Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2001-1-17
pubmed:abstractText
In budding yeast, the mitotic spindle moves into the neck between the mother and bud via dynein-dependent sliding of cytoplasmic microtubules along the cortex of the bud. How dynein and microtubules interact with the cortex is unknown. We found that cells lacking Num1p failed to exhibit dynein-dependent microtubule sliding in the bud, resulting in defective mitotic spindle movement and nuclear segregation. Num1p localized to the bud cortex, and that localization was independent of microtubules, dynein, or dynactin. These data are consistent with Num1p being an essential element of the cortical attachment mechanism for dynein-dependent sliding of microtubules in the bud.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-10477756, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-10531032, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-10607597, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-10712505, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-10811827, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-11056548, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-1400581, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-1745235, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-7490278, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-7622568, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-8069915, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-8603918, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-9201714, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-9228009, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-9281575, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-9281581, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-9281582, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-9348543, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-9362516, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-9398684, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-9442113, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-9646876, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-9658168, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-9693366, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-9700152, http://linkedlifedata.com/resource/pubmed/commentcorrection/11121446-9744880
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Actins, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Dyneins, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/KAR9 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/KIP3 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Kinesin, http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins, http://linkedlifedata.com/resource/pubmed/chemical/NUM1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9525
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
151
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1337-44
pubmed:dateRevised
2010-8-17
pubmed:meshHeading
pubmed-meshheading:11121446-Actins, pubmed-meshheading:11121446-Calcium-Binding Proteins, pubmed-meshheading:11121446-Cell Compartmentation, pubmed-meshheading:11121446-Chromosome Segregation, pubmed-meshheading:11121446-Cytoskeletal Proteins, pubmed-meshheading:11121446-Dyneins, pubmed-meshheading:11121446-Fungal Proteins, pubmed-meshheading:11121446-Kinesin, pubmed-meshheading:11121446-Microscopy, pubmed-meshheading:11121446-Microtubule-Associated Proteins, pubmed-meshheading:11121446-Microtubules, pubmed-meshheading:11121446-Mitosis, pubmed-meshheading:11121446-Mitotic Spindle Apparatus, pubmed-meshheading:11121446-Movement, pubmed-meshheading:11121446-Nuclear Proteins, pubmed-meshheading:11121446-Phenotype, pubmed-meshheading:11121446-Saccharomyces cerevisiae Proteins, pubmed-meshheading:11121446-Saccharomycetales
pubmed:year
2000
pubmed:articleTitle
The cortical protein Num1p is essential for dynein-dependent interactions of microtubules with the cortex.
pubmed:affiliation
Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.