Desclozeaux, M; Poulat, F; Barbara, PD; Capony, JP; Turowski, P; Jay, P; ... Berta, P; + view all Desclozeaux, M; Poulat, F; Barbara, PD; Capony, JP; Turowski, P; Jay, P; Mejean, C; Moniot, B; Boizet, B; Berta, P; - view fewer (1998) Phosphorylation of an N-terminal motif enhances DNA-bindng activity of the human SRY protein. J BIOL CHEM , 273 (14) 7988 - 7995.
Of the several strategies that eukaryotes have evolved to modulate transcription factor activity, phosphorylation is regarded as one of the major mechanisms in signal-dependent transcriptional control, To conclusively demonstrate that the human sex-determining gene SRY is affected by such a post-translational control mechanism, we have analyzed its phosphorylation status in living cells. in the present study, we show that the cyclic AMP-dependent protein kinase (PKA) phosphorylates the human SRY protein in vitro as well as in vivo on serine residues located in the N-terminal part of the protein, This phosphorylation event was shown to positively regulate SRY DNA-binding activity and to enhance the ability of SRY to inhibit a basal promoter activity located downstream of an SRY DNA-binding site concatamer. Together these results strongly support the hypothesis that human SRY is a natural substrate for PKA in vivo and that this phosphorylation significantly modulates its major activity, DNA-binding, thereby possibly altering its biological function.
|Title:||Phosphorylation of an N-terminal motif enhances DNA-bindng activity of the human SRY protein|
|Open access status:||An open access publication|
|Keywords:||MAMMALIAN SEX DETERMINATION, TESTIS-DETERMINING FACTOR, DETERMINING GENE SRY, HMG BOX, TRANSCRIPTIONAL ACTIVITY, BINDING PROPERTIES, TRANSFECTED CELLS, C-JUN, KINASE, SEQUENCE|
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