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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
16
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pubmed:dateCreated |
2005-8-17
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pubmed:abstractText |
alpha-RIMs and Munc13s are active zone proteins that control priming of synaptic vesicles to a readily releasable state, and interact with each other via their N-terminal sequences. The alpha-RIM N-terminal sequence also binds to Rab3s (small synaptic vesicle GTPases), an interaction that regulates presynaptic plasticity. We now demonstrate that alpha-RIMs contain adjacent but separate Munc13- and Rab3-binding sites, allowing formation of a tripartite Rab3/RIM/Munc13 complex. Munc13 binding is mediated by the alpha-RIM zinc-finger domain. Elucidation of the three-dimensional structure of this domain by NMR spectroscopy facilitated the design of a mutation that abolishes alpha-RIM/Munc13 binding. Selective disruption of this interaction in the calyx of Held synapse decreased the size of the readily releasable vesicle pool. Our data suggest that the ternary Rab3/RIM/Munc13 interaction approximates synaptic vesicles to the priming machinery, providing a substrate for presynaptic plasticity. The modular architecture of alpha-RIMs, with nested binding sites for Rab3 and other targets, may be a general feature of Rab effectors that share homology with the alpha-RIM N-terminal sequence.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-10025402,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-10440375,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-10449403,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-10504306,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-10526333,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-10748113,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-11031229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-11134008,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-11160425,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-11252952,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-11343654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-11431472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-11460165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-11559854,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-11754842,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-11792326,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-11797009,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-11797010,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-12070347,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-12154365,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-12578829,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-12620390,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-12628170,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-15066271,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-15207234,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-15269275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-15330860,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-15713878,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-1655810,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-2062851,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-7559667,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-8999968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-9252190,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-9252191,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16052212-9267032
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2839-50
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16052212-Amino Acid Sequence,
pubmed-meshheading:16052212-Binding Sites,
pubmed-meshheading:16052212-Calorimetry,
pubmed-meshheading:16052212-Electrophysiology,
pubmed-meshheading:16052212-Escherichia coli,
pubmed-meshheading:16052212-GTP-Binding Proteins,
pubmed-meshheading:16052212-Glutathione Transferase,
pubmed-meshheading:16052212-Humans,
pubmed-meshheading:16052212-Models, Molecular,
pubmed-meshheading:16052212-Molecular Sequence Data,
pubmed-meshheading:16052212-Multiprotein Complexes,
pubmed-meshheading:16052212-Mutagenesis,
pubmed-meshheading:16052212-Nerve Tissue Proteins,
pubmed-meshheading:16052212-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:16052212-Sequence Alignment,
pubmed-meshheading:16052212-Synaptic Vesicles,
pubmed-meshheading:16052212-rab3 GTP-Binding Proteins
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pubmed:year |
2005
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pubmed:articleTitle |
A Munc13/RIM/Rab3 tripartite complex: from priming to plasticity?
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pubmed:affiliation |
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390-8816, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, N.I.H., Extramural
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