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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6371
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pubmed:dateCreated |
1992-5-28
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pubmed:abstractText |
Studies of organelle movement in axoplasm extruded from the squid giant axon have led to the basic discoveries of microtubule-dependent organelle motility and the characterization of the microtubule-based motor proteins kinesin and cytoplasmic dynein. Rapid organelle movement in higher animal cells, especially in neurons, is considered to be microtubule-based. The role of actin filaments, which are also abundant in axonal cytoplasm, has remained unclear. The inhibition of organelle movement in axoplasm by actin-binding proteins such as DNase I, gelsolin and synapsin I has been attributed to their ability to disorganize the microtubule domains where most of the actin-filaments are located. Here we provide evidence of a new type of organelle movement in squid axoplasm which is independent of both microtubules and microtubule-based motors. This movement is ATP-dependent, unidirectional, actin-dependent, and probably generated by a myosin-like motor. These results demonstrate that an actomyosin-like mechanism can be directly involved in the generation of rapid organelle transport in nerve cells.
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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/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Adenylyl Imidodiphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Apyrase,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochalasin B,
http://linkedlifedata.com/resource/pubmed/chemical/Edetic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Egtazic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Hexokinase,
http://linkedlifedata.com/resource/pubmed/chemical/Nocodazole,
http://linkedlifedata.com/resource/pubmed/chemical/Vanadates
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0028-0836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
356
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
722-5
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:1570018-Actin Cytoskeleton,
pubmed-meshheading:1570018-Actins,
pubmed-meshheading:1570018-Adenylyl Imidodiphosphate,
pubmed-meshheading:1570018-Animals,
pubmed-meshheading:1570018-Apyrase,
pubmed-meshheading:1570018-Axons,
pubmed-meshheading:1570018-Cytochalasin B,
pubmed-meshheading:1570018-Decapodiformes,
pubmed-meshheading:1570018-Edetic Acid,
pubmed-meshheading:1570018-Egtazic Acid,
pubmed-meshheading:1570018-Hexokinase,
pubmed-meshheading:1570018-Movement,
pubmed-meshheading:1570018-Nocodazole,
pubmed-meshheading:1570018-Organelles,
pubmed-meshheading:1570018-Vanadates
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pubmed:year |
1992
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pubmed:articleTitle |
Actin-dependent organelle movement in squid axoplasm.
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pubmed:affiliation |
Marine Biological Laboratory, Woods Hole, Massachusetts 02543.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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