메뉴 건너뛰기




Volumn 491, Issue 7425, 2012, Pages 618-621

BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs

Author keywords

[No Author keywords available]

Indexed keywords

CULLIN 3; HISTONE H2A; PROMYELOCYTIC LEUKEMIA ZINC FINGER; PROTEIN BCL 6; TRANSCRIPTION FACTOR; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84869866718     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature11548     Document Type: Article
Times cited : (85)

References (33)
  • 1
    • 51349121407 scopus 로고    scopus 로고
    • The transcription factor PLZF directs the effector program of the NKT cell lineage
    • Savage, A. K. et al. The transcription factor PLZF directs the effector program of the NKT cell lineage. Immunity 29, 391-403 (2008).
    • (2008) Immunity , vol.29 , pp. 391-403
    • Savage, A.K.1
  • 2
    • 50049084627 scopus 로고    scopus 로고
    • The BTB-zinc finger transcriptional regulatorPLZF controls the development of invariant natural killer T cell effector functions
    • Kovalovsky, D. et al. The BTB-zinc finger transcriptional regulatorPLZF controls the development of invariant natural killer T cell effector functions. Nature Immunol. 9, 1055-1064 (2008).
    • (2008) Nature Immunol. , vol.9 , pp. 1055-1064
    • Kovalovsky, D.1
  • 3
    • 0141493447 scopus 로고    scopus 로고
    • BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3
    • Xu, L. et al. BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3. Nature 425, 316-321 (2003).
    • (2003) Nature , vol.425 , pp. 316-321
    • Xu, L.1
  • 4
    • 0242575197 scopus 로고    scopus 로고
    • Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases
    • Furukawa, M., He, Y. J., Borchers, C. & Xiong, Y. Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases. Nature Cell Biol. 5, 1001-1007 (2003).
    • (2003) Nature Cell Biol. , vol.5 , pp. 1001-1007
    • Furukawa, M.1    He, Y.J.2    Borchers, C.3    Xiong, Y.4
  • 5
    • 0141750416 scopus 로고    scopus 로고
    • BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases
    • Geyer, R., Wee, S., Anderson, S., Yates, J. & Wolf, D. A. BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases. Mol. Cell 12, 783-790 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 783-790
    • Geyer, R.1    Wee, S.2    Anderson, S.3    Yates, J.4    Wolf, D.A.5
  • 6
    • 2442529664 scopus 로고    scopus 로고
    • Cullin-based ubiquitin ligases: Cul3-BTB complexes join the family
    • Pintard, L., Willems, A. & Peter, M. Cullin-based ubiquitin ligases: Cul3-BTB complexes join the family. EMBO J. 23, 1681-1687 (2004).
    • (2004) EMBO J. , vol.23 , pp. 1681-1687
    • Pintard, L.1    Willems, A.2    Peter, M.3
  • 7
    • 78649653568 scopus 로고    scopus 로고
    • Structural assemblyofcullin-RING ubiquitin ligase complexes
    • Zimmerman, E. S., Schulman, B. A. & Zheng, N. Structural assemblyofcullin-RING ubiquitin ligase complexes. Curr. Opin. Struct. Biol. 20, 714-721 (2010).
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 714-721
    • Zimmerman, E.S.1    Schulman, B.A.2    Zheng, N.3
  • 8
    • 77955949060 scopus 로고    scopus 로고
    • BCL6: Master regulator ofthe germinal center reaction and key oncogene in B cell lymphomagenesis
    • Basso, K. & Dalla-Favera, R. BCL6: master regulator ofthe germinal center reaction and key oncogene in B cell lymphomagenesis. Adv. Immunol. 105, 193-210 (2010).
    • (2010) Adv. Immunol. , vol.105 , pp. 193-210
    • Basso, K.1    Dalla-Favera, R.2
  • 10
    • 36749092865 scopus 로고    scopus 로고
    • RARa-PLZF overcomes PLZF-mediated repression of CRABPI, contributing to retinoid resistance in t(11;17) acute promyelocytic leukemia
    • Guidez, F. et al. RARa-PLZF overcomes PLZF-mediated repression of CRABPI, contributing to retinoid resistance in t(11;17) acute promyelocytic leukemia. Proc. Natl Acad. Sci. USA 104, 18694-18699 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 18694-18699
    • Guidez, F.1
  • 11
    • 0037057668 scopus 로고    scopus 로고
    • SATB1 targets chromatin remodelling toregulate genes over long distances
