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pubmed-article:11120586pubmed:abstractTextTyrosine phosphorylation events are key components of several cellular signal transduction pathways. This study describes a novel method for identification of substrates for tyrosine kinases. Co-expression of the tyrosine kinase EphB1 with the intracellular domain of guanylyl cyclase C (GCC) in Escherichia coli cells resulted in tyrosine phosphorylation of GCC, indicating that GCC is a potential substrate for tyrosine kinases. Indeed, GCC expressed in mammalian cells is tyrosine phosphorylated, suggesting that tyrosine phosphorylation may play a role in regulation of GCC signalling. This is the first demonstration of tyrosine phosphorylation of any member of the family of membrane-associated guanylyl cyclases.lld:pubmed
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pubmed-article:11120586pubmed:articleTitleTyrosine phosphorylation of the human guanylyl cyclase C receptor.lld:pubmed
pubmed-article:11120586pubmed:affiliationDepartment of Molecular Reproduction, Development and Genetics, Indian Institute of Science, Bangalore, India.lld:pubmed
pubmed-article:11120586pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11120586pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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