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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2001-1-22
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pubmed:abstractText |
Tyrosine 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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Ephrin-B1,
http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin G,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Guanylate Cyclase-Coupled,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Peptide,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/enterotoxin receptor
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0250-5991
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
339-46
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:11120586-Animals,
pubmed-meshheading:11120586-Blotting, Western,
pubmed-meshheading:11120586-Cell Line,
pubmed-meshheading:11120586-Chromatography, Thin Layer,
pubmed-meshheading:11120586-Ephrin-B1,
pubmed-meshheading:11120586-Escherichia coli,
pubmed-meshheading:11120586-Guanylate Cyclase,
pubmed-meshheading:11120586-Humans,
pubmed-meshheading:11120586-Immunoglobulin G,
pubmed-meshheading:11120586-Membrane Proteins,
pubmed-meshheading:11120586-Mice,
pubmed-meshheading:11120586-Peptide Mapping,
pubmed-meshheading:11120586-Phosphorylation,
pubmed-meshheading:11120586-Plasmids,
pubmed-meshheading:11120586-Precipitin Tests,
pubmed-meshheading:11120586-Protein Structure, Tertiary,
pubmed-meshheading:11120586-Receptors, Cell Surface,
pubmed-meshheading:11120586-Receptors, Guanylate Cyclase-Coupled,
pubmed-meshheading:11120586-Receptors, Peptide,
pubmed-meshheading:11120586-Recombinant Fusion Proteins,
pubmed-meshheading:11120586-Signal Transduction,
pubmed-meshheading:11120586-Tyrosine
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pubmed:year |
2000
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pubmed:articleTitle |
Tyrosine phosphorylation of the human guanylyl cyclase C receptor.
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pubmed:affiliation |
Department of Molecular Reproduction, Development and Genetics, Indian Institute of Science, Bangalore, India.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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