336792     Document Type: Article
Times cited : (41)

References (64)
  • 1
    • 77957065896 scopus 로고    scopus 로고
    • Role of cardiac myocyte CXCR4 expression in development and left ventricular remodeling after acute myocardial infarction
    • Agarwal, U., Ghalayini, W., Dong, F., Weber, K., Zou, Y. R., Rabbany, S. Y., Rafii, S., and Penn, M. S. (2010) Role of cardiac myocyte CXCR4 expression in development and left ventricular remodeling after acute myocardial infarction. Circ. Res. 107, 667-676
    • (2010) Circ. Res. , vol.107 , pp. 667-676
    • Agarwal, U.1    Ghalayini, W.2    Dong, F.3    Weber, K.4    Zou, Y.R.5    Rabbany, S.Y.6    Rafii, S.7    Penn, M.S.8
  • 4
    • 0032507962 scopus 로고    scopus 로고
    • Function of the chemokine receptor CXCR4 in heaematopolesis and in cerebellar development
    • DOI 10.1038/31269
    • Zou, Y. R., Kottmann, A. H., Kuroda, M., Taniuchi, I., and Littman, D. R. (1998) Function of the chemokine receptor CXCR4 in haematopoiesis and in cerebellar development. Nature 393, 595-599 (Pubitemid 28319251)
    • (1998) Nature , vol.393 , Issue.6685 , pp. 595-599
    • Zou, Y.-R.1    Kottman, A.H.2    Kuroda, M.3    Taniuchi, I.4    Littman, D.R.5
  • 5
    • 0037656291 scopus 로고    scopus 로고
    • Mutations in the chemokine receptor gene CXCR4 are associated with WHIM syndrome, a combined immunodeficiency disease
    • DOI 10.1038/ng1149
    • Hernandez, P. A., Gorlin, R. J., Lukens, J. N., Taniuchi, S., Bohinjec, J., Francois, F., Klotman, M. E., and Diaz, G. A. (2003) Mutations in the chemokine receptor gene CXCR4 are associated with WHIM syndrome, a combined immunodeficiency disease. Nat. Genet. 34, 70-74 (Pubitemid 36548793)
    • (2003) Nature Genetics , vol.34 , Issue.1 , pp. 70-74
    • Hernandez, P.A.1    Gorlin, R.J.2    Lukens, J.N.3    Taniuchi, S.4    Bohinjec, J.5    Francois, F.6    Klotman, M.E.7    Diaz, G.A.8
  • 8
    • 2342591450 scopus 로고    scopus 로고
    • The significance of cancer cell expression of the chemokine receptor CXCR4
    • Balkwill, F. (2004) The significance of cancer cell expression of the chemokine receptor CXCR4. Semin. Cancer Biol. 14, 171-179
    • (2004) Semin. Cancer Biol. , vol.14 , pp. 171-179
    • Balkwill, F.1
  • 9
  • 10
    • 18844428327 scopus 로고    scopus 로고
    • Stromal fibroblasts present in invasive human breast carcinomas promote tumor growth and angiogenesis through elevated SDF-1/CXCL12 secretion
    • DOI 10.1016/j.cell.2005.02.034, PII S0092867405002370
    • Orimo, A., Gupta, P. B., Sgroi, D. C., Arenzana-Seisdedos, F., Delaunay, T., Naeem, R., Carey, V. J., Richardson, A. L., and Weinberg, R. A. (2005) Stromal fibroblasts present in invasive human breast carcinomas promote tumor growth and angiogenesis through elevated SDF-1/CXCL12 secretion. Cell 121, 335-348 (Pubitemid 40692295)
    • (2005) Cell , vol.121 , Issue.3 , pp. 335-348
    • Orimo, A.1    Gupta, P.B.2    Sgroi, D.C.3    Arenzana-Seisdedos, F.4    Delaunay, T.5    Naeem, R.6    Carey, V.J.7    Richardson, A.L.8    Weinberg, R.A.9
  • 12
    • 4143070533 scopus 로고    scopus 로고
    • Differential kinetic and spatial patterns of β-arrestin and G protein-mediated ERK activation by the angiotensin II receptor
    • DOI 10.1074/jbc.M405878200
    • Ahn, S., Shenoy, S. K., Wei, H., and Lefkowitz, R. J. (2004) Differential kinetic and spatial patterns of β-arrestin and G protein-mediated ERK activation by the angiotensin II receptor. J. Biol. Chem. 279, 35518-35525 (Pubitemid 39100552)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.34 , pp. 35518-35525
