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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1991-4-11
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pubmed:abstractText |
We find that half of the pertussis toxin-sensitive guanine nucleotide-binding protein (G protein) in the squid (Loligo pealei) giant axon is cytoplasmic and that this species of G protein is intermediate in size between the two forms present in axolemma. This G protein is transported toward synaptic terminals at 44 mm/day. Moreover, these data are consistent with there being two additional steps leading to the maturation of G proteins: (i) association with and transport on intracellular organelles and (ii) modification at the time of transfer to the plasmalemma resulting in a molecular weight shift. Since the other two components of G protein-mediated signal transduction pathways, receptors and effector enzymes, are known to be delivered to the synaptic terminals by fast axonal transport, our findings introduce the possibility that these three macromolecules are assembled as a complex in the cell body and delivered together to the plasma membrane of the axon and synaptic terminals.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-2158629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-2419517,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-2536957,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-2913212,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-3079909,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-3080332,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-3113327,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-3115830,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-3134354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-3151168,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-3919024,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-4100673,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-4105450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-49355,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-6157104,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-6158097,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-6159657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-6178165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-6178808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-69682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-7062032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-81302,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705707-89886
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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 |
Mar
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1775-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:1705707-Adenosine Diphosphate Ribose,
pubmed-meshheading:1705707-Animals,
pubmed-meshheading:1705707-Axonal Transport,
pubmed-meshheading:1705707-Axons,
pubmed-meshheading:1705707-Decapodiformes,
pubmed-meshheading:1705707-GTP-Binding Proteins,
pubmed-meshheading:1705707-Kinetics,
pubmed-meshheading:1705707-Models, Neurological,
pubmed-meshheading:1705707-NAD,
pubmed-meshheading:1705707-Pertussis Toxin,
pubmed-meshheading:1705707-Synapses,
pubmed-meshheading:1705707-Temperature,
pubmed-meshheading:1705707-Virulence Factors, Bordetella
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pubmed:year |
1991
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pubmed:articleTitle |
Pertussis toxin-sensitive G proteins are transported toward synaptic terminals by fast axonal transport.
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pubmed:affiliation |
Marine Biological Laboratory, Woods Hole, MA 02543.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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