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Titolo:
The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases
Autore:
Wu, WS; Vallian, S; Seto, E; Yang, WM; Edmondson, D; Roth, S; Chang, KS;
Indirizzi:
Univ Texas, MD Anderson Canc Ctr, Dept Mol Pathol, Houston, TX 77030 USA Univ Texas Houston TX USA 77030 r, Dept Mol Pathol, Houston, TX 77030 USA Univ Texas, MD Anderson Canc Ctr, Dept Biochem & Mol Biol, Houston, TX 77030 USA Univ Texas Houston TX USA 77030 Biochem & Mol Biol, Houston, TX 77030 USA Univ S Florida, Coll Med, H Lee Moffitt Canc Ctr & Res Inst, Tampa, FL 33612 USA Univ S Florida Tampa FL USA 33612 anc Ctr & Res Inst, Tampa, FL 33612 USA
Titolo Testata:
MOLECULAR AND CELLULAR BIOLOGY
fascicolo: 7, volume: 21, anno: 2001,
pagine: 2259 - 2268
SICI:
0270-7306(200104)21:7<2259:TGSPRT>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACUTE PROMYELOCYTIC LEUKEMIA; ARSENIC TRIOXIDE AS2O3; TRANS-RETINOIC ACID; RAR-ALPHA; RETINOBLASTOMA PROTEIN; NUCLEAR-BODIES; T(15-17) TRANSLOCATION; HUMAN CYTOMEGALOVIRUS; NUCLEOSOMAL DNA; CANCER CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
77
Recensione:
Indirizzi per estratti:
Indirizzo: Chang, KS Univ Texas, MD Anderson Canc Ctr, Dept Mol Pathol, Box 054,1515 Holcombe Blvd, Houston, TX 77030 USA Univ Texas Box 054,1515 Holcombe Blvd Houston TX USA 77030 0 USA
Citazione:
W.S. Wu et al., "The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases", MOL CELL B, 21(7), 2001, pp. 2259-2268

Abstract

The growth suppressor promyelocytic leukemia protein (PML) is disrupted bythe chromosomal translocation t(15;17) in acute promyelocytic leukemia (APL). PML plays a key role in multiple pathways of apoptosis and regulates cell cycle progression. The present study demonstrates that PML represses transcription by functionally and physically interacting with histone deacetylase (HDAC). Transcriptional repression mediated by PML can be inhibited by trichostatin A, a specific inhibitor of HDAC. PML coimmunoprecipitates a significant level of HDAC activity in several cell lines. PML is associated with HDAC in vivo and directly interacts with HDAC in vitro. The fusion protein PML-RAR alpha encoded by the t(15;17) breakpoint interacts with HDAC poorly. PML interacts with all three isoforms of HDAC through specific domains, and its expression deacetylates histone H3 in vivo. Together, the results of our study show that PML modulates histone deacetylation and that loss of this function in APL alters chromatin remodeling and gene expression. This event may contribute to the development of leukemia.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 02:46:25