    • Ahn, S.1    Shenoy, S.K.2    Wei, H.3    Lefkowitz, R.J.4
  • 13
    • 22744449073 scopus 로고    scopus 로고
    • An Akt/β-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior
    • DOI 10.1016/j.cell.2005.05.012, PII S0092867405004575
    • Beaulieu, J. M., Sotnikova, T. D., Marion, S., Lefkowitz, R. J., Gainetdinov, R. R., and Caron, M. G. (2005) An Akt/β-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior. Cell 122, 261-273 (Pubitemid 41032989)
    • (2005) Cell , vol.122 , Issue.2 , pp. 261-273
    • Beaulieu, J.-M.1    Sotnikova, T.D.2    Marion, S.3    Lefkowitz, R.J.4    Gainetdinov, R.R.5    Caron, M.G.6
  • 17
    • 0034718604 scopus 로고    scopus 로고
    • The proliferative and antiapoptotic effects of substance P are facilitated by formation of a β-arrestin-dependent scaffolding complex
    • DeFea, K. A., Vaughn, Z. D., O'Bryan, E. M., Nishijima, D., Déry, O., and Bunnett, N. W. (2000) The proliferative and antiapoptotic effects of substance P are facilitated by formation of a β-arrestin-dependent scaffolding complex. Proc. Natl. Acad. Sci. U.S.A. 97, 11086-11091
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 11086-11091
    • DeFea, K.A.1    Vaughn, Z.D.2    O'Bryan, E.M.3    Nishijima, D.4    Déry, O.5    Bunnett, N.W.6
  • 18
    • 77951230331 scopus 로고    scopus 로고
    • Site-specific phosphorylation of CXCR4 is dynamically regulated by multiple kinases and results in differential modulation of CXCR4 signaling
    • Busillo, J. M., Armando, S., Sengupta, R., Meucci, O., Bouvier, M., and Benovic, J. L. (2010) Site-specific phosphorylation of CXCR4 is dynamically regulated by multiple kinases and results in differential modulation of CXCR4 signaling. J. Biol. Chem. 285, 7805-7817
    • (2010) J. Biol. Chem. , vol.285 , pp. 7805-7817
    • Busillo, J.M.1    Armando, S.2    Sengupta, R.3    Meucci, O.4    Bouvier, M.5    Benovic, J.L.6
  • 19
    • 0037147145 scopus 로고    scopus 로고
    • β-arrestin2 is critically involved in CXCR4-mediated chemotaxis, and this is mediated by its enhancement of p38 MAPK activation
    • DOI 10.1074/jbc.M207294200
    • Sun, Y., Cheng, Z., Ma, L., and Pei, G. (2002) β-Arrestin2 is critically involved in CXCR4-mediated chemotaxis, and this is mediated by its enhancement of p38 MAPK activation. J. Biol. Chem. 277, 49212-49219 (Pubitemid 36014350)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.51 , pp. 49212-49219
    • Sun, Y.1    Cheng, Z.2    Ma, L.3    Pei, G.4
  • 20
    • 33947314576 scopus 로고    scopus 로고
    • Regulation of receptor trafficking by GRKs and arrestins
    • DOI 10.1146/annurev.physiol.69.022405.154712
    • Moore, C. A., Milano, S. K., and Benovic, J. L. (2007) Regulation of receptor trafficking by GRKs and arrestins. Annu. Rev. Physiol. 69, 451-482 (Pubitemid 46457651)
    • (2007) Annual Review of Physiology , vol.69 , pp. 451-482
    • Moore, C.A.C.1    Milano, S.K.2    Benovic, J.L.3
  • 21
    • 0025352299 scopus 로고
    • β-Arrestin. A protein that regulates β-adrenergic receptor function
    • Lohse, M. J., Benovic, J. L., Codina, J., Caron, M. G., and Lefkowitz, R. J. (1990) β-Arrestin. A protein that regulates β-adrenergic receptor function. Science 248, 1547-1550
    • (1990) Science , vol.248 , pp. 1547-1550
    • Lohse, M.J.1    Benovic, J.L.2    Codina, J.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 24
