Max is a ubiquitous transcription factor with a bHLHZip [basic HLH (helix–loop–helix) leucine zipper] DNA-binding/dimerization domain and the central component of the Myc/Max/Mad transcription factor network that controls cell growth, proliferation, differentiation and apoptotic cell death in metazoans. Max is the obligatory DNA-binding and dimerization partner for all the bHLHZip regulators of the Myc/Max/Mad network, including the Myc family of oncoproteins and the Mad family of Myc antagonists, which recognize E-box DNA elements in the regulatory regions of target genes. Max lacks a transcription regulatory domain and is the only member of the network that efficiently homodimerizes. Binding of Max homodimers to E-box elements suppresses the transcription regulatory functions of its network partners and of other non-network E-box-binding regulators. In contrast with its highly regulated partners, Max is a constitutively expressed and phosphorylated protein. Phosphorylation is, however, the only Max post-translational modification identified so far. In the present study, we have analysed Max posttranslational modifications by MS. We have found that Max is acetylated at several lysine residues (Lys-57, Lys-144 and Lys-145) in mammalian cells. Max acetylation is stimulated by inhibitors of histone deacetylases and by overexpression of the p300 co-activator/HAT (histone acetyltransferase). The p300 HAT also directly acetylates Max in vitro at these three residues. Interestingly, the three Max residues acetylated in vivo and in vitro by p300 are important for Max nuclear localization and Max-mediated suppression of Myc transactivation. These results uncover novel post-translational modifications of Max and suggest the potential regulation of specific Max complexes by p300 and reversible acetylation.
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Research Article|
April 12 2007
Max is acetylated by p300 at several nuclear localization residues
Francesco Faiola;
Francesco Faiola
1
*Department of Biochemistry, University of California Riverside, Riverside, CA 92521, U.S.A.
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Yi-Ting Wu;
Yi-Ting Wu
1
*Department of Biochemistry, University of California Riverside, Riverside, CA 92521, U.S.A.
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Songqin Pan;
Songqin Pan
†W.M. Keck Proteomics Laboratory, Center for Plant Cell Biology, University of California Riverside, Riverside, CA 92521, U.S.A.
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Kangling Zhang;
Kangling Zhang
‡Department of Chemistry, University of California Riverside, Riverside, CA 92521, U.S.A.
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Anthony Farina;
Anthony Farina
*Department of Biochemistry, University of California Riverside, Riverside, CA 92521, U.S.A.
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Ernest Martinez
Ernest Martinez
2
*Department of Biochemistry, University of California Riverside, Riverside, CA 92521, U.S.A.
2To whom correspondence should be addressed (email ernest.martinez@ucr.edu).
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Publisher: Portland Press Ltd
Received:
October 20 2006
Revision Received:
December 13 2006
Accepted:
January 12 2007
Accepted Manuscript online:
January 12 2007
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Authors Journal compilation, The Biochemical Society, London
2007
Biochem J (2007) 403 (3): 397–407.
Article history
Received:
October 20 2006
Revision Received:
December 13 2006
Accepted:
January 12 2007
Accepted Manuscript online:
January 12 2007
Citation
Francesco Faiola, Yi-Ting Wu, Songqin Pan, Kangling Zhang, Anthony Farina, Ernest Martinez; Max is acetylated by p300 at several nuclear localization residues. Biochem J 1 May 2007; 403 (3): 397–407. doi: https://doi.org/10.1042/BJ20061593
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