메뉴 건너뛰기




Volumn 289, Issue 4, 2014, Pages 2043-2054

Protein interaction screening for the ankyrin repeats and suppressor of cytokine signaling (SOCS) box (ASB) family identify asb11 as a novel endoplasmic reticulum resident ubiquitin ligase

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN REPEATS; BIOLOGICAL FUNCTIONS; DATA RESOURCES; ENDOPLASMIC RETICULUM; INTERACTORS; PROTEIN INTERACTION; SUPPRESSOR OF CYTOKINE SIGNALING; UBIQUITIN LIGASES;

EID: 84893077593     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.534602     Document Type: Article
Times cited : (38)

References (44)
  • 1
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl, M., Hoppe, T., Schlenker, S., Ulrich, H. D., Mayer, T. U., and Jentsch, S. (1999) A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96, 635-644
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 2
    • 10644276385 scopus 로고    scopus 로고
    • VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases
    • Kamura, T., Maenaka, K., Kotoshiba, S., Matsumoto, M., Kohda, D., Conaway, R. C., Conaway, J. W., and Nakayama, K. I. (2004) VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases. Genes Dev. 18, 3055-3065
    • (2004) Genes Dev. , vol.18 , pp. 3055-3065
    • Kamura, T.1    Maenaka, K.2    Kotoshiba, S.3    Matsumoto, M.4    Kohda, D.5    Conaway, R.C.6    Conaway, J.W.7    Nakayama, K.I.8
  • 7
    • 0036233985 scopus 로고    scopus 로고
    • Regulation of Jak2 through the ubiquitin-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1
    • Ungureanu, D., Saharinen, P., Junttila, I., Hilton, D. J., and Silvennoinen, O. (2002) Regulation of Jak2 through the ubiquitin-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1. Mol. Cell. Biol. 22, 3316-3326
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3316-3326
    • Ungureanu, D.1    Saharinen, P.2    Junttila, I.3    Hilton, D.J.4    Silvennoinen, O.5
  • 8
    • 14044267523 scopus 로고    scopus 로고
    • ASB2 is an Elongin BCinteracting protein that can assemble with Cullin 5 and Rbx1 to reconstitute an E3 ubiquitin ligase complex
    • Heuzé, M. L., Guibal, F. C., Banks, C. A., Conaway, J. W., Conaway, R. C., Cayre, Y. E., Benecke, A., and Lutz, P. G. (2005) ASB2 is an Elongin BCinteracting protein that can assemble with Cullin 5 and Rbx1 to reconstitute an E3 ubiquitin ligase complex. J. Biol. Chem. 280, 5468-5474
    • (2005) J. Biol. Chem. , vol.280 , pp. 5468-5474
    • Heuzé, M.L.1    Guibal, F.C.2    Banks, C.A.3    Conaway, J.W.4    Conaway, R.C.5    Cayre, Y.E.6    Benecke, A.7    Lutz, P.G.8
  • 9
    • 28844473943 scopus 로고    scopus 로고
    • ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes
    • Kohroki, J., Nishiyama, T., Nakamura, T., and Masuho, Y. (2005) ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes. FEBS Lett. 579, 6796-6802
    • (2005) FEBS Lett. , vol.579 , pp. 6796-6802
    • Kohroki, J.1    Nishiyama, T.2    Nakamura, T.3    Masuho, Y.4
  • 11
    • 18944380864 scopus 로고    scopus 로고
    • Ankyrin repeat and SOCS box 3 (ASB3) mediates ubiquitination and degradation of tumor necrosis factor receptor II
    • Chung, A. S., Guan, Y. J., Yuan, Z. L., Albina, J. E., and Chin, Y. E. (2005) Ankyrin repeat and SOCS box 3 (ASB3) mediates ubiquitination and degradation of tumor necrosis factor receptor II. Mol. Cell. Biol. 25, 4716-4726
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 4716-4726
    • Chung, A.S.1    Guan, Y.J.2    Yuan, Z.L.3    Albina, J.E.4    Chin, Y.E.5
  • 13
    • 77951936368 scopus 로고    scopus 로고
    • ASB9 interacts with ubiquitous mitochondrial creatine kinase and inhibits mitochondrial function
    • Kwon, S., Kim, D., Rhee, J. W., Park, J. A., Kim, D. W., Kim, D. S., Lee, Y., and Kwon, H. J. (2010) ASB9 interacts with ubiquitous mitochondrial creatine kinase and inhibits mitochondrial function. BMC Biol. 8, 23
    • (2010) BMC Biol. , vol.8 , pp. 23
    • Kwon, S.1    Kim, D.2    Rhee, J.W.3    Park, J.A.4    Kim, D.W.5    Kim, D.S.6    Lee, Y.7    Kwon, H.J.8
  • 16
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa, M. E., Bennett, E. J., Gygi, S. P., and Harper, J. W. (2009) Defining the human deubiquitinating enzyme interaction landscape. Cell 138, 389-403