    • 65249115360 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase atrophin-interacting protein 4 binds directly to the chemokine receptor CXCR4 via a novel WW domain-mediated interaction
    • Bhandari, D., Robia, S. L., and Marchese, A. (2009) The E3 ubiquitin ligase atrophin-interacting protein 4 binds directly to the chemokine receptor CXCR4 via a novel WW domain-mediated interaction. Mol. Biol. Cell 20, 1324-1339
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1324-1339
    • Bhandari, D.1    Robia, S.L.2    Marchese, A.3
  • 25
    • 0035824563 scopus 로고    scopus 로고
    • Agonist-promoted ubiquitination of the G protein-coupled receptor CXCR4 mediates lysosomal sorting
    • Marchese, A., and Benovic, J. L. (2001) Agonist-promoted ubiquitination of the G protein-coupled receptor CXCR4 mediates lysosomal sorting. J. Biol. Chem. 276, 45509-45512
    • (2001) J. Biol. Chem. , vol.276 , pp. 45509-45512
    • Marchese, A.1    Benovic, J.L.2
  • 26
    • 37549035071 scopus 로고    scopus 로고
    • Arrestin-2 interacts with the ubiquitin-protein isopeptide ligase atrophin-interacting protein 4 and mediates endosomal sorting of the chemokine receptor CXCR4
    • Bhandari, D., Trejo, J., Benovic, J. L., and Marchese, A. (2007) Arrestin-2 interacts with the ubiquitin-protein isopeptide ligase atrophin-interacting protein 4 and mediates endosomal sorting of the chemokine receptor CXCR4. J. Biol. Chem. 282, 36971-36979
    • (2007) J. Biol. Chem. , vol.282 , pp. 36971-36979
    • Bhandari, D.1    Trejo, J.2    Benovic, J.L.3    Marchese, A.4
  • 27
    • 77954626403 scopus 로고    scopus 로고
    • Arrestin-2 interacts with the endosomal sorting complex required for transport machinery to modulate endosomal sorting of CXCR4
    • Malik, R., and Marchese, A. (2010) Arrestin-2 interacts with the endosomal sorting complex required for transport machinery to modulate endosomal sorting of CXCR4. Mol. Biol. Cell 21, 2529-2541
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2529-2541
    • Malik, R.1    Marchese, A.2
  • 28
    • 0242362743 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase AIP4 mediates ubiquitination and sorting of the G protein-coupled receptor CXCR4
    • DOI 10.1016/S1534-5807(03)00321-6, PII S1534580703003216
    • Marchese, A., Raiborg, C., Santini, F., Keen, J. H., Stenmark, H., and Benovic, J. L. (2003) The E3 ubiquitin ligase AIP4 mediates ubiquitination and sorting of the G protein-coupled receptor CXCR4. Dev. Cell 5, 709-722 (Pubitemid 37362215)
    • (2003) Developmental Cell , vol.5 , Issue.5 , pp. 709-722
    • Marchese, A.1    Raiborg, C.2    Santini, F.3    Keen, J.H.4    Stenmark, H.5    Benovic, J.L.6
  • 29
    • 77954957013 scopus 로고    scopus 로고
    • Membrane budding and scission by the ESCRT machinery. It's all in the neck
    • Hurley, J. H., and Hanson, P. I. (2010) Membrane budding and scission by the ESCRT machinery. It's all in the neck. Nat. Rev. Mol. Cell Biol. 11, 556-566
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 556-566
    • Hurley, J.H.1    Hanson, P.I.2
  • 30
    • 79955828987 scopus 로고    scopus 로고
    • Molecular mechanisms of ubiquitin- dependent membrane traffic
    • Hurley, J. H., and Stenmark, H. (2011) Molecular mechanisms of ubiquitin- dependent membrane traffic. Annu. Rev. Biophys. 40, 119-142
    • (2011) Annu. Rev. Biophys. , vol.40 , pp. 119-142
    • Hurley, J.H.1    Stenmark, H.2
  • 31
    • 0029912981 scopus 로고    scopus 로고
    • Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent- free purification of caveolae microdomains
