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Volumn 108, Issue 51, 2011, Pages 20603-20608

Cullin 3 mediates SRC-3 ubiquitination and degradation to control the retinoic acid response

Author keywords

[No Author keywords available]

Indexed keywords

CULLIN; CULLIN 3; PROTEIN; RBX1 PROTEIN; RETINOIC ACID; RETINOIC ACID RECEPTOR; SERINE; SRC 3 PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84855510640     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1102572108     Document Type: Article
Times cited : (30)

References (28)
  • 1
    • 68049143179 scopus 로고    scopus 로고
    • Dynamic and combinatorial control of gene expression by nuclear retinoic acid receptors
    • Rochette-Egly C, Germain P (2009) Dynamic and combinatorial control of gene expression by nuclear retinoic acid receptors. Nucl Recept Signal 7:e005.
    • (2009) Nucl Recept Signal , vol.7
    • Rochette-Egly, C.1    Germain, P.2
  • 2
    • 58149142965 scopus 로고    scopus 로고
    • Multi-modulation of nuclear receptor coactivators through posttranslational modifications
    • Han SJ, Lonard DM, O'Malley BW (2009) Multi-modulation of nuclear receptor coactivators through posttranslational modifications. Trends Endocrinol Metab 20:8-15.
    • (2009) Trends Endocrinol Metab , vol.20 , pp. 8-15
    • Han, S.J.1    Lonard, D.M.2    O'Malley, B.W.3
  • 4
    • 34250001084 scopus 로고    scopus 로고
    • SRC-3 Coactivator Functional Lifetime Is Regulated by a Phospho-Dependent Ubiquitin Time Clock
    • DOI 10.1016/j.cell.2007.04.039, PII S0092867407005855
    • Wu RC, Feng Q, Lonard DM, O'Malley BW (2007) SRC-3 coactivator functional lifetime is regulated by a phospho-dependent ubiquitin time clock. Cell 129:1125-1140. (Pubitemid 46891039)
    • (2007) Cell , vol.129 , Issue.6 , pp. 1125-1140
    • Wu, R.-C.1    Feng, Q.2    Lonard, D.M.3    O'Malley, B.W.4
  • 5
    • 4644252581 scopus 로고    scopus 로고
    • Selective phosphorylations of the SRC-3/AIB1 coactivator integrate genomic reponses to multiple cellular signaling pathways
    • Wu RC, et al. (2004) Selective phosphorylations of the SRC-3/AIB1 coactivator integrate genomic reponses to multiple cellular signaling pathways. Mol Cell 15:937-949.
    • (2004) Mol Cell , vol.15 , pp. 937-949
    • Wu, R.C.1
  • 7
    • 65549158253 scopus 로고    scopus 로고
    • SUG-1 plays proteolytic and non-proteolytic roles in the control of retinoic acid target genes via its interaction with SRC-3
    • Ferry C, et al. (2009) SUG-1 plays proteolytic and non-proteolytic roles in the control of retinoic acid target genes via its interaction with SRC-3. J Biol Chem 284:8127-8135.
    • (2009) J Biol Chem , vol.284 , pp. 8127-8135
    • Ferry, C.1
  • 9
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • DOI 10.1038/nrm1547
    • Petroski MD, Deshaies RJ (2005) Function and regulation of cullin-RING ubiquitin ligases. Nat Rev Mol Cell Biol 6:9-20. (Pubitemid 40064895)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.1 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 10
    • 65849096454 scopus 로고    scopus 로고
    • Proteasome-mediated turnover of the transcription coactivator NPR1 plays dual roles in regulating plant immunity
    • Spoel SH, et al. (2009) Proteasome-mediated turnover of the transcription coactivator NPR1 plays dual roles in regulating plant immunity. Cell 137:860-872.
    • (2009) Cell , vol.137 , pp. 860-872
    • Spoel, S.H.1
  • 11
    • 75849129292 scopus 로고    scopus 로고
    • Multiple Ser/Thr-rich degrons mediate the degradation of Ci/Gli by the Cul3-HIB/SPOP E3 ubiquitin ligase
    • Zhang Q, et al. (2009) Multiple Ser/Thr-rich degrons mediate the degradation of Ci/Gli by the Cul3-HIB/SPOP E3 ubiquitin ligase. Proc Natl Acad Sci USA 106:21191-21196.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 21191-21196
    • Zhang, Q.1
  • 12
    • 77951257955 scopus 로고    scopus 로고
    • PEST sequences mediate heat shock factor 2 turnover by interacting with the Cul3 subunit of the Cul3-RING ubiquitin ligase
    • Xing H, Hong Y, Sarge KD (2010) PEST sequences mediate heat shock factor 2 turnover by interacting with the Cul3 subunit of the Cul3-RING ubiquitin ligase. Cell Stress Chaperones 15:301-308.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 301-308
    • Xing, H.1    Hong, Y.2    Sarge, K.D.3
  • 13
    • 58149354155 scopus 로고    scopus 로고
    • A coordinated phosphorylation cascade initiated by p38MAPK/MSK1 directs RARalpha to target promoters
    • Bruck N, et al. (2009) A coordinated phosphorylation cascade initiated by p38MAPK/MSK1 directs RARalpha to target promoters. EMBO J 28:34-47.
    • (2009) EMBO J , vol.28 , pp. 34-47
    • Bruck, N.1
  • 14
    • 84863804595 scopus 로고    scopus 로고
    • A retinoic acid receptor RARα pool present in membrane lipid rafts forms complexes with G protein αQ to activate p38MAPK
