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Volumn 288, Issue 21, 2013, Pages 15181-15193

Amot130 adapts atrophin-1 interacting protein 4 to inhibit yes-associated protein signaling and cell growth

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEINS; PROTEIN SIGNALING; TRANSCRIPTIONAL CO-ACTIVATORS; TUMOR SUPPRESSORS; UBIQUITIN LIGASES; UBIQUITINATION;

EID: 84878215401     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.446534     Document Type: Article
Times cited : (53)

References (52)
  • 3
    • 0037130937 scopus 로고    scopus 로고
    • Angiomotin belongs to a novel protein family with conserved coiled-coil and PDZ binding domains
    • DOI 10.1016/S0378-1119(02)00928-9, PII S0378111902009289
    • Bratt, A., Wilson, W. J., Troyanovsky, B., Aase, K., Kessler, R., Van Meir, E. G., Holmgren, L., and Meir, E. G. (2002) Angiomotin belongs to a novel protein family with conserved coiled-coil and PDZ binding domains. Gene 298, 69-77 (Pubitemid 35284264)
    • (2002) Gene , vol.298 , Issue.1 , pp. 69-77
    • Bratt, A.1    Wilson, W.J.2    Troyanovsky, B.3    Aase, K.4    Kessler, R.5    Meir, E.G.V.6    Holmgren, L.7
  • 4
    • 0037380116 scopus 로고    scopus 로고
    • Angiomotin regulates visceral endoderm movements during mouse embryogenesis
    • DOI 10.1016/S0960-9822(03)00204-5
    • Shimono, A., and Behringer, R. R. (2003) Angiomotin regulates visceral endoderm movements during mouse embryogenesis. Curr. Biol. 13, 613-617 (Pubitemid 36391942)
    • (2003) Current Biology , vol.13 , Issue.7 , pp. 613-617
    • Shimono, A.1    Behringer, R.R.2
  • 6
    • 79952769108 scopus 로고    scopus 로고
    • The adaptor protein AMOT promotes the proliferation of mammary epithelial cells via the prolonged activation of the extracellular signal-regulated kinases
    • Ranahan, W. P., Han, Z., Smith-Kinnaman, W., Nabinger, S. C., Heller, B., Herbert, B. S., Chan, R., and Wells, C. D. (2011) The adaptor protein AMOT promotes the proliferation of mammary epithelial cells via the prolonged activation of the extracellular signal-regulated kinases. Cancer Res. 71, 2203-2211
    • (2011) Cancer Res. , vol.71 , pp. 2203-2211
    • Ranahan, W.P.1    Han, Z.2    Smith-Kinnaman, W.3    Nabinger, S.C.4    Heller, B.5    Herbert, B.S.6    Chan, R.7    Wells, C.D.8
  • 8
    • 79953223677 scopus 로고    scopus 로고
    • Hippo pathway-independent restriction of TAZ and YAP by angiomotin
    • Chan, S. W., Lim, C. J., Chong, Y. F., Pobbati, A. V., Huang, C., and Hong, W. (2011) Hippo pathway-independent restriction of TAZ and YAP by angiomotin. J. Biol. Chem. 286, 7018-7026
    • (2011) J. Biol. Chem. , vol.286 , pp. 7018-7026
    • Chan, S.W.1    Lim, C.J.2    Chong, Y.F.3    Pobbati, A.V.4    Huang, C.5    Hong, W.6
  • 9
    • 78650895035 scopus 로고    scopus 로고
    • Angiomotin is a novel Hippo pathway component that inhibits YAP oncoprotein
    • Zhao, B., Li, L., Lu, Q., Wang, L. H., Liu, C. Y., Lei, Q., and Guan, K. L. (2011) Angiomotin is a novel Hippo pathway component that inhibits YAP oncoprotein. Genes Dev. 25, 51-63
    • (2011) Genes Dev. , vol.25 , pp. 51-63
    • Zhao, B.1    Li, L.2    Lu, Q.3    Wang, L.H.4    Liu, C.Y.5    Lei, Q.6    Guan, K.L.7
  • 10
    • 77951837150 scopus 로고    scopus 로고