    • Song, K. S., Li, S., Okamoto, T., Quilliam, L. A., Sargiacomo, M., and Lisanti, M. P. (1996) Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent- free purification of caveolae microdomains. J. Biol. Chem. 271, 9690-9697
    • (1996) J. Biol. Chem. , vol.271 , pp. 9690-9697
    • Song, K.S.1    Li, S.2    Okamoto, T.3    Quilliam, L.A.4    Sargiacomo, M.5    Lisanti, M.P.6
  • 32
    • 79952777210 scopus 로고    scopus 로고
    • Small ubiquitin- like modifier modification of arrestin-3 regulates receptor trafficking
    • Wyatt, D., Malik, R., Vesecky, A. C., and Marchese, A. (2011) Small ubiquitin- like modifier modification of arrestin-3 regulates receptor trafficking. J. Biol. Chem. 286, 3884-3893
    • (2011) J. Biol. Chem. , vol.286 , pp. 3884-3893
    • Wyatt, D.1    Malik, R.2    Vesecky, A.C.3    Marchese, A.4
  • 33
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse, J. M., Scheffner, M., Beaudenon, S., and Howley, P. M. (1995) A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl. Acad. Sci. U.S.A. 92, 2563-2567
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 2563-2567
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 34
    • 0037138411 scopus 로고    scopus 로고
    • WW and SH3 domains, two different scaffolds to recognize proline-rich ligands
    • DOI 10.1016/S0014-5793(01)03290-2, PII S0014579301032902
    • Macias, M. J., Wiesner, S., and Sudol, M. (2002) WW and SH3 domains, two different scaffolds to recognize proline-rich ligands. FEBS Lett. 513, 30-37 (Pubitemid 34242975)
    • (2002) FEBS Letters , vol.513 , Issue.1 , pp. 30-37
    • Macias, M.J.1    Wiesner, S.2    Sudol, M.3
  • 35
    • 2442509573 scopus 로고    scopus 로고
    • The C2 domain of the Rsp5 ubiquitin ligase binds membrane phosphoinositides and directs ubiquitination of endosomal cargo
    • DOI 10.1083/jcb.200309026
    • Dunn, R., Klos, D. A., Adler, A. S., and Hicke, L. (2004) The C2 domain of the Rsp5 ubiquitin ligase binds membrane phosphoinositides and directs ubiquitination of endosomal cargo. J. Cell Biol. 165, 135-144 (Pubitemid 38649183)
    • (2004) Journal of Cell Biology , vol.165 , Issue.1 , pp. 135-144
    • Dunn, R.1    Klos, D.A.2    Adler, A.S.3    Hicke, L.4
  • 37
    • 34547958577 scopus 로고    scopus 로고
    • Autoinhibition of the HECT-Type Ubiquitin Ligase Smurf2 through Its C2 Domain
    • DOI 10.1016/j.cell.2007.06.050, PII S0092867407009002
    • Wiesner, S., Ogunjimi, A. A., Wang, H. R., Rotin, D., Sicheri, F., Wrana, J. L., and Forman-Kay, J. D. (2007) Autoinhibition of the HECT-type ubiquitin ligase Smurf2 through its C2 domain. Cell 130, 651-662 (Pubitemid 47268058)
    • (2007) Cell , vol.130 , Issue.4 , pp. 651-662
    • Wiesner, S.1    Ogunjimi, A.A.2    Wang, H.-R.3    Rotin, D.4    Sicheri, F.5    Wrana, J.L.6    Forman-Kay, J.D.7
  • 38
    • 1642565079 scopus 로고    scopus 로고
    • The HECT Domain Ligase Itch Ubiquitinates Endophilin and Localizes to the trans-Golgi Network and Endosomal System
    • DOI 10.1074/jbc.M309934200
    • Angers, A., Ramjaun, A. R., and McPherson, P. S. (2004) The HECT domain ligase itch ubiquitinates endophilin and localizes to the trans-Golgi network and endosomal system. J. Biol. Chem. 279, 11471-11479 (Pubitemid 38401647)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.12 , pp. 11471-11479
    • Angers, A.1    Ramjaun, A.R.2    McPherson, P.S.3
  • 39
    • 24044540256 scopus 로고    scopus 로고
