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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2002-12-16
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pubmed:abstractText |
Using antibody against the Rho binding domain of ROKalpha, two neuronal phosphoproteins of 62 and 80 kDa were co-immunoprecipitated from brain extracts. Peptide analysis revealed their identity as collapsin response mediator proteins (CRMPs); p62 was CRMP-2 whereas p80 was a novel splice form of CRMP-1 with an extended N-terminus. p80 CRMP-1 was able to complex with CRMP-2, suggesting that p80 CRMP-1 and CRMP-2 form oligomers. CRMP-2 was the major substrate of ROK. p80 CRMP-1 interacted with the kinase domain of ROKalpha, resulting in inhibition of the catalytic activity towards other substrates. Over-expression of p80 CRMP-1 and CRMP-2 together counteracted the effects of RhoA on neurite retraction, an effect enhanced by mutation of the ROK phosphorylation site in CRMP-2. p80 CRMP-1 and CRMP-2 may be modulators of RhoA-dependent signaling, through interaction with and regulation of ROKalpha.
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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/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/collapsin response mediator...,
http://linkedlifedata.com/resource/pubmed/chemical/collapsin response mediator...,
http://linkedlifedata.com/resource/pubmed/chemical/rho-Associated Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/rhoA GTP-Binding Protein
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
532
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
445-9
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:12482610-Alternative Splicing,
pubmed-meshheading:12482610-Amino Acid Sequence,
pubmed-meshheading:12482610-Animals,
pubmed-meshheading:12482610-Blotting, Western,
pubmed-meshheading:12482610-Brain,
pubmed-meshheading:12482610-COS Cells,
pubmed-meshheading:12482610-Catalysis,
pubmed-meshheading:12482610-Chromosome Mapping,
pubmed-meshheading:12482610-DNA, Complementary,
pubmed-meshheading:12482610-Dimerization,
pubmed-meshheading:12482610-Genetic Vectors,
pubmed-meshheading:12482610-Humans,
pubmed-meshheading:12482610-Intercellular Signaling Peptides and Proteins,
pubmed-meshheading:12482610-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:12482610-Mice,
pubmed-meshheading:12482610-Molecular Sequence Data,
pubmed-meshheading:12482610-Nerve Tissue Proteins,
pubmed-meshheading:12482610-Neurons,
pubmed-meshheading:12482610-PC12 Cells,
pubmed-meshheading:12482610-Peptides,
pubmed-meshheading:12482610-Phosphoproteins,
pubmed-meshheading:12482610-Phosphorylation,
pubmed-meshheading:12482610-Precipitin Tests,
pubmed-meshheading:12482610-Protein Structure, Tertiary,
pubmed-meshheading:12482610-Protein-Serine-Threonine Kinases,
pubmed-meshheading:12482610-Rats,
pubmed-meshheading:12482610-Signal Transduction,
pubmed-meshheading:12482610-Transfection,
pubmed-meshheading:12482610-Tumor Cells, Cultured,
pubmed-meshheading:12482610-rho-Associated Kinases,
pubmed-meshheading:12482610-rhoA GTP-Binding Protein
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pubmed:year |
2002
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pubmed:articleTitle |
p80 ROKalpha binding protein is a novel splice variant of CRMP-1 which associates with CRMP-2 and modulates RhoA-induced neuronal morphology.
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pubmed:affiliation |
Glaxo-IMCB Group, Institute of Molecular and Cell Biology, 30 Medical Drive, 117609, Singapore. mcbthoml@imcb.nus.edu.sg
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pubmed:publicationType |
Journal Article
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