    • The Hippo-YAP pathway in organ size control and tumorigenesis: An updated version
    • Zhao, B., Li, L., Lei, Q., and Guan, K. L. (2010) The Hippo-YAP pathway in organ size control and tumorigenesis: an updated version. Genes Dev. 24, 862-874
    • (2010) Genes Dev. , vol.24 , pp. 862-874
    • Zhao, B.1    Li, L.2    Lei, Q.3    Guan, K.L.4
  • 12
    • 55549098921 scopus 로고    scopus 로고
    • Mst2 and Lats kinases regulate apoptotic function of Yes kinase-associated protein (YAP)
    • Oka, T., Mazack, V., and Sudol, M. (2008) Mst2 and Lats kinases regulate apoptotic function of Yes kinase-associated protein (YAP). J. Biol. Chem. 283, 27534-27546
    • (2008) J. Biol. Chem. , vol.283 , pp. 27534-27546
    • Oka, T.1    Mazack, V.2    Sudol, M.3
  • 13
    • 0035873391 scopus 로고    scopus 로고
    • TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm
    • DOI 10.1101/gad.888601
    • Vassilev, A., Kaneko, K. J., Shu, H., Zhao, Y., and DePamphilis, M. L. (2001) TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm. Genes Dev. 15, 1229-1241 (Pubitemid 32472752)
    • (2001) Genes and Development , vol.15 , Issue.10 , pp. 1229-1241
    • Vassilev, A.1    Kaneko, K.J.2    Shu, H.3    Zhao, Y.4    DePamphilis, M.L.5
  • 16
    • 79953310106 scopus 로고    scopus 로고
    • Taxol resistance in breast cancer cells is mediated by the hippo pathway component TAZ and its downstream transcriptional targets Cyr61 and CTGF
    • Lai, D., Ho, K. C., Hao, Y., and Yang, X. (2011) Taxol resistance in breast cancer cells is mediated by the hippo pathway component TAZ and its downstream transcriptional targets Cyr61 and CTGF. Cancer Res. 71, 2728-2738
    • (2011) Cancer Res. , vol.71 , pp. 2728-2738
    • Lai, D.1    Ho, K.C.2    Hao, Y.3    Yang, X.4
  • 18
    • 41949138130 scopus 로고    scopus 로고
    • Tumor suppressor LATS1 is a negative regulator of oncogene YAP
    • Hao, Y., Chun, A., Cheung, K., Rashidi, B., and Yang, X. (2008) Tumor suppressor LATS1 is a negative regulator of oncogene YAP. J. Biol. Chem. 283, 5496-5509
    • (2008) J. Biol. Chem. , vol.283 , pp. 5496-5509
    • Hao, Y.1    Chun, A.2    Cheung, K.3    Rashidi, B.4    Yang, X.5
  • 19
    • 79953010044 scopus 로고    scopus 로고
    • Angiomotin-like proteins associate with and negatively regulate YAP1
    • Wang, W., Huang, J., and Chen, J. (2011) Angiomotin-like proteins associate with and negatively regulate YAP1. J. Biol. Chem. 286, 4364-4370
    • (2011) J. Biol. Chem. , vol.286 , pp. 4364-4370
    • Wang, W.1    Huang, J.2    Chen, J.3
  • 20
    • 84860870373 scopus 로고    scopus 로고
    • The Nedd4-like ubiquitin E3 ligases target angiomotin/p130 to ubiquitin-dependent degradation
    • Wang, C., An, J., Zhang, P., Xu, C., Gao, K., Wu, D., Wang, D., Yu, H., Liu, J. O., and Yu, L. (2012) The Nedd4-like ubiquitin E3 ligases target angiomotin/p130 to ubiquitin-dependent degradation. Biochem. J. 444, 279-289
    • (2012) Biochem. J. , vol.444 , pp. 279-289
    • Wang, C.1    An, J.2    Zhang, P.3    Xu, C.4    Gao, K.5    Wu, D.6    Wang, D.7    Yu, H.8    Liu, J.O.9    Yu, L.10
  • 21
    • 33645468737 scopus 로고    scopus 로고
    • Modification of the Creator recombination system for proteomics applications - Improved expression by addition of splice sites
