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Phosphorylation Negatively Regulates the Function of Coactivator PC4

Phosphorylation Negatively Regulates the Function of Coactivator PC4

H Ge, Y Zhao, B T Chait, R G Roeder

Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12691-5.

PMID: 7809103

Abstract:

Human positive cofactor 4 (PC4) mediates activator-dependent transcription by RNA polymerase II, apparently through interactions with transcriptional activators and the basal transcription machinery. We report here that PC4 function is modulated by in vivo phosphorylation. Protein-protein interaction studies and in vitro transcription assays demonstrate that only the nonphosphorylated form of PC4 is functionally active. Although recombinant PC4 can be phosphorylated by casein kinase II and protein kinase C in vitro, mutational and mass spectrometric analyses suggest that the in vivo hyperphosphorylation of PC4 is mediated mainly by casein kinase II and restricted to an N-terminal serine-rich region. These observations provide one example of a transcriptional cofactor that is negatively regulated by casein kinase II phosphorylation.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42414933	PC4, serine mutations human			Price

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