PubMed Journals: Mol Cell Biol

  Source:		PMID: 9199329

    		Mol Cell Biol. 1997 Jul;17(7):3947-54.
			Mitogen-activated and cyclin-dependent protein
			kinases selectively and differentially modulate
			transcriptional enhancement by the glucocorticoid

			Krstic MD(1), Rogatsky I, Yamamoto KR, Garabedian

			Author Information
			(1) Biochemistry and Biophysics,
			University of California, San Francisco,
			94143-0445, USA.

			Cyclin-dependent kinase (CDK) and mitogen-activated
			protein kinase (MAPK) phosphorylate the
			rat glucocorticoid receptor in vitro at
			distinct sites that together correspond
			to the major phosphorylated receptor residues
			observed in vivo; MAPK phosphorylates receptor
			residues threonine 171 and serine 246, whereas
			multiple CDK complexes modify serines 224
			and 232. Mutations in these kinases have
			opposite effects on receptor transcriptional
			activity in vivo. Receptor-dependent transcriptional
			enhancement is reduced in yeast strains
			deficient in the catalytic (p34CDC28) or
			certain regulatory (cyclin) subunits of
			CDK complexes and is increased in a strain
			devoid of the mammalian MAPK homologs FUS3
			and KSS1. These findings indicate that the
			glucocorticoid receptor is a target for
			multiple kinases in vivo, which either positively
			or negatively regulate receptor transcriptional
			enhancement. The control of receptor transcriptional
			activity via phosphorylation provides an
			increased array of regulatory inputs that,
			in addition to steroid hormones, can influence
			receptor function.

			PMCID: PMC232247 PMID: 9199329 [Indexed
			for MEDLINE]

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