|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5
|
|
pubmed:dateCreated |
1991-5-21
|
|
pubmed:abstractText |
GTPase-activating protein (GAP) stimulates the ability of p21ras to hydrolyze GTP to GDP. Since GAP is phosphorylated by a variety of activated or oncogenic protein-tyrosine kinases, it may couple tyrosine kinases to the Ras signaling pathway. The epidermal growth factor (EGF) receptor cytoplasmic domain phosphorylated human GAP in vitro within a single tryptic phosphopeptide. The same GAP peptide was also apparently phosphorylated on tyrosine in EGF-stimulated rat fibroblasts. Circumstantial evidence suggested that residue 460 might be the site of GAP tyrosine phosphorylation. This possibility was confirmed by phosphorylation of a synthetic peptide corresponding to the predicted tryptic peptide containing Tyr-460. Alteration of Tyr-460 to phenylalanine by site-directed mutagenesis diminished the in vitro phosphorylation of a bacterial GAP polypeptide by the EGF receptor. We conclude that Tyr-460 is a site of GAP tyrosine phosphorylation by the EGF receptor in vitro and likely in vivo. GAP Tyr-460 is located immediately C terminal to the second GAP SH2 domain, suggesting that its phosphorylation might have a role in regulating protein-protein interactions.
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-1688326,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-1689011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-1689310,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-1689311,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-1696179,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-2153302,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-2153914,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-2156626,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-2157284,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-2158859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-2173144,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-2176151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-2236073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-2430174,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-2441878,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-2472218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-2472219,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-2475255,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-2480526,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-2821624,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-2833702,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-2833817,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-2842690,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-3078956,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-3201259,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-3927152,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-6196603,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1850098-6327076
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotide Probes,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/ras GTPase-Activating Proteins
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
May
|
|
pubmed:issn |
0270-7306
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
11
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
2511-6
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:1850098-Amino Acid Sequence,
pubmed-meshheading:1850098-Animals,
pubmed-meshheading:1850098-Base Sequence,
pubmed-meshheading:1850098-Cell Line,
pubmed-meshheading:1850098-Cloning, Molecular,
pubmed-meshheading:1850098-GTPase-Activating Proteins,
pubmed-meshheading:1850098-Humans,
pubmed-meshheading:1850098-Molecular Sequence Data,
pubmed-meshheading:1850098-Mutagenesis, Site-Directed,
pubmed-meshheading:1850098-Oligonucleotide Probes,
pubmed-meshheading:1850098-Peptide Fragments,
pubmed-meshheading:1850098-Peptide Mapping,
pubmed-meshheading:1850098-Phosphorylation,
pubmed-meshheading:1850098-Protein-Tyrosine Kinases,
pubmed-meshheading:1850098-Proteins,
pubmed-meshheading:1850098-Rats,
pubmed-meshheading:1850098-Receptor, Epidermal Growth Factor,
pubmed-meshheading:1850098-Recombinant Fusion Proteins,
pubmed-meshheading:1850098-Transfection,
pubmed-meshheading:1850098-Trypsin,
pubmed-meshheading:1850098-Tyrosine,
pubmed-meshheading:1850098-ras GTPase-Activating Proteins
|
|
pubmed:year |
1991
|
|
pubmed:articleTitle |
The epidermal growth factor receptor phosphorylates GTPase-activating protein (GAP) at Tyr-460, adjacent to the GAP SH2 domains.
|
|
pubmed:affiliation |
Division of Molecular and Developmental Biology, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