    • Yasui, D., Miyano, M., Cai, S., Varga-Weisz, P. & Kohwi-Shigematsu, T. SATB1 targets chromatin remodelling toregulate genes over long distances. Nature 419, 641-645 (2002).
    • (2002) Nature , vol.419 , pp. 641-645
    • Yasui, D.1    Miyano, M.2    Cai, S.3    Varga-Weisz, P.4    Kohwi-Shigematsu, T.5
  • 12
    • 33750465872 scopus 로고    scopus 로고
    • SATB1 packages densely looped, transcriptionally active chromatin for coordinated expression of cytokine genes
    • Cai, S., Lee, C. C. & Kohwi-Shigematsu, T. SATB1 packages densely looped, transcriptionally active chromatin for coordinated expression of cytokine genes. Nature Genet. 38, 1278-1288 (2006).
    • (2006) Nature Genet. , vol.38 , pp. 1278-1288
    • Cai, S.1    Lee, C.C.2    Kohwi-Shigematsu, T.3
  • 13
    • 40749122641 scopus 로고    scopus 로고
    • Transcriptional repression mediated by repositioning of genes to the nuclear lamina
    • Reddy, K. L., Zullo, J. M., Bertolino, E. & Singh, H. Transcriptional repression mediated by repositioning of genes to the nuclear lamina. Nature 452, 243-247 (2008).
    • (2008) Nature , vol.452 , pp. 243-247
    • Reddy, K.L.1    Zullo, J.M.2    Bertolino, E.3    Singh, H.4
  • 14
    • 84862639469 scopus 로고    scopus 로고
    • DNA sequence-dependent compartmentalization and silencing of chromatin at the nuclear lamina
    • Zullo, J. M. et al. DNA sequence-dependent compartmentalization and silencing of chromatin at the nuclear lamina. Cell 149, 1474-1487 (2012).
    • (2012) Cell , vol.149 , pp. 1474-1487
    • Zullo, J.M.1
  • 15
    • 84858692205 scopus 로고    scopus 로고
    • BAZF, a novel component of cullin3-based E3 ligase complex, mediates VEGFR and Notch cross-signaling in angiogenesis
    • Ohnuki, H. et al. BAZF, a novel component of cullin3-based E3 ligase complex, mediates VEGFR and Notch cross-signaling in angiogenesis. Blood 119, 2688-2698 (2012).
    • (2012) Blood , vol.119 , pp. 2688-2698
    • Ohnuki, H.1
  • 16
    • 79956194247 scopus 로고    scopus 로고
    • Promyelocytic leukemia zinc finger turns on the effector T cell program without requirement for agonist TCR signaling
    • Savage, A. K., Constantinides, M. G. & Bendelac, A. Promyelocytic leukemia zinc finger turns on the effector T cell program without requirement for agonist TCR signaling. J. Immunol. 186, 5801-5806 (2011).
    • (2011) J. Immunol. , vol.186 , pp. 5801-5806
    • Savage, A.K.1    Constantinides, M.G.2    Bendelac, A.3
  • 17
    • 33646886500 scopus 로고    scopus 로고
    • BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase
    • Kwon, J. E. et al. BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase. J. Biol. Chem. 281, 12664-12672 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 12664-12672
    • Kwon, J.E.1
  • 18
    • 33947107495 scopus 로고    scopus 로고
    • The Cullin3 ubiquitin ligase functions as a Nedd8-bound heterodimer
    • Wimuttisuk, W. & Singer, J. D. The Cullin3 ubiquitin ligase functions as a Nedd8-bound heterodimer. Mol. Biol. Cell 18, 899-909 (2007).
    • (2007) Mol. Biol. Cell , vol.18 , pp. 899-909
    • Wimuttisuk, W.1    Singer, J.D.2
  • 19
    • 84863505152 scopus 로고    scopus 로고
    • Adaptor protein self-assembly drives the control of a Cullin-RING ubiquitin ligase
    • Errington, W. J. et al. Adaptor protein self-assembly drives the control of a Cullin-RING ubiquitin ligase. Structure 20, 1141-1153 (2012).
    • (2012) Structure , vol.20 , pp. 1141-1153
    • Errington, W.J.1
  • 20
    • 79952675131 scopus 로고    scopus 로고
    • Follicular helper CD4 T cells (TFH)
    • Crotty, S. Follicular helper CD4 T cells (TFH). Annu. Rev. Immunol. 29, 621-663 (2011).
    • (2011) Annu. Rev. Immunol. , vol.29 , pp. 621-663
    • Crotty, S.1
  • 21
    • 0035169598 scopus 로고    scopus 로고
    • BCL-6 protein is expressed in precursor T-cell lymphoblastic lymphoma and in prenatal and postnatal thymus
    • Hyjek, E., Chadburn, A., Liu, Y. F., Cesarman, E. & Knowles, D. M. BCL-6 protein is expressed in precursor T-cell lymphoblastic lymphoma and in prenatal and postnatal thymus. Blood 97, 270-276 (2001).
