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J. Biol. Chem., Vol. 279, Issue 53, 55667-55674, December 31, 2004

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Nerve Growth Factor Receptor Signaling Induces Histone Acetyltransferase Domain-dependent Nuclear Translocation of p300/CREB-binding Protein-associated Factor and hGCN5 Acetyltransferases^*

Kasuen Wong, Junyu Zhang, Soumya Awasthi, Anima Sharma, Lowery Rogers, Elizabeth F. Matlock, Carine Van Lint¶||, Tatiana Karpova**, James McNally**, and Robert Harrod

From the Laboratory of Molecular Virology, Department of Biological Sciences, Southern Methodist University, Dallas, Texas 75275-0376, ^¶Universite Libre de Bruxelles, Institut de Biologie et de Medecine Moleculaires, Laboratoire de Chimie Biologique, 12 Rue des Profs. Jeener et Brachet, 6041 Gosselies, Belgium, and ^**Laboratory of Receptor Biology and Gene Expression, Fluorescence Imaging Facility, Center for Cancer Research, NCI, National Institutes of Health, Bethesda, Maryland 20892-0001

The transcriptional coactivators, p300/CREB-binding protein-associated factor (PCAF) and hGCN5, are recruited to chromatin-remodeling complexes on enhancers of various gene promoters in response to growth factor stimulation. However, the molecular mechanisms by which surface receptor signals modulate the assembly of nuclear transcription complexes are not fully understood. Here we report that nerve growth factor receptor signaling induces nuclear translocation of PCAF and hGCN5 dependent upon the phosphorylation of Ser and Thr residues within their histone acetyltransferase domains, which requires activation of PI3K, Rsk2^pp90, and MSK-1. Neurotrophin stimulation induces p53_K320 acetylation by PCAF and transcriptionally activates p53-responsive enhancer elements within the p21^WAF/CIP1 promoter associated with G₁/S arrest during neuronal differentiation. Most importantly, these findings represent the first evidence for signal-dependent nuclear translocation of PCAF and hGCN5 acetyltransferases and allude to a novel mechanism for ligand/receptor modulation of nuclear chromatin-remodeling complexes in neurons.

Received for publication, July 19, 2004 , and in revised form, October 12, 2004.

^* This work was supported in part by the Department of Biological Sciences, Southern Methodist University, Dallas, and the NCI, National Institutes of Health. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Both authors contributed equally to this work.

^|| Maître de Recherches from the Fonds National de la Recherche Scientifique (Belgium) and supported by grants from Fonds National de la Recherche Scientifique, Televie, Free University of Brussels (ARC), Internationale Brachet Stiftung, CGRI-INSERM Cooperation, and Theyskens-Mineur Foundation, Region Wallone-Commission Europeenne FEDER, and the Agence Nationale de Recherches sur le SIDA (France).

To whom correspondence should be addressed: Laboratory of Molecular Virology, Dept. of Biological Sciences, Southern Methodist University, 334-DLS, 6501 Airline Dr., Dallas, TX 75275-0376. Tel.: 214-768-3864; Fax: 214-768-3955; E-mail: rharrod{at}mail.smu.edu.

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