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			PubMed Journals: Nucleic Acids Res

  Source:		PMID: 9016641


    		Nucleic Acids Res. 1997 Feb 15;25(4):877-82.
     
			Phosphorylation of ATF-1 enhances its DNA
			binding and transcription of the Na,K-ATPase
			alpha 1 subunit gene promoter.

			Kobayashi M(1), Shimomura A, Hagiwara M,
			Kawakami K.

			Author Information
			(1) Department of Biology, Jichi Medical
			School, Tochigi, Japan.

			Transcriptional activity of both ATF-1 and
			CREB is enhanced by protein phosphorylation.
			While enhancement has been attributed to
			an increase in binding affinity for a co-activator
			(CBP), induction of the DNA binding activity
			by phosphorylation is an open question.
			Using the Na,K-ATPase alpha1 subunit gene
			promoter, which has an asymmetrical ATF/CRE
			site, we analyzed the effect of phosphorylation
			on DNA binding activity of the ATF-1-CREB
			heterodimer. Dephosphorylation of the heterodimer
			in nuclear extracts reduced binding to the
			ATF/CRE site. Phosphorylation of ATF-1 at
			Ser63 enhanced its binding to the ATF/CRE
			site in both the homodimeric and heterodimeric
			forms. Transcription of the Na,K-ATPase
			alpha 1 subunit gene promoter was also stimulated
			by phosphorylated ATF-1 in vitro.

			PMCID: PMC146500 PMID: 9016641 [Indexed
			for MEDLINE]

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