    • Colwill, K., Wells, C.D., Elder, K., Goudreault, M., Hersi, K., Kulkarni, S., Hardy, W. R., Pawson, T., and Morin, G. B. (2006) Modification of the Creator recombination system for proteomics applications - improved expression by addition of splice sites. BMC Biotechnol. 6, 13
    • (2006) BMC Biotechnol. , vol.6 , pp. 13
    • Colwill, K.1    Wells, C.D.2    Elder, K.3    Goudreault, M.4    Hersi, K.5    Kulkarni, S.6    Hardy, W.R.7    Pawson, T.8    Morin, G.B.9
  • 25
    • 79952266588 scopus 로고    scopus 로고
    • Negative regulation of the Hippo pathway by E3 ubiquitin ligase ITCH is sufficient to promote tumorigenicity
    • Salah, Z., Melino, G., and Aqeilan, R. I. (2011) Negative regulation of the Hippo pathway by E3 ubiquitin ligase ITCH is sufficient to promote tumorigenicity. Cancer Res. 71, 2010-2020
    • (2011) Cancer Res. , vol.71 , pp. 2010-2020
    • Salah, Z.1    Melino, G.2    Aqeilan, R.I.3
  • 27
    • 84855271946 scopus 로고    scopus 로고
    • Version 1.44o. U. S. National Institutes of Health, Bethesda, MD
    • Rasband, W. S. (2011) ImageJ Version 1.44o. U. S. National Institutes of Health, Bethesda, MD
    • (2011) ImageJ
    • Rasband, W.S.1
  • 28
    • 33645703441 scopus 로고    scopus 로고
    • A tandem affinity tag for two-step purification under fully denaturing conditions: Application in ubiquitin profiling and protein complex identification combined with in vivo cross-linking
    • Tagwerker, C., Flick, K., Cui, M., Guerrero, C., Dou, Y., Auer, B., Baldi, P., Huang, L., and Kaiser, P. (2006) A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivo cross-linking. Mol. Cell. Proteomics 5, 737-748
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 737-748
    • Tagwerker, C.1    Flick, K.2    Cui, M.3    Guerrero, C.4    Dou, Y.5    Auer, B.6    Baldi, P.7    Huang, L.8    Kaiser, P.9
  • 29
    • 79851497821 scopus 로고    scopus 로고
    • Novel pyrrolopyrimidine-based α-helix mimetics: Cell-permeable inhibitors of protein-protein interactions
    • Lee, J. H., Zhang, Q., Jo, S., Chai, S. C., Oh, M., Im, W., Lu, H., and Lim, H. S. (2011) Novel pyrrolopyrimidine-based α-helix mimetics: cell-permeable inhibitors of protein-protein interactions. J. Am. Chem. Soc. 133, 676-679
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 676-679
    • Lee, J.H.1    Zhang, Q.2    Jo, S.3    Chai, S.C.4    Oh, M.5    Im, W.6    Lu, H.7    Lim, H.S.8
  • 30
    • 84860484234 scopus 로고    scopus 로고
    • YAP1 recruits c-Abl to protect angiomotin-like 1 from Nedd4-mediated degradation
    • Skouloudaki, K., and Walz, G. (2012) YAP1 recruits c-Abl to protect angiomotin-like 1 from Nedd4-mediated degradation. PLoS One 7, e35735
    • (2012) PLoS One , vol.7
    • Skouloudaki, K.1    Walz, G.2
  • 31
    • 67349128620 scopus 로고    scopus 로고
    • Control of the activity of WW-HECT domain E3 ubiquitin ligases by NDFIP proteins
    • Mund, T., and Pelham, H. R. (2009) Control of the activity of WW-HECT domain E3 ubiquitin ligases by NDFIP proteins. EMBO Rep. 10, 501-507
    • (2009) EMBO Rep. , vol.10 , pp. 501-507
    • Mund, T.1    Pelham, H.R.2
  • 32
    • 77952616841 scopus 로고    scopus 로고
    • Spartin activates atrophin-1-interacting protein 4 (AIP4) E3 ubiquitin ligase and promotes ubiquitination of adipophilin on lipid droplets
