Nucleic Acids Research, 1993, Vol. 21, No. 18 4166-4173
© 1993
MOLECULAR BIOLOGY |
In vitro phosphorylation studies of a conserved region of the transcription factor ATF1
Imperial Cancer Reseearch Fund, Clare Hall Laboratories South Mimms, Herts En6 3LD, UK
*To whom correspondence should be addressed
Received July 8, 1993. Revised August 10, 1992. Accepted August 10, 1992.
A large family of mammalian transcription factors Including multiple variants of CREB, CREM and ATF1 have been Implicated in signal transduction by cAMP and other cellular pathways. Although the roles of some members of the family have been characterised the function of ATF1 Is poorly understood. We have Identified one or more key serine residues that are required for a phosphorylatlon-induced conformational change In ATF1. The critical serlnes map to a putative transcriptlonal activation domain of ATF1 and affect the stability of ATF1 DNA-blndlng. Intrigulngly phosphorylation is modulated by ATF1 homodimerisation and by ATF1 binding to DNA. One of the key serine residues required for ATF1 phosphorylation is not conserved In CREB and CREM suggesting that It Is likely to determine some specialised function of ATF1.
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