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 17
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko, A., Tomas, H., Havlis, J., Olsen, J. V., and Mann, M. (2006) In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1, 2856-2860
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 18
    • 44449108277 scopus 로고    scopus 로고
    • Iodoacetamide-induced artifact mimics ubiquitination in mass spectrometry
    • Nielsen, M. L., Vermeulen, M., Bonaldi, T., Cox, J., Moroder, L., and Mann, M. (2008) Iodoacetamide-induced artifact mimics ubiquitination in mass spectrometry. Nat. Methods 5, 459-460
    • (2008) Nat. Methods , vol.5 , pp. 459-460
    • Nielsen, M.L.1    Vermeulen, M.2    Bonaldi, T.3    Cox, J.4    Moroder, L.5    Mann, M.6
  • 20
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J., and Mann, M. (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367-1372
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 22
    • 40549097761 scopus 로고    scopus 로고
    • A functional link between the human cell cycle-regulatory phosphatase Cdc14A and the atypical mitogen-activated kinase ERK3
    • Hansen, C. A., Bartek, J., and Jensen, S. (2008) A functional link between the human cell cycle-regulatory phosphatase Cdc14A and the atypical mitogen-activated kinase ERK3. Cell Cycle 7, 325-334
    • (2008) Cell Cycle , vol.7 , pp. 325-334
    • Hansen, C.A.1    Bartek, J.2    Jensen, S.3
  • 23
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • Ong, S. E., and Mann, M. (2006) A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nat. Protoc. 1, 2650-2660
    • (2006) Nat. Protoc. , vol.1 , pp. 2650-2660
    • Ong, S.E.1    Mann, M.2
  • 24
    • 0036929129 scopus 로고    scopus 로고
    • NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases
    • Liu, J., Furukawa, M., Matsumoto, T., and Xiong, Y. (2002) NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases. Mol. Cell 10, 1511-1518
    • (2002) Mol. Cell , vol.10 , pp. 1511-1518
    • Liu, J.1    Furukawa, M.2    Matsumoto, T.3    Xiong, Y.4
  • 26
    • 70349339322 scopus 로고    scopus 로고
    • Regulation of Cullin-RING E3 ubiquitin-ligases by neddylation and dimerization
    • Merlet, J., Burger, J., Gomes, J. E., and Pintard, L. (2009) Regulation of Cullin-RING E3 ubiquitin-ligases by neddylation and dimerization. Cell Mol. Life Sci. 66, 1924-1938
    • (2009) Cell Mol. Life Sci. , vol.66 , pp. 1924-1938
    • Merlet, J.1    Burger, J.2    Gomes, J.E.3    Pintard, L.4
  • 28
    • 50449108516 scopus 로고    scopus 로고
    • Structural insights into NEDD8 activation of Cullin-RING ligases: Conformational control of conjugation
    • Duda, D. M., Borg, L. A., Scott, D. C., Hunt, H. W., Hammel, M., and Schulman, B. A. (2008) Structural insights into NEDD8 activation of Cullin-RING ligases: conformational control of conjugation. Cell 134, 995-1006
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1    Borg, L.A.2    Scott, D.C.3    Hunt, H.W.4    Hammel, M.5    Schulman, B.A.6
  • 31
    • 33947107495 scopus 로고    scopus 로고
    • The Cullin3 ubiquitin ligase functions as a Nedd8-bound heterodimer
    • Wimuttisuk, W., and Singer, J. D. (2007) The Cullin3 ubiquitin ligase functions as a Nedd8-bound heterodimer. Mol. Biol. Cell 18, 899-909
    • (2007) Mol. Biol. Cell , vol.18 , pp. 899-909
    • Wimuttisuk, W.1    Singer, J.D.2
  • 32
    • 78649653568 scopus 로고    scopus 로고
    • Structural assembly of Cullin-RING ubiquitin ligase complexes
    • Zimmerman, E. S., Schulman, B. A., and Zheng, N. (2010) Structural assembly of Cullin-RING ubiquitin ligase complexes. Curr. Opin. Struct. Biol. 20, 714-721
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 714-721
    • Zimmerman, E.S.1    Schulman, B.A.2    Zheng, N.3
  • 33
    • 79955580832 scopus 로고    scopus 로고
    • Notch-induced Asb2 expression promotes protein ubiquitination by forming non-canonical E3 ligase complexes
    • Nie, L., Zhao, Y., Wu, W., Yang, Y. Z., Wang, H. C., and Sun, X. H. (2011) Notch-induced Asb2 expression promotes protein ubiquitination by forming non-canonical E3 ligase complexes. Cell Res. 21, 754-769