    • Hooper, C., Puttamadappa, S. S., Loring, Z., Shekhtman, A., and Bakowska, J. C. (2010) Spartin activates atrophin-1-interacting protein 4 (AIP4) E3 ubiquitin ligase and promotes ubiquitination of adipophilin on lipid droplets. BMC Biol. 8, 72
    • (2010) BMC Biol. , vol.8 , pp. 72
    • Hooper, C.1    Puttamadappa, S.S.2    Loring, Z.3    Shekhtman, A.4    Bakowska, J.C.5
  • 34
    • 67349132223 scopus 로고    scopus 로고
    • Physiological functions of the HECT family of ubiquitin ligases
    • Rotin, D., and Kumar, S. (2009) Physiological functions of the HECT family of ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 10, 398-409
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 398-409
    • Rotin, D.1    Kumar, S.2
  • 35
    • 36248989248 scopus 로고    scopus 로고
    • The Nedd4-like family of E3 ubiquitin ligases and cancer
    • DOI 10.1007/s10555-007-9091-x, Forty Years of Metastasis Research: A Tribute to Dr. Isaiah J. Fidler
    • Chen, C., and Matesic, L. (2007) The Nedd4-like family of E3 ubiquitin ligases and cancer. Cancer Metastasis Rev. 26, 587-604 (Pubitemid 350119775)
    • (2007) Cancer and Metastasis Reviews , vol.26 , Issue.3-4 , pp. 587-604
    • Chen, C.1    Matesic, L.E.2
  • 36
    • 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
  • 37
    • 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
    • 76349086181 scopus 로고    scopus 로고
    • The ubiquitin ligase Itch mediates the antiapoptotic activity of epidermal growth factor by promoting the ubiquitylation and degradation of the truncated C-terminal portion of Bid
    • Azakir, B. A., Desrochers, G., and Angers, A. (2010) The ubiquitin ligase Itch mediates the antiapoptotic activity of epidermal growth factor by promoting the ubiquitylation and degradation of the truncated C-terminal portion of Bid. FEBS J. 277, 1319-1330
    • (2010) FEBS J. , vol.277 , pp. 1319-1330
    • Azakir, B.A.1    Desrochers, G.2    Angers, A.3
  • 42
    • 79955028943 scopus 로고    scopus 로고
    • The E3 ligase Itch is a negative regulator of the homeostasis and function of hematopoietic stem cells
    • Rathinam, C., Matesic, L. E., and Flavell, R. A. (2011) The E3 ligase Itch is a negative regulator of the homeostasis and function of hematopoietic stem cells. Nat. Immunol. 12, 399-407
    • (2011) Nat. Immunol. , vol.12 , pp. 399-407
    • Rathinam, C.1    Matesic, L.E.2    Flavell, R.A.3
  • 43
    • 0036471394 scopus 로고    scopus 로고
    • A single WW domain is the predominant mediator of the interaction between the human ubiquitin-protein ligase Nedd4 and the human epithelial sodium channel
    • DOI 10.1042/0264-6021:3610481
    • Lott, J. S., Coddington-Lawson, S. J., Teesdale-Spittle, P. H., and McDonald, F. J. (2002) A singleWWdomain is the predominant mediator of the interaction between the human ubiquitin-protein ligase Nedd4 and the human epithelial sodium channel. Biochem. J. 361, 481-488 (Pubitemid 34177817)
    • (2002) Biochemical Journal , vol.361 , Issue.3 , pp. 481-488
    • Lott, J.S.1    Coddington-Lawson, S.J.2    Teesdale-Spittle, P.H.3    McDonald, F.J.4
  • 44
    • 78649875435 scopus 로고    scopus 로고
    • Coupling of tandem Smad ubiquitination regulatory factor (Smurf) WW domains modulates target specificity