    • Specificity and versatility of SH3 and other proline-recognition domains. Structural basis and implications for cellular signal transduction
    • Li, S. S. (2005) Specificity and versatility of SH3 and other proline-recognition domains. Structural basis and implications for cellular signal transduction. Biochem. J. 390, 641-653
    • (2005) Biochem. J. , vol.390 , pp. 641-653
    • Li, S.S.1
  • 40
    • 0034682840 scopus 로고    scopus 로고
    • Trafficking of the HIV coreceptor CXCR4. Role of arrestins and identification of residues in the C-terminal tail that mediate receptor internalization
    • Orsini, M. J., Parent, J. L., Mundell, S. J., Marchese, A., and Benovic, J. L. (2000) Trafficking of the HIV coreceptor CXCR4. Role of arrestins and identification of residues in the C-terminal tail that mediate receptor internalization J. Biol. Chem. 275, 25876
    • (2000) J. Biol. Chem. , vol.275 , pp. 25876
    • Orsini, M.J.1    Parent, J.L.2    Mundell, S.J.3    Marchese, A.4    Benovic, J.L.5
  • 41
    • 0037163045 scopus 로고    scopus 로고
    • Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein-coupled receptor trafficking
    • Kim, Y. M., and Benovic, J. L. (2002) Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein-coupled receptor trafficking. J. Biol. Chem. 277, 30760-30768
    • (2002) J. Biol. Chem. , vol.277 , pp. 30760-30768
    • Kim, Y.M.1    Benovic, J.L.2
  • 42
    • 0023228992 scopus 로고
    • 100-kDa coated vesicle proteins. Molecular heterogeneity and intracellular distribution studied with monoclonal antibodies
    • Robinson, M. S. (1987) 100-kDa coated vesicle proteins. Molecular heterogeneity and intracellular distribution studied with monoclonal antibodies. J. Cell Biol. 104, 887-895
    • (1987) J. Cell Biol. , vol.104 , pp. 887-895
    • Robinson, M.S.1
  • 43
    • 0037090162 scopus 로고    scopus 로고
    • CXCR4 function requires membrane cholesterol: Implications for HIV infection
    • Nguyen, D. H., and Taub, D. (2002) CXCR4 function requires membrane cholesterol. Implications for HIV infection. J. Immunol. 168, 4121-4126 (Pubitemid 34298420)
    • (2002) Journal of Immunology , vol.168 , Issue.8 , pp. 4121-4126
    • Nguyen, D.H.1    Taub, D.2
  • 44
    • 41149124594 scopus 로고    scopus 로고
    • Caveolae as organizers of pharmacologically relevant signal transduction molecules
    • DOI 10.1146/annurev.pharmtox.48.121506.124841
    • Patel, H. H., Murray, F., and Insel, P. A. (2008) Caveolae as organizers of pharmacologically relevant signal transduction molecules. Annu. Rev. Pharmacol. Toxicol. 48, 359-391 (Pubitemid 351738158)
    • (2008) Annual Review of Pharmacology and Toxicology , vol.48 , pp. 359-391
    • Patel, H.H.1    Murray, F.2    Insel, P.A.3
  • 45
    • 78049508213 scopus 로고    scopus 로고
    • Caveolin-1 is ubiquitinated and targeted to intralumenal vesicles in endolysosomes for degradation
    • Hayer, A., Stoeber, M., Ritz, D., Engel, S., Meyer, H. H., and Helenius, A. (2010) Caveolin-1 is ubiquitinated and targeted to intralumenal vesicles in endolysosomes for degradation. J. Cell Biol. 191, 615-629
    • (2010) J. Cell Biol. , vol.191 , pp. 615-629
    • Hayer, A.1    Stoeber, M.2    Ritz, D.3    Engel, S.4    Meyer, H.H.5    Helenius, A.6
  • 46
    • 0027997787 scopus 로고
    • Filipin-sensitive caveolae-mediated transport in endothelium: Reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules
    • DOI 10.1083/jcb.127.5.1217
