Source:http://linkedlifedata.com/resource/pubmed/id/21385318
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
2011-5-4
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pubmed:abstractText |
The kinase noncatalytic C-lobe domain (KIND) is a putative protein-protein interaction module. Four KIND-containing proteins, Spir-2 (actin-nuclear factor), PTPN13 (protein tyrosine phosphatase), FRMPD2 (scaffold protein) and very-KIND (v-KIND) (brain-specific Ras guanine nucleotide exchange factor), have been identified to date. Uniquely, v-KIND has two KINDs (i.e. KIND1 and KIND2), whereas the other three proteins have only one. The functional role of KIND, however, remains unclear. We previously demonstrated that v-KIND interacts with the high-molecular weight microtubule-associated protein 2 (MAP2), a dendritic microtubule-associated protein, leading to negative regulation of neuronal dendrite growth. In the present study, we analyzed the structure-function relationships of the v-KIND-MAP2 interaction by generating a series of mutant constructs. The interaction with endogenous MAP2 in mouse cerebellar granule cells was specific to v-KIND KIND2, but not KIND1, and was not observed for the KINDs from other KIND-containing proteins. The binding core modules critical for the v-KIND-MAP2 interaction were defined within 32 residues of the mouse v-KIND KIND2 and 43 residues of the mouse MAP2 central domain. Three Leu residues at amino acid positions 461, 474 and 477 in the MAP2-binding core module of KIND2 contributed to the interaction. The MAP2-binding core module itself promoted dendrite branching as a dominant-negative regulator of v-KIND in hippocampal neurons. The results reported in the present study demonstrate the structural and functional determinant underlying the v-KIND-MAP2 interaction that controls dendrite arborization patterns.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Leucine,
http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mtap2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Ptpn13 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/ras Guanine Nucleotide Exchange...
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1742-4658
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pubmed:author | |
pubmed:copyrightInfo |
© 2011 The Authors Journal compilation © 2011 FEBS.
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pubmed:issnType |
Electronic
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1651-61
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pubmed:meshHeading |
pubmed-meshheading:21385318-Amino Acid Sequence,
pubmed-meshheading:21385318-Animals,
pubmed-meshheading:21385318-Chickens,
pubmed-meshheading:21385318-Dendrites,
pubmed-meshheading:21385318-Hippocampus,
pubmed-meshheading:21385318-Humans,
pubmed-meshheading:21385318-Leucine,
pubmed-meshheading:21385318-Mice,
pubmed-meshheading:21385318-Microtubule-Associated Proteins,
pubmed-meshheading:21385318-Neurons,
pubmed-meshheading:21385318-Protein Interaction Mapping,
pubmed-meshheading:21385318-Protein Structure, Tertiary,
pubmed-meshheading:21385318-Protein Tyrosine Phosphatase, Non-Receptor Type 13,
pubmed-meshheading:21385318-ras Guanine Nucleotide Exchange Factors
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pubmed:year |
2011
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pubmed:articleTitle |
Interaction between very-KIND Ras guanine exchange factor and microtubule-associated protein 2, and its role in dendrite growth--structure and function of the second kinase noncatalytic C-lobe domain.
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pubmed:affiliation |
Laboratory for Molecular Neurogenesis, RIKEN Brain Science Institute, Saitama, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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