    • Chong, P. A., Lin, H., Wrana, J. L., and Forman-Kay, J. D. (2010) Coupling of tandem Smad ubiquitination regulatory factor (Smurf) WW domains modulates target specificity. Proc. Natl. Acad. Sci. U.S.A. 107, 18404-18409
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 18404-18409
    • Chong, P.A.1    Lin, H.2    Wrana, J.L.3    Forman-Kay, J.D.4
  • 45
    • 79955101793 scopus 로고    scopus 로고
    • Structural features and ligand binding properties of tandemWWdomains from YAP and TAZ, nuclear effectors of the Hippo pathway
    • Webb, C., Upadhyay, A., Giuntini, F., Eggleston, I., Furutani-Seiki, M., Ishima, R., and Bagby, S. (2011) Structural features and ligand binding properties of tandemWWdomains from YAP and TAZ, nuclear effectors of the Hippo pathway. Biochemistry 50, 3300-3309
    • (2011) Biochemistry , vol.50 , pp. 3300-3309
    • Webb, C.1    Upadhyay, A.2    Giuntini, F.3    Eggleston, I.4    Furutani-Seiki, M.5    Ishima, R.6    Bagby, S.7
  • 46
    • 68549115210 scopus 로고    scopus 로고
    • Human angiomotin-like 1 associates with an angiomotin protein complex through its coiled-coil domain and induces the remodeling of the actin cytoskeleton
    • Gagné, V., Moreau, J., Plourde, M., Lapointe, M., Lord, M., Gagnon, E., and Fernandes, M. J. (2009) Human angiomotin-like 1 associates with an angiomotin protein complex through its coiled-coil domain and induces the remodeling of the actin cytoskeleton. Cell Motil. Cytoskeleton 66, 754-768
    • (2009) Cell Motil. Cytoskeleton , vol.66 , pp. 754-768
    • Gagné, V.1    Moreau, J.2    Plourde, M.3    Lapointe, M.4    Lord, M.5    Gagnon, E.6    Fernandes, M.J.7
  • 47
    • 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
  • 49
    • 73549095761 scopus 로고    scopus 로고
    • A coordinated phosphorylation by Lats and CK1 regulates YAP stability through SCF(β)-TRCP
    • Zhao, B., Li, L., Tumaneng, K., Wang, C. Y., and Guan, K. L. (2010) A coordinated phosphorylation by Lats and CK1 regulates YAP stability through SCF(β)-TRCP. Genes Dev. 24, 72-85
    • (2010) Genes Dev. , vol.24 , pp. 72-85
    • Zhao, B.1    Li, L.2    Tumaneng, K.3    Wang, C.Y.4    Guan, K.L.5
  • 50
    • 1942453854 scopus 로고    scopus 로고
    • Degradation of Bcl10 Induced by T-Cell Activation Negatively Regulates NF-κB Signaling
    • DOI 10.1128/MCB.24.9.3860-3873.2004
    • Scharschmidt, E., Wegener, E., Heissmeyer, V., Rao, A., and Krappmann, D. (2004) Degradation of Bcl10 induced by T-cell activation negatively regulates NF-κB signaling. Mol. Cell. Biol. 24, 3860-3873 (Pubitemid 38496164)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.9 , pp. 3860-3873
    • Scharschmidt, E.1    Wegener, E.2    Heissmeyer, V.3    Rao, A.4    Krappmann, D.5
  • 52
    • 80053363788 scopus 로고    scopus 로고
    • Angiomotin family proteins are novel activators of the LATS2 kinase tumor suppressor
    • Paramasivam, M., Sarkeshik, A., Yates, J. R., 3rd, Fernandes, M. J., and McCollum, D. (2011) Angiomotin family proteins are novel activators of the LATS2 kinase tumor suppressor. Mol. Biol. Cell 22, 3725-3733
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3725-3733
    • Paramasivam, M.1    Sarkeshik, A.2    Yates III, J.R.3    Fernandes, M.J.4    McCollum, D.5


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