Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2002-3-5
pubmed:abstractText
Many cellular components are transported using a combination of the actin- and microtubule-based transport systems. However, how these two systems work together to allow well-regulated transport is not clearly understood. We investigate this question in the Xenopus melanophore model system, where three motors, kinesin II, cytoplasmic dynein, and myosin V, drive aggregation or dispersion of pigment organelles called melanosomes. During dispersion, myosin V functions as a "molecular ratchet" to increase outward transport by selectively terminating dynein-driven minus end runs. We show that there is a continual tug-of-war between the actin and microtubule transport systems, but the microtubule motors kinesin II and dynein are likely coordinated. Finally, we find that the transition from dispersion to aggregation increases dynein-mediated motion, decreases myosin V--mediated motion, and does not change kinesin II--dependent motion. Down-regulation of myosin V contributes to aggregation by impairing its ability to effectively compete with movement along microtubules.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-10477758, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-10491390, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-10611957, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-10704445, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-11018061, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-11509731, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-1570018, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-2165596, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-3915782, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-7755993, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-8202156, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-8232586, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-8522592, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-9045707, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-9108044, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-9133672, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-9144193, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-9443916, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-9443917, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-9491895, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-9508772, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-9712266, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-9751895, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-9763516, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-9852146, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-9852150, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-9864363, http://linkedlifedata.com/resource/pubmed/commentcorrection/11864991-9930703
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Dyneins, http://linkedlifedata.com/resource/pubmed/chemical/Kinesin, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Motor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Monophenol Monooxygenase, http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Myosin Type V, http://linkedlifedata.com/resource/pubmed/chemical/Phenylthiourea, http://linkedlifedata.com/resource/pubmed/chemical/Pigments, Biological, http://linkedlifedata.com/resource/pubmed/chemical/XKLP3 protein, Xenopus, http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins, http://linkedlifedata.com/resource/pubmed/chemical/kinesin-II
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9525
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
156
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
855-65
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Interactions and regulation of molecular motors in Xenopus melanophores.
pubmed:affiliation
Department of Developmental and Cell Biology, University of California, Irvine, Irvine, CA 92697.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't