http://www.cnr.it/ontology/cnr/individuo/prodotto/ID4619

PC4 co-activates MyoD by relieving the HDAC4-mediated inhibition of MEF2C. (Articolo in rivista)

Type

Label

PC4 co-activates MyoD by relieving the HDAC4-mediated inhibition of MEF2C. (Articolo in rivista) (literal)

Anno

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

Alternative label

Micheli L.,1; Leonardi L.,1; Conti F.,1; Buanne P.,1; Canu N.,2; Caruso M.,1; and Tirone F.,1 (2005)
PC4 co-activates MyoD by relieving the HDAC4-mediated inhibition of MEF2C.
in Molecular and cellular biology (Print); ASM, American society for microbiology, Washington, DC (Stati Uniti d'America)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Micheli L.,1; Leonardi L.,1; Conti F.,1; Buanne P.,1; Canu N.,2; Caruso M.,1; and Tirone F.,1 (literal)

Pagina inizio

Pagina fine

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

Rivista

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

Note

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

1 = Istituto di Neurobiologia e Medicina Molecolare, Consiglio Nazionale delle Ricerche/Fondazione Santa Lucia, Via del Fosso di Fiorano, 64 - 00143, Rome, Italy; 2 = Dipartimento di Neuroscienze, Facoltà di Medicina e Chirurgia, Università di Tor Vergata, Rome, Italy. (literal)

Titolo

PC4 co-activates MyoD by relieving the HDAC4-mediated inhibition of MEF2C. (literal)

Abstract

Histone deacetylase 4 (HDAC4) negatively regulates skeletal myogenesis by associating with the myocyte enhancer factor 2 (MEF2) transcription factors. Our data indicate that the gene PC4 (interferon-related developmental regulator 1 [IFRD1], Tis7), which we have previously shown to be required for myoblast differentiation, is both induced by MyoD and potentiates the transcriptional activity of MyoD, thus revealing a positive regulatory loop between these molecules. Enhancement by PC4 of MyoD-dependent activation of muscle gene promoters occurs selectively through MEF2 binding sites. Furthermore, PC4 localizes in the nucleus of differentiating myoblasts, associates with MEF2C, and is able to counteract the HDAC4-mediated inhibition of MEF2C. This latter action can be explained by the observed ability of PC4 to dose dependently displace HDAC4 from MEF2C. Consistently, we have observed that (i) the region of PC4 that binds MEF2C is sufficient to counteract the inhibition by HDAC4; (ii) PC4, although able to bind HDAC4, does not inhibit the enzymatic activity of HDAC4; and (iii) PC4 overcomes the inhibition mediated by the amino-terminal domain of HDAC4, which associates with MEF2C but not with PC4. Together, our findings strongly suggest that PC4 acts as a coactivator of MyoD and MEF2C by removing the inhibitory effect of HDAC4, thus exerting a pivotal function during myogenesis. (literal)

Editore