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			PubMed Journals: Biochim Biophys Acta

  Source:		PMID: 8898866


    		Biochim Biophys Acta. 1996 Oct 11;1313(3):283-9.
     
			Mapping of a regulatory important site for
			protein kinase C phosphorylation in the
			N-terminal domain of annexin II.

			Jost M(1), Gerke V.

			Author Information
			(1) University of Münster, Clinical Research
			Group for Endothelial Cell Biology, Münster,
			Germany.

			Annexin II is a Ca(2+)-regulated membrane-
			and cytoskeleton-binding protein implicated
			in membrane transport events along the
			Ca(2+)-regulated secretory and the early
			endocytic pathway. Biochemical properties
			of this annexin and its intracellular distribution
			are regulated by complex formation with
			p11 (S100A10), a member of the S100 protein
			family. The annexin II-p11 interaction is
			mediated through the unique N-terminal domain
			of annexin II and is inhibited by protein
			kinase C phosphorylation of a serine residue
			in annexin II. To map this regulatory serine
			phosphorylation site we developed a
			baculovirus-mediated expression system for
			wild-type annexin II and for a series of
			annexin II mutants which contained substitutions
			in one or more serine residues present in
			the N-terminal domain. The different mutant
			derivatives were purified and shown to display
			the same biochemical properties as recombinant
			wild-type annexin II and the authentic protein
			purified from porcine intestine. However,
			significant differences in phosphate incorporation
			were observed when the individual serine
			mutants were subjected to phosphorylation
			by protein kinase C. A comparison of the
			phosphorylation patterns obtained identified
			Ser-II as the protein kinase C site responsible
			for regulating the annexin II-p11 interaction.
			Ser-II lies within the sequence mediating
			p11 binding, i.e. amino-acid residues 1
			to 14 of annexin II, and phosphorylation
			at this site most likely leads to a direct
			spatial interference with p11 binding.

			PMID: 8898866 [Indexed for MEDLINE]

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