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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2011-3-24
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pubmed:abstractText |
Dendritic arbors are compartments of neurons dedicated to receiving synaptic inputs. Their shape is an outcome of both the intrinsic genetic program and environmental signals. The microtubules and actin cytoskeleton are both crucial for proper dendritic morphology, but how they interact is unclear. The present study demonstrates that microtubule plus-end tracking protein CLIP-170 and actin-binding protein IQGAP1 regulate dendrite morphology of rat neurons by coordinating the interaction between microtubules and the actin cytoskeleton. Moreover, we show that mTOR kinase interacts with CLIP-170 and is needed for efficient formation of a protein complex containing CLIP-170 and IQGAP1. Dynamic microtubules, CLIP-170, and IQGAP1 are required for proper dendritic arbor morphology and PI3K-mTOR-induced increase in dendritic arbor complexity. Moreover, CLIP-170 and IQGAP1 knockdown modulates dendritic arbor growth via regulation of the actin cytoskeleton. We postulate that mTOR controls dendritic arbor morphology by enhancing cross talk between dynamic microtubules and actin through CLIP-170 and IQGAP1.
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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/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/IQ motif containing GTPase...,
http://linkedlifedata.com/resource/pubmed/chemical/Indicators and Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/TOR Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/cytoplasmic linker protein 170,
http://linkedlifedata.com/resource/pubmed/chemical/ras GTPase-Activating Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1529-2401
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
23
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pubmed:volume |
31
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4555-68
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pubmed:meshHeading |
pubmed-meshheading:21430156-Actins,
pubmed-meshheading:21430156-Animals,
pubmed-meshheading:21430156-Biotinylation,
pubmed-meshheading:21430156-Cells, Cultured,
pubmed-meshheading:21430156-Cytoskeleton,
pubmed-meshheading:21430156-DNA,
pubmed-meshheading:21430156-Dendrites,
pubmed-meshheading:21430156-Fluorescent Antibody Technique,
pubmed-meshheading:21430156-Green Fluorescent Proteins,
pubmed-meshheading:21430156-Hippocampus,
pubmed-meshheading:21430156-Image Processing, Computer-Assisted,
pubmed-meshheading:21430156-Indicators and Reagents,
pubmed-meshheading:21430156-Microtubule-Associated Proteins,
pubmed-meshheading:21430156-Microtubules,
pubmed-meshheading:21430156-Neoplasm Proteins,
pubmed-meshheading:21430156-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:21430156-Phosphorylation,
pubmed-meshheading:21430156-Rats,
pubmed-meshheading:21430156-TOR Serine-Threonine Kinases,
pubmed-meshheading:21430156-Transfection,
pubmed-meshheading:21430156-ras GTPase-Activating Proteins
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pubmed:year |
2011
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pubmed:articleTitle |
CLIP-170 and IQGAP1 cooperatively regulate dendrite morphology.
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pubmed:affiliation |
Laboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell Biology, 02-109 Warsaw, Poland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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