    • in press
    • Piskunov A, Rochette-Egly C (2011) A retinoic acid receptor RARα pool present in membrane lipid rafts forms complexes with G protein αQ to activate p38MAPK. Oncogene, in press.
    • (2011) Oncogene
    • Piskunov, A.1    Rochette-Egly, C.2
  • 16
    • 79952260898 scopus 로고    scopus 로고
    • Nucleolar targeting of the fbw7 ubiquitin ligase by a pseudosubstrate and glycogen synthase kinase 3
    • Welcker M, Larimore EA, Frappier L, Clurman BE (2011) Nucleolar targeting of the fbw7 ubiquitin ligase by a pseudosubstrate and glycogen synthase kinase 3. Mol Cell Biol 31:1214-1224.
    • (2011) Mol Cell Biol , vol.31 , pp. 1214-1224
    • Welcker, M.1    Larimore, E.A.2    Frappier, L.3    Clurman, B.E.4
  • 17
    • 0037043821 scopus 로고    scopus 로고
    • Her2/neu induces all-trans retinoic acid (ATRA) resistance in breast cancer cells
    • DOI 10.1038/sj.onc.1205660
    • Tari AM, Lim SJ, Hung MC, Esteva FJ, Lopez-Berestein G (2002) Her2/neu induces all-trans retinoic acid (ATRA) resistance in breast cancer cells. Oncogene 21:5224-5232. (Pubitemid 34948134)
    • (2002) Oncogene , vol.21 , Issue.34 , pp. 5224-5232
    • Tari, A.M.1    Lim, S.-J.2    Hung, M.-C.3    Esteva, F.J.4    Lopez-Berestein, G.5
  • 18
    • 69249110003 scopus 로고    scopus 로고
    • Normal and cancer-related functions of the p160 steroid receptor co-activator (SRC) family
    • Xu J, Wu RC, O'Malley BW (2009) Normal and cancer-related functions of the p160 steroid receptor co-activator (SRC) family. Nat Rev Cancer 9:615-630.
    • (2009) Nat Rev Cancer , vol.9 , pp. 615-630
    • Xu, J.1    Wu, R.C.2    O'Malley, B.W.3
  • 19
    • 1142277924 scopus 로고    scopus 로고
    • Protein degradation: CUL-3 and BTB - Partners in proteolysis
    • van den Heuvel S (2004) Protein degradation: CUL-3 and BTB - partners in proteolysis. Curr Biol 14:R59-R61.
    • (2004) Curr Biol , vol.14
    • Van Den Heuvel, S.1
  • 21
    • 34047249627 scopus 로고    scopus 로고
    • Structure of a Fbw7-Skp1-Cyclin E Complex: Multisite-Phosphorylated Substrate Recognition by SCF Ubiquitin Ligases
    • DOI 10.1016/j.molcel.2007.02.022, PII S1097276507001220
    • Hao B, Oehlmann S, Sowa ME, Harper JW, Pavletich NP (2007) Structure of a Fbw7-Skp1-cyclin E complex: Multisite-phosphorylated substrate recognition by SCF ubiquitin ligases. Mol Cell 26:131-143. (Pubitemid 46550934)
    • (2007) Molecular Cell , vol.26 , Issue.1 , pp. 131-143
    • Hao, B.1    Oehlmann, S.2    Sowa, M.E.3    Harper, J.W.4    Pavletich, N.P.5
  • 22
    • 79959425215 scopus 로고    scopus 로고
    • Evolution of nuclear retinoic acid receptor alpha (RARα) phosphorylation sites. Serine gain provides fine-tuned regulation
    • Samarut E, et al. (2011) Evolution of nuclear retinoic acid receptor alpha (RARα) phosphorylation sites. Serine gain provides fine-tuned regulation. Mol Biol Evol 28:2125-2137.
    • (2011) Mol Biol Evol , vol.28 , pp. 2125-2137
    • Samarut, E.1
  • 23
    • 80054908957 scopus 로고    scopus 로고
    • Tumor-suppressor role for the SPOP ubiquitin ligase in signal-dependent proteolysis of the oncogenic co-activator SRC-3/AIB1
    • Li C, et al. (2011) Tumor-suppressor role for the SPOP ubiquitin ligase in signal-dependent proteolysis of the oncogenic co-activator SRC-3/AIB1. Oncogene 30:4350-4364.
    • (2011) Oncogene , vol.30 , pp. 4350-4364
    • Li, C.1
  • 24
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • DOI 10.1038/35077225
    • Blume-Jensen P, Hunter T (2001) Oncogenic kinase signalling. Nature 411:355-365. (Pubitemid 32467045)
    • (2001) Nature , vol.411 , Issue.6835 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 25
    • 80054694510 scopus 로고    scopus 로고
    • Global identification of modular cullin-RING ligase substrates
    • Emanuele MJ, et al. (2011) Global identification of modular cullin-RING ligase substrates. Cell 147:459-474.
    • (2011) Cell , vol.147 , pp. 459-474
    • Emanuele, M.J.1
  • 26
    • 67549104319 scopus 로고    scopus 로고
    • Genomic antagonism between retinoic acid and estrogen signaling in breast cancer
    • Hua S, Kittler R, White KP (2009) Genomic antagonism between retinoic acid and estrogen signaling in breast cancer. Cell 137:1259-1271.
    • (2009) Cell , vol.137 , pp. 1259-1271
    • Hua, S.1    Kittler, R.2    White, K.P.3
  • 27
    • 75149194937 scopus 로고    scopus 로고
    • Cooperative interaction between retinoic acid receptor-alpha and estrogen receptor in breast cancer
    • Ross-Innes CS, et al. (2010) Cooperative interaction between retinoic acid receptor-alpha and estrogen receptor in breast cancer. Genes Dev 24:171-182.
    • (2010) Genes Dev , vol.24 , pp. 171-182
    • Ross-Innes, C.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.