p300 modulates ATF4 stability and transcriptional activity independently of its acetyltransferase domain

doi:10.1074/jbc.M505294200

HOME

QUICK SEARCH:

	Author:		Keyword(s):
Year:		Vol:		Page:

A more recent version of this article appeared on December 16, 2005

This Article

	Full Text (Accepted Manuscript)
	All Versions of this Article: 280/50/41537 most recent M505294200v1
	Alert me when this article is cited
	Alert me if a correction is posted

Services

	Email this article to a friend
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new issues of the journal
	Download to citation manager
	Request Permissions

Citing Articles

	Citing Articles via HighWire
	Citing Articles via Google Scholar

Google Scholar

	Articles by Lassot, I.
	Articles by Margottin-Goguet, F.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Lassot, I.
	Articles by Margottin-Goguet, F.

Social Bookmarking

	What's this?

Papers In Press, published online ahead of print October 11, 2005
J. Biol. Chem, 10.1074/jbc.M505294200
Submitted on May 13, 2005
Revised on September 16, 2005
Accepted on October 5, 2005

p300 modulates ATF4 stability and transcriptional activity independently of its acetyltransferase domain

Irina Lassot, Emilie Estrabaud, Stephane Emiliani, Monsef Benkirane, Richard Benarous, and Florence Margottin-Goguet

Infectious deseases, Institut Cochin, Paris 75014

Corresponding Author: margottin-goguet{at}cochin.inserm.fr

ATF4 plays a crucial role in the cellular response to stress and multiple stress responses pathways converge to the translational upregulation of ATF4. ATF4 is a substrate of the SCFßTrCP ubiquitin ligase that binds to ßTrCP through phosphorylation on a DSGXXXS motif. We show here that ATF4 stability is also modulated by the histone acetyltransferase p300 which induces ATF4 stabilization by inhibiting its ubiquitination. Despite p300 acetylates ATF4, we found that p300 mediated ATF4 stabilization is independent of p300 catalytic activity, using either the inactive form of p300 or the acetylation mutant ATF4-K311R. ATF4 deleted of its p300 binding domain, is no more stabilized by p300, nor recruited into nuclear speckles. In consequence of ATF4 stabilization, both p300 and the catalytically inactive enzyme increases ATF4 transcriptional activity.

Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Add to Reddit Reddit Add to Technorati Technorati What's this?

This article has been cited by other articles:

S. Yu, Y. Jiang, D. L. Galson, M. Luo, Y. Lai, Y. Lu, H.-J. Ouyang, J. Zhang, and G. Xiao
General Transcription Factor IIA-{gamma} Increases Osteoblast-specific Osteocalcin Gene Expression via Activating Transcription Factor 4 and Runt-related Transcription Factor 2
J. Biol. Chem., February 29, 2008; 283(9): 5542 - 5553.
[Abstract] [Full Text] [PDF]

Y. Cherasse, A.-C. Maurin, C. Chaveroux, C. Jousse, V. Carraro, L. Parry, C. Deval, C. Chambon, P. Fafournoux, and A. Bruhat
The p300/CBP-associated factor (PCAF) is a cofactor of ATF4 for amino acid-regulated transcription of CHOP
Nucleic Acids Res., September 27, 2007; 35(17): 5954 - 5965.
[Abstract] [Full Text] [PDF]

C. M. Adams
Role of the Transcription Factor ATF4 in the Anabolic Actions of Insulin and the Anti-anabolic Actions of Glucocorticoids
J. Biol. Chem., June 8, 2007; 282(23): 16744 - 16753.
[Abstract] [Full Text] [PDF]