메뉴 건너뛰기




Volumn 339, Issue 4, 2006, Pages 1069-1075

Acetylation and alternative splicing regulate ZNF76-mediated transcription

Author keywords

Acetylation; Alternative splicing; Sumoylation; TBP; Transcriptional repression; ZNF76

Indexed keywords

HISTONE DEACETYLASE 1; ISOPROTEIN; LYSINE; PROTEIN P300; PROTEIN ZNF76; TATA BINDING PROTEIN; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 29044435504     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.11.122     Document Type: Article
Times cited : (7)

References (22)
  • 2
    • 0025103786 scopus 로고
    • Characteristic chromosome abnormalities, including rearrangements of 6p, del(7q), +12, and t(12;14), in 44 uterine leiomyomas
    • M. Nilbert, S. Heim, N. Mandahl, U.M. Floderus, H. Willen, and F. Mitelman Characteristic chromosome abnormalities, including rearrangements of 6p, del(7q), +12, and t(12;14), in 44 uterine leiomyomas Hum. Genet. 85 1990 605 611
    • (1990) Hum. Genet. , vol.85 , pp. 605-611
    • Nilbert, M.1    Heim, S.2    Mandahl, N.3    Floderus, U.M.4    Willen, H.5    Mitelman, F.6
  • 3
    • 0029093828 scopus 로고
    • Staf, a novel zinc finger protein that activates the RNA polymerase III promoter of the selenocysteine tRNA gene
    • C. Schuster, E. Myslinski, A. Krol, and P. Carbon Staf, a novel zinc finger protein that activates the RNA polymerase III promoter of the selenocysteine tRNA gene EMBO J. 14 1995 3777 3787
    • (1995) EMBO J. , vol.14 , pp. 3777-3787
    • Schuster, C.1    Myslinski, E.2    Krol, A.3    Carbon, P.4
  • 4
    • 0037067750 scopus 로고    scopus 로고
    • Complex regulation of human neuronal nitric-oxide synthase exon 1c gene transcription. Essential role of Sp and ZNF family members of transcription factors
    • D. Saur, B. Seidler, H. Paehge, V. Schusdziarra, and H.D. Allescher Complex regulation of human neuronal nitric-oxide synthase exon 1c gene transcription. Essential role of Sp and ZNF family members of transcription factors J. Biol. Chem. 277 2002 25798 25814
    • (2002) J. Biol. Chem. , vol.277 , pp. 25798-25814
    • Saur, D.1    Seidler, B.2    Paehge, H.3    Schusdziarra, V.4    Allescher, H.D.5
  • 5
    • 0034666140 scopus 로고    scopus 로고
    • Transcriptional regulation of the mouse cytosolic chaperonin subunit gene Ccta/t-complex polypeptide 1 by selenocysteine tRNA gene transcription activating factor family zinc finger proteins
    • H. Kubota, S. Yokota, H. Yanagi, and T. Yura Transcriptional regulation of the mouse cytosolic chaperonin subunit gene Ccta/t-complex polypeptide 1 by selenocysteine tRNA gene transcription activating factor family zinc finger proteins J. Biol. Chem. 275 2000 28641 28648
    • (2000) J. Biol. Chem. , vol.275 , pp. 28641-28648
    • Kubota, H.1    Yokota, S.2    Yanagi, H.3    Yura, T.4
  • 6
    • 5644261273 scopus 로고    scopus 로고
    • ZNF76, a novel transcriptional repressor targeting TATA-binding protein, is modulated by sumoylation
    • G. Zheng, and Y.C. Yang ZNF76, a novel transcriptional repressor targeting TATA-binding protein, is modulated by sumoylation J. Biol. Chem. 279 2004 42410 42421
    • (2004) J. Biol. Chem. , vol.279 , pp. 42410-42421
    • Zheng, G.1    Yang, Y.C.2
  • 7
    • 0032555502 scopus 로고    scopus 로고
    • ZNF76 and ZNF143 are two human homologs of the transcriptional activator Staf
    • E. Myslinski, A. Krol, and P. Carbon ZNF76 and ZNF143 are two human homologs of the transcriptional activator Staf J. Biol. Chem. 273 1998 21998 22006
    • (1998) J. Biol. Chem. , vol.273 , pp. 21998-22006
    • Myslinski, E.1    Krol, A.2    Carbon, P.3
  • 8
    • 0013900616 scopus 로고
    • RNA synthesis and histone acetylation during the course of gene activation in lymphocytes
    • B.G. Pogo, V.G. Allfrey, and A.E. Mirsky RNA synthesis and histone acetylation during the course of gene activation in lymphocytes Proc. Natl. Acad. Sci. USA 55 1966 805 812
    • (1966) Proc. Natl. Acad. Sci. USA , vol.55 , pp. 805-812
    • Pogo, B.G.1    Allfrey, V.G.2    Mirsky, A.E.3
  • 9
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • W. Gu, and R.G. Roeder Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain Cell 90 1997 595 606
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 10
    • 0035694469 scopus 로고    scopus 로고
    • Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases
    • N.A. Barlev, L. Liu, N.H. Chehab, K. Mansfield, K.G. Harris, T.D. Halazonetis, and S.L. Berger Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases Mol. Cell 8 2001 1243 1254
    • (2001) Mol. Cell , vol.8 , pp. 1243-1254
    • Barlev, N.A.1    Liu, L.2    Chehab, N.H.3    Mansfield, K.4    Harris, K.G.5    Halazonetis, T.D.6    Berger, S.L.7
  • 11
    • 0032910957 scopus 로고    scopus 로고
    • CREB-Binding protein acetylates hematopoietic transcription factor GATA-1 at functionally important sites
    • H.L. Hung, J. Lau, A.Y. Kim, M.J. Weiss, and G.A. Blobel CREB-Binding protein acetylates hematopoietic transcription factor GATA-1 at functionally important sites Mol. Cell. Biol. 19 1999 3496 3505
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3496-3505
    • Hung, H.L.1    Lau, J.2    Kim, A.Y.3    Weiss, M.J.4    Blobel, G.A.5
  • 12
    • 0037184969 scopus 로고    scopus 로고
    • Acetylation of p53 inhibits its ubiquitination by Mdm2
    • M. Li, J. Luo, C.L. Brooks, and W. Gu Acetylation of p53 inhibits its ubiquitination by Mdm2 J. Biol. Chem. 277 2002 50607 50611
    • (2002) J. Biol. Chem. , vol.277 , pp. 50607-50611
    • Li, M.1    Luo, J.2    Brooks, C.L.3    Gu, W.4
  • 15
    • 0035979737 scopus 로고    scopus 로고
    • Duration of nuclear NF-kappaB action regulated by reversible acetylation
    • L. Chen, W. Fischle, E. Verdin, and W.C. Greene Duration of nuclear NF-kappaB action regulated by reversible acetylation Science 293 2001 1653 1657
    • (2001) Science , vol.293 , pp. 1653-1657
    • Chen, L.1    Fischle, W.2    Verdin, E.3    Greene, W.C.4
  • 16
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • T. Kouzarides Acetylation: a regulatory modification to rival phosphorylation? EMBO J. 19 2000 1176 1179
    • (2000) EMBO J. , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 17
    • 0037154963 scopus 로고    scopus 로고
    • Cooperation between complexes that regulate chromatin structure and transcription
    • G.J. Narlikar, H.Y. Fan, and R.E. Kingston Cooperation between complexes that regulate chromatin structure and transcription Cell 108 2002 475 487
    • (2002) Cell , vol.108 , pp. 475-487
    • Narlikar, G.J.1    Fan, H.Y.2    Kingston, R.E.3
  • 18
    • 0036337915 scopus 로고    scopus 로고
    • A genomic view of alternative splicing
    • B. Modrek, and C. Lee A genomic view of alternative splicing Nat. Genet. 30 2002 13 19
    • (2002) Nat. Genet. , vol.30 , pp. 13-19
    • Modrek, B.1    Lee, C.2
  • 19
    • 4744361591 scopus 로고    scopus 로고
    • Site-specific acetylation of the fetal globin activator NF-E4 prevents its ubiquitination and regulates its interaction with the histone deacetylase, HDAC1
    • Q. Zhao, H. Cumming, L. Cerruti, J.M. Cunningham, and S.M. Jane Site-specific acetylation of the fetal globin activator NF-E4 prevents its ubiquitination and regulates its interaction with the histone deacetylase, HDAC1 J. Biol. Chem. 279 2004 41477 41486
    • (2004) J. Biol. Chem. , vol.279 , pp. 41477-41486
    • Zhao, Q.1    Cumming, H.2    Cerruti, L.3    Cunningham, J.M.4    Jane, S.M.5
  • 20
    • 0034721644 scopus 로고    scopus 로고
    • Protein diversity from alternative splicing: A challenge for bioinformatics and post-genome biology
    • D.L. Black Protein diversity from alternative splicing: a challenge for bioinformatics and post-genome biology Cell 103 2000 367 370
    • (2000) Cell , vol.103 , pp. 367-370
    • Black, D.L.1
  • 21
    • 0036753547 scopus 로고    scopus 로고
    • Control of Smad7 stability by competition between acetylation and ubiquitination
    • E. Gronroos, U. Hellman, C.H. Heldin, and J. Ericsson Control of Smad7 stability by competition between acetylation and ubiquitination Mol. Cell 10 2002 483 493
    • (2002) Mol. Cell , vol.10 , pp. 483-493
    • Gronroos, E.1    Hellman, U.2    Heldin, C.H.3    Ericsson, J.4
  • 22
    • 3142720638 scopus 로고    scopus 로고
    • Transforming growth factor-beta stimulates p300-dependent RUNX3 acetylation, which inhibits ubiquitination-mediated degradation
    • Y.H. Jin, E.J. Jeon, Q.L. Li, Y.H. Lee, J.K. Choi, W.J. Kim, K.Y. Lee, and S.C. Bae Transforming growth factor-beta stimulates p300-dependent RUNX3 acetylation, which inhibits ubiquitination-mediated degradation J. Biol. Chem. 279 2004 29409 29417
    • (2004) J. Biol. Chem. , vol.279 , pp. 29409-29417
    • Jin, Y.H.1    Jeon, E.J.2    Li, Q.L.3    Lee, Y.H.4    Choi, J.K.5    Kim, W.J.6    Lee, K.Y.7    Bae, S.C.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.