    • Schnitzer, J. E., Oh, P., Pinney, E., and Allard, J. (1994) Filipin-sensitive caveolae-mediated transport in endothelium. Reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules. J. Cell Biol. 127, 1217-1232 (Pubitemid 24362558)
    • (1994) Journal of Cell Biology , vol.127 , Issue.5 , pp. 1217-1232
    • Schnitzer, J.E.1    Oh, P.2    Pinney, E.3    Allard, J.4
  • 48
    • 0034535340 scopus 로고    scopus 로고
    • A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP
    • DOI 10.1074/jbc.M007251200
    • Kato, M., Miyazawa, K., and Kitamura, N. (2000) A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP. J. Biol. Chem. 275, 37481-37487 (Pubitemid 32004855)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.48 , pp. 37481-37487
    • Kato, M.1    Miyazawa, K.2    Kitamura, N.3
  • 51
    • 79951841782 scopus 로고    scopus 로고
    • CXCR4 promotes oral squamous cell carcinoma migration and invasion through inducing expression of MMP-9 and MMP-13 via the ERK signaling pathway
    • Yu, T., Wu, Y., Helman, J. I., Wen, Y., Wang, C., and Li, L. (2011) CXCR4 promotes oral squamous cell carcinoma migration and invasion through inducing expression of MMP-9 and MMP-13 via the ERK signaling pathway. Mol. Cancer Res. 9, 161-172
    • (2011) Mol. Cancer Res. , vol.9 , pp. 161-172
    • Yu, T.1    Wu, Y.2    Helman, J.I.3    Wen, Y.4    Wang, C.5    Li, L.6
  • 52
    • 1842591240 scopus 로고    scopus 로고
    • The Nedd4 family of E3 ubiquitin ligases: Functional diversity within a common modular architecture
    • DOI 10.1038/sj.onc.1207436
    • Ingham, R. J., Gish, G., and Pawson, T. (2004) The Nedd4 family of E3 ubiquitin ligases. Functional diversity within a common modular architecture. Oncogene 23, 1972-1984 (Pubitemid 38496727)
    • (2004) Oncogene , vol.23 , Issue.11 REV. ISS. 1 , pp. 1972-1984
    • Ingham, R.J.1    Gish, G.2    Pawson, T.3
  • 53
    • 73849113734 scopus 로고    scopus 로고
    • Late domain-independent rescue of a release-deficient Moloney murine leukemia virus by the ubiquitin ligase Itch
    • Jadwin, J. A., Rudd, V., Sette, P., Challa, S., and Bouamr, F. (2010) Late domain-independent rescue of a release-deficient Moloney murine leukemia virus by the ubiquitin ligase Itch. J. Virol. 84, 704-715
    • (2010) J. Virol. , vol.84 , pp. 704-715
    • Jadwin, J.A.1    Rudd, V.2    Sette, P.3    Challa, S.4    Bouamr, F.5
  • 54
    • 29344451650 scopus 로고    scopus 로고
    • CXCL12/CXCR4 signaling activates Akt-1 and MMP-9 expression in prostate cancer cells: The role of bone microenvironment-associated CXCL12
    • DOI 10.1002/pros.20318
    • Chinni, S. R., Sivalogan, S., Dong, Z., Filho, J. C., Deng, X., Bonfil, R. D., and Cher, M. L. (2006) CXCL12/CXCR4 signaling activates Akt-1 and MMP-9 expression in prostate cancer cells. The role of bone microenvironment- associated CXCL12. Prostate 66, 32-48 (Pubitemid 43005947)
    • (2006) Prostate , vol.66 , Issue.1 , pp. 32-48
    • Chinni, S.R.1    Sivalogan, S.2    Dong, Z.3    Trindade Filho, J.C.4    Deng, X.5    Bonfil, R.D.6    Cher, M.L.7
  • 55
    • 40949136474 scopus 로고    scopus 로고
    • CXCL12/CXCR4 transactivates HER2 in lipid rafts of prostate cancer cells and promotes growth of metastatic deposits in bone
    • DOI 10.1158/1541-7786.MCR-07-0117
    • Chinni, S. R., Yamamoto, H., Dong, Z., Sabbota, A., Bonfil, R. D., and Cher, M. L. (2008) CXCL12/CXCR4 transactivates HER2 in lipid rafts of prostate cancer cells and promotes growth of metastatic deposits in bone. Mol. Cancer Res. 6, 446-457 (Pubitemid 351416535)