    • (2011) Cell Res. , vol.21 , pp. 754-769
    • Nie, L.1    Zhao, Y.2    Wu, W.3    Yang, Y.Z.4    Wang, H.C.5    Sun, X.H.6
  • 34
    • 82355171881 scopus 로고    scopus 로고
    • A mechanism underlying NOTCH-induced and ubiquitin-mediated JAK3 degradation
    • Wu, W., and Sun, X. H. (2011) A mechanism underlying NOTCH-induced and ubiquitin-mediated JAK3 degradation. J. Biol. Chem. 286, 41153-41162
    • (2011) J. Biol. Chem. , vol.286 , pp. 41153-41162
    • Wu, W.1    Sun, X.H.2
  • 35
    • 34248209547 scopus 로고    scopus 로고
    • Stealing the spotlight: CUL4-DDB1 ubiquitin ligase docks WD40-repeat proteins to destroy
    • Higa, L. A., and Zhang, H. (2007) Stealing the spotlight: CUL4-DDB1 ubiquitin ligase docks WD40-repeat proteins to destroy. Cell Div. 2, 5
    • (2007) Cell Div. , vol.2 , pp. 5
    • Higa, L.A.1    Zhang, H.2
  • 36
    • 0036288185 scopus 로고    scopus 로고
    • CUL-4A is critical for early embryonic development
    • Li, B., Ruiz, J. C., and Chun, K. T. (2002) CUL-4A is critical for early embryonic development. Mol. Cell. Biol. 22, 4997-5005
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4997-5005
    • Li, B.1    Ruiz, J.C.2    Chun, K.T.3
  • 37
    • 0033544942 scopus 로고    scopus 로고
    • Cullin 4A associates with the UV-damaged DNA-binding protein DDB
    • Shiyanov, P., Nag, A., and Raychaudhuri, P. (1999) Cullin 4A associates with the UV-damaged DNA-binding protein DDB. J. Biol. Chem. 274, 35309-35312
    • (1999) J. Biol. Chem. , vol.274 , pp. 35309-35312
    • Shiyanov, P.1    Nag, A.2    Raychaudhuri, P.3
  • 38
    • 78649974984 scopus 로고    scopus 로고
    • Dynamics of Cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics
    • Bennett, E. J., Rush, J., Gygi, S. P., and Harper, J. W. (2010) Dynamics of Cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics. Cell 143, 951-965
    • (2010) Cell , vol.143 , pp. 951-965
    • Bennett, E.J.1    Rush, J.2    Gygi, S.P.3    Harper, J.W.4
  • 39
    • 0026502044 scopus 로고
    • Carboxy terminally truncated forms of ribophorin i are degraded in pre-Golgi compartments by a calcium-dependent process
    • Tsao, Y. S., Ivessa, N. E., Adesnik, M., Sabatini, D. D., and Kreibich, G. (1992) Carboxy terminally truncated forms of ribophorin I are degraded in pre-Golgi compartments by a calcium-dependent process. J. Cell Biol. 116, 57-67
    • (1992) J. Cell Biol. , vol.116 , pp. 57-67
    • Tsao, Y.S.1    Ivessa, N.E.2    Adesnik, M.3    Sabatini, D.D.4    Kreibich, G.5
  • 40
    • 0032540384 scopus 로고    scopus 로고
    • Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome
    • de Virgilio, M., Weninger, H., and Ivessa, N. E. (1998) Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome. J. Biol. Chem. 273, 9734-9743
    • (1998) J. Biol. Chem. , vol.273 , pp. 9734-9743
    • De Virgilio, M.1    Weninger, H.2    Ivessa, N.E.3
  • 41
    • 30344482590 scopus 로고    scopus 로고
    • Lingering mysteries of ubiquitin-chain assembly
    • Hochstrasser, M. (2006) Lingering mysteries of ubiquitin-chain assembly. Cell 124, 27-34
    • (2006) Cell , vol.124 , pp. 27-34
    • Hochstrasser, M.1
  • 42
    • 33749506057 scopus 로고    scopus 로고
    • Mms2-Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation
    • Eddins, M. J., Carlile, C. M., Gomez, K. M., Pickart, C. M., and Wolberger, C. (2006) Mms2-Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation. Nat. Struct. Mol. Biol. 13, 915-920
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 915-920
    • Eddins, M.J.1    Carlile, C.M.2    Gomez, K.M.3    Pickart, C.M.4    Wolberger, C.5
  • 43
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege, C., Pfander, B., Moldovan, G. L., Pyrowolakis, G., and Jentsch, S. (2002) RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419, 135-141
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 44
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of Cullin-RING ubiquitin ligases
    • Petroski, M. D., and Deshaies, R. J. (2005) Function and regulation of Cullin-RING ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 6, 9-20
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.