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			PubMed Journals: Proc Natl Acad Sci U S A

  Source:		PMID: 7708691


    		Proc Natl Acad Sci U S A. 1995 Mar
     		28;92(7):2597-601.

			Mutation of juxtamembrane tyrosine residue
			1001 suppresses loss-of-function mutations
			of the met receptor in epithelial cells.

			Weidner KM(1), Sachs M, Riethmacher D, Birchmeier
			W.

			Author Information
			(1) Max-Delbrück-Center for Molecular Medicine,
			Berlin, Germany.

			Signals transduced by the met tyrosine kinase,
			which is the receptor for scatter
			factor/hepatocyte growth factor, are of major
			importance for the regulation of epithelial
			cell motility, morphogenesis, and proliferation.
			We report here that different sets of tyrosine
			residues in the cytoplasmic domain of the
			met receptor affect signal transduction
			in epithelial cells in a positive or negative
			fashion: mutation of the C-terminal tyrosine
			residues 13-16 (Y1311, Y1347, Y1354, and
			Y1363) reduced or abolished ligand-induced
			cell motility and branching morphogenesis.
			In contrast, mutation of the juxtamembrane
			tyrosine residue 2 (Y1001) produced constitutively
			mobile, fibroblastoid cells. Furthermore,
			the gain-of-function mutation of tyrosine
			residue 2 suppressed the loss-of-function
			mutations of tyrosine residue 15 or 16.
			The opposite roles of the juxtamembrane
			and C-terminal tyrosine residues may explain
			the suggested dual function of the met receptor
			in both epithelial-mesenchymal interactions
			and tumor progression.

			PMCID: PMC42265 PMID: 7708691 [Indexed
			for MEDLINE]

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