    • (2008) Molecular Cancer Research , vol.6 , Issue.3 , pp. 446-457
    • Chinni, S.R.1    Yamamoto, H.2    Dong, Z.3    Sabbota, A.4    Bonfil, R.D.5    Cher, M.L.6
  • 56
    • 5044225158 scopus 로고    scopus 로고
    • Jun turnover is controlled through JNK-dependent phosphorylation of the E3 ligase itch
    • DOI 10.1126/science.1099414
    • Gao, M., Labuda, T., Xia, Y., Gallagher, E., Fang, D., Liu, Y. C., and Karin, M. (2004) Jun turnover is controlled through JNK-dependent phosphorylation of the E3 ligase Itch. Science 306, 271-275 (Pubitemid 39336871)
    • (2004) Science , vol.306 , Issue.5694 , pp. 271-275
    • Gao, M.1    Labuda, T.2    Xia, Y.3    Gallagher, E.4    Fang, D.5    Liu, Y.-C.6    Karin, M.7
  • 57
    • 70350353084 scopus 로고    scopus 로고
    • MKK4/SEK1 is negatively regulated through a feedback loop involving the E3 ubiquitin ligase Itch
    • Ahn, Y. H., and Kurie, J. M. (2009) MKK4/SEK1 is negatively regulated through a feedback loop involving the E3 ubiquitin ligase Itch. J. Biol. Chem. 284, 29399-29404
    • (2009) J. Biol. Chem. , vol.284 , pp. 29399-29404
    • Ahn, Y.H.1    Kurie, J.M.2
  • 59
    • 2342539846 scopus 로고    scopus 로고
    • ITAM motif in an apoptosis receptor
    • Lohi, O., and Lehto, V. P. (1998) ITAM motif in an apoptosis receptor. Apoptosis 3, 335-336
    • (1998) Apoptosis , vol.3 , pp. 335-336
    • Lohi, O.1    Lehto, V.P.2
  • 61
    • 17044444647 scopus 로고    scopus 로고
    • STAM, signal transducing adaptor molecule, is associated with janus kinases and involved in signaling for cell growth and c-myc induction
    • Takeshita, T., Arita, T., Higuchi, M., Asao, H., Endo, K., Kuroda, H., Tanaka, N., Murata, K., Ishii, N., and Sugamura, K. (1997) STAM, signal-transducing adaptor molecule, is associated with Janus kinases and involved in signaling for cell growth and c-myc induction. Immunity. 6, 449-457 (Pubitemid 27208200)
    • (1997) Immunity , vol.6 , Issue.4 , pp. 449-457
    • Takeshita, T.1    Arita, T.2    Higuchi, M.3    Asao, H.4    Endo, K.5    Kuroda, H.6    Tanaka, N.7    Murata, K.8    Ishii, N.9    Sugamura, K.10
  • 62
    • 0036893553 scopus 로고    scopus 로고
    • Signal-transducing adaptor molecules STAM1 and STAM2 are required for T-cell development and survival
    • DOI 10.1128/MCB.22.24.8648-8658.2002
    • Yamada, M., Ishii, N., Asao, H., Murata, K., Kanazawa, C., Sasaki, H., and Sugamura, K. (2002) Signal-transducing adaptor molecules STAM1 and STAM2 are required for T-cell development and survival. Mol. Cell Biol. 22, 8648-8658 (Pubitemid 35397179)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.24 , pp. 8648-8658
    • Yamada, M.1    Ishii, N.2    Asao, H.3    Murata, K.4    Kanazawa, C.5    Sasaki, H.6    Sugamura, K.7
  • 64
    • 33846137688 scopus 로고    scopus 로고
    • Hse1, a component of the yeast Hrs-STAM ubiquitin-sorting complex, associates with ubiquitin peptidases and a ligase to control sorting efficiency into multivesicular bodies
    • DOI 10.1091/mbc.E06-06-0557
    • Ren, J., Kee, Y., Huibregtse, J. M., and Piper, R. C. (2007) Hse1, a component of the yeast Hrs-STAM ubiquitin-sorting complex, associates with ubiquitin peptidases and a ligase to control sorting efficiency into multivesicular bodies. Mol. Biol. Cell 18, 324-335 (Pubitemid 46074967)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.1 , pp. 324-335
    • Ren, J.1    Kee, Y.2    Huibregtse, J.M.3    Piper, R.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.