    • (2001) Blood , vol.97 , pp. 270-276
    • Hyjek, E.1    Chadburn, A.2    Liu, Y.F.3    Cesarman, E.4    Knowles, D.M.5
  • 22
    • 78650964584 scopus 로고    scopus 로고
    • Cdt2 ubiquitin ligase inhibits invasion of a boundary-associated antisilencing factor into heterochromatin
    • Cdt2 ubiquitin ligase inhibits invasion of a boundary-associated antisilencing factor into heterochromatin. Cell 144, 41-54 (2011).
    • (2011) Cell , vol.144 , pp. 41-54
    • Braun, S.1
  • 23
    • 7244234099 scopus 로고    scopus 로고
    • Role of histone H2A ubiquitination in Polycomb silencing
    • Wang, H. et al. Role of histone H2A ubiquitination in Polycomb silencing. Nature 431, 873-878 (2004).
    • (2004) Nature , vol.431 , pp. 873-878
    • Wang, H.1
  • 24
    • 79954467406 scopus 로고    scopus 로고
    • Stabilization of Suv39H1 by SirT1 is part of oxidative stress response and ensures genome protection
    • Bosch-Presegué, L. et al. Stabilization of Suv39H1 by SirT1 is part of oxidative stress response and ensures genome protection. Mol. Cell 42, 210-223 (2011).
    • (2011) Mol. Cell , vol.42 , pp. 210-223
    • Bosch-Presegué, L.1
  • 25
    • 78049510229 scopus 로고    scopus 로고
    • DNMT1 stabilityisregulated by proteins coordinating deubiquitination and acetylation-driven ubiquitination
    • Du, Z. et al. DNMT1 stabilityisregulated by proteins coordinating deubiquitination and acetylation-driven ubiquitination. Sci. Signal. 3, ra80 (2010).
    • (2010) Sci. Signal. , vol.3
    • Du, Z.1
  • 26
    • 21144446865 scopus 로고    scopus 로고
    • Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase
    • Hernández-Muñoz, I. et al. Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase. Proc. Natl Acad. Sci. USA 102, 7635-7640 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 7635-7640
    • Hernández-Muñoz, I.1
  • 27
    • 79952539053 scopus 로고    scopus 로고
    • ATP-dependent chromatin remodeling: Genetics, genomics and mechanisms
    • Hargreaves, D. C. & Crabtree, G. R. ATP-dependent chromatin remodeling: genetics, genomics and mechanisms. Cell Res. 21, 396-420 (2011).
    • (2011) Cell Res. , vol.21 , pp. 396-420
    • Hargreaves, D.C.1    Crabtree, G.R.2
  • 28
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa, M. E., Bennett, E. J., Gygi, S. P. & Harper, J. W. Defining the human deubiquitinating enzyme interaction landscape. Cell 138, 389-403 (2009).
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 29
    • 78751590899 scopus 로고    scopus 로고
    • Silencing chromatin: Comparing modes and mechanisms
    • Beisel, C. & Paro, R. Silencing chromatin: comparing modes and mechanisms. Nature Rev. Genet. 12, 123-135 (2011).
    • (2011) Nature Rev. Genet. , vol.12 , pp. 123-135
    • Beisel, C.1    Paro, R.2
  • 30
    • 34248387664 scopus 로고    scopus 로고
    • Constitutive turnover of cyclin e by Cul3 maintains quiescence
    • McEvoy, J. D., Kossatz, U., Malek, N. & Singer, J. D. Constitutive turnover of cyclin E by Cul3 maintains quiescence. Mol. Cell. Biol. 27, 3651-3666 (2007).
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 3651-3666
    • McEvoy, J.D.1    Kossatz, U.2    Malek, N.3    Singer, J.D.4
  • 32
    • 21144458164 scopus 로고    scopus 로고
    • Immunoaffinity profiling oftyrosine phosphorylation incancer cells
    • Rush, J. et al. Immunoaffinity profiling oftyrosine phosphorylation incancer cells. Nature Biotechnol. 23, 94-101 (2005).
    • (2005) Nature Biotechnol. , vol.23 , pp. 94-101
    • Rush, J.1
  • 33
    • 23944464542 scopus 로고    scopus 로고
    • Characterization of the early stages inthymic NKT cell development
    • Benlagha, K., Wei, D. G., Veiga, J., Teyton, L. & Bendelac, A. Characterization of the early stages inthymic NKT cell development. J. Exp. Med. 202, 485-492 (2005).
    • (2005) J. Exp. Med. , vol.202 , pp. 485-492
    • Benlagha, K.1    Wei, D.G.2    Veiga, J.3    Teyton, L.4    Bendelac, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.