rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2002-7-2
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pubmed:abstractText |
Sensory (hair) cells of the inner ear contain two specialized areas of membrane delivery. The first, located at the cell base, is the afferent synapse where rapid delivery of synaptic vesicles is required to convey information about auditory signals with exceedingly high temporal precision. The second area is at the apex. To accommodate the continuous movement of stereocilia and facilitate their repair, recycling of membrane components is required. Intense vesicular traffic is restricted to a narrow band of cytoplasm around the cuticular plate, which anchors stereocilia. Our previous analyses showed that SNARE proteins (syntaxin 1A/SNAP25/VAMP1) are concentrated at both poles of hair cells, consistent with their involvement in membrane delivery at both locations. To investigate further the molecules involved in membrane delivery at these two sites, we constructed a two-hybrid library of the organ of Corti and probed it with syntaxin 1A. Here we report the cloning of a novel syntaxin-binding protein that is concentrated in a previously uncharacterized organelle at the apex of inner hair cells.
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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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Indicators and Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Qa-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/STX1A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Syntaxin 1
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1044-7431
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pubmed:author |
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pubmed:copyrightInfo |
(c) 2002 Elsevier Science (USA).
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pubmed:issnType |
Print
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
343-53
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:12093165-Animals,
pubmed-meshheading:12093165-Base Sequence,
pubmed-meshheading:12093165-Carrier Proteins,
pubmed-meshheading:12093165-Cell Compartmentation,
pubmed-meshheading:12093165-Cilia,
pubmed-meshheading:12093165-Cloning, Molecular,
pubmed-meshheading:12093165-DNA, Complementary,
pubmed-meshheading:12093165-Endosomes,
pubmed-meshheading:12093165-Green Fluorescent Proteins,
pubmed-meshheading:12093165-Guinea Pigs,
pubmed-meshheading:12093165-Hair Cells, Auditory, Inner,
pubmed-meshheading:12093165-HeLa Cells,
pubmed-meshheading:12093165-Hearing,
pubmed-meshheading:12093165-Humans,
pubmed-meshheading:12093165-Immunohistochemistry,
pubmed-meshheading:12093165-Indicators and Reagents,
pubmed-meshheading:12093165-Luminescent Proteins,
pubmed-meshheading:12093165-Male,
pubmed-meshheading:12093165-Membrane Proteins,
pubmed-meshheading:12093165-Molecular Sequence Data,
pubmed-meshheading:12093165-Nerve Tissue Proteins,
pubmed-meshheading:12093165-Organelles,
pubmed-meshheading:12093165-Protein Transport,
pubmed-meshheading:12093165-Qa-SNARE Proteins,
pubmed-meshheading:12093165-Sequence Homology, Amino Acid,
pubmed-meshheading:12093165-Synaptic Membranes,
pubmed-meshheading:12093165-Syntaxin 1
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pubmed:year |
2002
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pubmed:articleTitle |
Ocsyn, a novel syntaxin-interacting protein enriched in the subapical region of inner hair cells.
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pubmed:affiliation |
Laboratory of Neurochemistry, National Institute on Deafness and Other Communication Disorders, Bethesda, Maryland 20892, USA.
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pubmed:publicationType |
Journal Article
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