Acetylation of adenovirus E1A regulates binding of the transcriptional corepressor CtBP

Zhang, Qinghong; Hong, Ying; Vo, Ngan; Goodman, Richard H.

doi:10.1073/pnas.011283598

Cited by 111 publications

(99 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…During the last few years, there have been several reports showing that the acetylation of lysine residues by HAT enzymes is not restricted to histones but is a frequent modification of transcription factors. Acetylation changes several functions of a protein and affects the DNA affinity, the cellular localization of transcription factors and the regulation of the cell cycle (Gu and Roeder, 1997;Imhof et al, 1997;Boyes et al, 1998;Zhang and Bieker, 1998;Hung et al, 1999;MartinezBalbas et al, 2000;Marzio et al, 2000;Zhang et al, 2000;Chan et al, 2001;Ferreira et al, 2001;Polanowska et al, 2001;Wang et al, 2001). Methylation, like acetylation and phosphorylation, represents a signal to perform a specific function and it is likely that in addition to histones, several transcription factors can be methylated.…”

Section: Discussionmentioning

confidence: 99%

SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo

et al. 2003

View full text Add to dashboard Cite

Acute myeloid leukemia 1 (AML1) belongs to a family of DNA-binding proteins highly conserved through evolution. AML1 regulates the expression of several hematopoietic genes and is essential for murine fetal liver hematopoiesis. We report here that the histone methyltransferase SUV39H1, a mammalian ortholog of the Drosophila melanogaster SU(VAR) 3-9, forms complex with AML1. SUV39H1 methylates lysine 9 of the histone protein H3 leading to the formation of the high-affinity binding site on chromatin for proteins of the heterochromatin protein 1 family (HP1). The interaction of AML1 with SUV39H1 requires the N-terminus of AML1 where the Runt domain is located. Binding of AML1 to SUV39H1 abrogates the transactivating and DNA-binding properties of AML1 and dissociates the net-like nuclear structure of AML1. It has been reported that AML1 is capable of interaction with histone acetyl transferases (CBP, p300, and MOZ) and with component of the histone deacetylase complex (Sin3), and that the interaction with these coregulators affects the strength of AML1 in promoter regulation. Our data suggest that other enzymes are also involved in gene regulation by AML1 activity by modulating the affinity of AML1 for DNA.

show abstract

Section: Discussionmentioning

confidence: 99%

SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo

et al. 2003

View full text Add to dashboard Cite

show abstract

“…PCAF is a coactivator that enhances the activity of numerous other activators and proteins involved in transcription, including class II transactivator (CIITA) (Spilianakis et al, 2000;Harton et al, 2001), MyoD (Sartorelli et al, 1999;Polesskaya et al, 2000), E2F1 (Martinez-Balbas et al, 2000), TAL1/SCL (Huang et al, 2000), RXR-RAR nuclear receptors (Blanco et al, 1998), E1A (Zhang et al, 2000) and TAF (Muth et al, 2001) and the architectural protein HMGI(Y) (Munshi et al, 2001). PCAF can function alone or together with p300/CBP coactivators through their interaction depending on target promoters.…”

Section: Discussionmentioning

confidence: 99%

PCAF is a coactivator for p73-mediated transactivation

et al. 2003

View full text Add to dashboard Cite

The tumor suppressor p53-related p73 shares significant amino-acid sequence identity with p53. Like p53, p73 recognizes canonical p53 DNA-binding sites and activates p53-responsive target genes and induces apoptosis. Moreover, transcription coactivator p300/CBP binds to and coactivates with both p53 and p73 in stimulating the expression of their target genes. Here, we report that coactivator PCAF binds to p73. The N-terminal transactivation domain (TAD) and the conserved oligomerization domain (OD) of p73 are both required for its interaction with PCAF. Conversely, PCAF's HAT-domain is required for and both the N-terminal region and Bromo domain enhance binding of PCAF to p73. Significantly, PCAF stimulates p73-mediated transactivation, and binding of PCAF to p73 is necessary for p73's transactivation activity. PCAF-specific siRNA dramatically reduces p73-mediated transactivation. Stimulation of p73-mediated transactivation by PCAF requires the HAT domain of PCAF and the p53-binding site within the p21 promoter. In vivo, coexpression of wild-type, but not HAT-deficient PCAF with p73b markedly increases p21 expression. Furthermore, cotransfection of PCAF and p73 leads to increased apoptosis and reduced colony formation. Collectively, these data suggest that p73 recruit PCAF to specific promoters to activate the transcription of p73 target genes.

show abstract

“…FLAG-CtBP and PET24bCtBP are described in ref. 10. CtBP1 was expressed as a His-6 fusion in BL21(DE3) and purified by Ni-nitrilotriacetic acid affinity chromatography (Qiagen, Valencia, CA).…”

Section: Methodsmentioning

confidence: 99%

Homeodomain-interacting protein kinase-2 mediates CtBP phosphorylation and degradation in UV-triggered apoptosis

Zhang

Nottke

Goodman

2005

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

View full text Add to dashboard Cite

Homeodomain-interacting protein kinase-2 (HIPK2) is a serine͞ threonine kinase involved in transcriptional regulation and apoptosis. The transcriptional corepressor CtBP (carboxyl-terminal binding protein) also plays a fundamental role in these processes. Our previous studies indicate that HIPK2 participates in a pathway of UV-triggered CtBP clearance that results in cell death. HIPK2 phosphorylates CtBP at Ser-422 in vitro. We developed a Ser-422 phospho-specific antibody to demonstrate that CtBP is phosphorylated on this residue in response to UV irradiation. HIPK2 knockdown blocked the UV-induced Ser-422 phosphorylation and degradation. The proteasomal inhibitor MG-132 treatment increased levels of ubiquitinated CtBP, which was induced by UV. Interference with HIPK2 function via the kinase-dead mutant decreased CtBP ubiquitination. Furthermore, a phosphopeptide spanning Ser-422 blocked UV-triggered CtBP degradation, confirming that Ser-422 phosphorylation marks CtBP for clearance. Consequently, interference with HIPK2 action in H1299 cells rescued UV-triggered apoptosis.

show abstract

Acetylation of adenovirus E1A regulates binding of the transcriptional corepressor CtBP

Cited by 111 publications

References 50 publications

SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo

SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo

PCAF is a coactivator for p73-mediated transactivation

Homeodomain-interacting protein kinase-2 mediates CtBP phosphorylation and degradation in UV-triggered apoptosis

Contact Info

Product

Resources

About