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			PubMed Journals: J Biol Chem

  Source:		PMID: 10318869


    		J Biol Chem. 1999 May 14;274(20):14434-43.
     
			MAPKAP kinase 2 phosphorylates
			serum response factor in vitro and in
			vivo.

			Heidenreich O(1), Neininger A, Schratt G,
			Zinck R, Cahill MA, Engel K, Kotlyarov A,
			Kraft R, Kostka S, Gaestel M, Nordheim A.

			Author Information
			(1) Institut für Zellbiologie, Abteilung
			Molekularbiologie, Universität Tübingen,
			D-72076 Tübingen, Germany.

			Several growth factor- and calcium-regulated
			kinases such as pp90(rsk) or CaM kinase
			IV can phosphorylate the transcription factor
			serum response factor (SRF) at serine 103
			(Ser-103). However, it is unknown whether
			stress-regulated kinases can also phosphorylate
			SRF. We show that treatment of cells with
			anisomycin, arsenite, sodium fluoride, or
			tetrafluoroaluminate induces phosphorylation
			of SRF at Ser-103 in both HeLa and NIH3T3
			cells. This phosphorylation is dependent
			on the kinase p38/SAPK2 and correlates with
			the activation of MAPKAP kinase 2 (MK2).
			MK2 phosphorylates SRF in vitro at Ser-103
			with similar efficiency as the small heat
			shock protein Hsp25 and significantly better
			than CREB. Comparison of wild type murine
			fibroblasts with those derived from MK2-deficient
			mice (Mk(-/-)) reveals MK2 as the major
			SRF kinase induced by arsenite. These results
			demonstrate that SRF is targeted by several
			signal transduction pathways within cells
			and establishes SRF as a nuclear target
			for MAPKAP kinase 2.

			PMID: 10318869 [Indexed for MEDLINE]

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