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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
31
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pubmed:dateCreated |
2001-7-30
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pubmed:abstractText |
The endophilin family of proteins function in clathrin-mediated endocytosis. Here, we have identified and cloned the rat germinal center kinase-like kinase (rGLK), a member of the GCK (germinal center kinase) family of c-Jun N-terminal kinase (JNK) activating enzymes, as a novel endophilin I-binding partner. The interaction occurs both in vitro and in cells and is mediated by the Src homology 3 domain of endophilin I and a region of rGLK containing the endophilin consensus-binding sequence PPRPPPPR. Overlay analysis of rat brain extracts demonstrates that endophilin I is a major Src homology 3 domain-binding partner for rGLK. Overexpression of full-length endophilin I activates rGLK-mediated JNK activation, whereas N- and C-terminal fragments of endophilin I block JNK activation. Thus, endophilin I appears to have a novel function in JNK activation.
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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/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/JNK Mitogen-Activated Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/MAP4K5 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SH3GL2 protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
28913-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11384986-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:11384986-Amino Acid Sequence,
pubmed-meshheading:11384986-Animals,
pubmed-meshheading:11384986-Base Sequence,
pubmed-meshheading:11384986-Binding Sites,
pubmed-meshheading:11384986-Brain,
pubmed-meshheading:11384986-Carrier Proteins,
pubmed-meshheading:11384986-Consensus Sequence,
pubmed-meshheading:11384986-Enzyme Activation,
pubmed-meshheading:11384986-Gene Library,
pubmed-meshheading:11384986-Humans,
pubmed-meshheading:11384986-JNK Mitogen-Activated Protein Kinases,
pubmed-meshheading:11384986-Mitogen-Activated Protein Kinases,
pubmed-meshheading:11384986-Molecular Sequence Data,
pubmed-meshheading:11384986-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11384986-Rats,
pubmed-meshheading:11384986-Recombinant Fusion Proteins,
pubmed-meshheading:11384986-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:11384986-Sequence Alignment,
pubmed-meshheading:11384986-Sequence Homology, Amino Acid,
pubmed-meshheading:11384986-src Homology Domains
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pubmed:year |
2001
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pubmed:articleTitle |
Endophilin regulates JNK activation through its interaction with the germinal center kinase-like kinase.
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pubmed:affiliation |
Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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