Phosphorylation of ATF-1 enhances its DNA binding and transcription of the Na,K-ATPase 1 subunit gene promoter | Zendy

Makoto Kobayashi | Zendy; Akihiro Shimomura | Zendy; Masatoshi Hagiwara | Zendy; Kiyoshi Kawakami | Zendy

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Phosphorylation of ATF-1 enhances its DNA binding and transcription of the Na,K-ATPase 1 subunit gene promoter

Author(s) -

Makoto Kobayashi,

Akihiro Shimomura,

Masatoshi Hagiwara,

Kiyoshi Kawakami

Publication year - 1997

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/25.4.877

Subject(s) - biology , protein subunit , phosphorylation , gene , dna , transcription (linguistics) , promoter , transcription factor , dna binding protein , microbiology and biotechnology , atpase , genetics , gene expression , biochemistry , enzyme , linguistics , philosophy

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.

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