Linked Life Data

15766794

Source:http://linkedlifedata.com/resource/pubmed/id/15766794

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2005-3-15
pubmed:abstractText
Loss of function of Cin8p (a yeast kinesin-like motor protein) in the absence of either Kip1p (a motor of the same family) or Dyn1p (the dynein heavy chain) is lethal. We report that cin8 mutants are sensitive to the cell wall disrupting agents calcofluor white and SDS. Conditionally lethal double mutants containing the temperature sensitive allele cin8-3 in a background deletion of either kip1 or dyn1 grew normally at the restrictive temperature when osmolytes such as sorbitol were added to the medium. Sorbitol could not alleviate the sensitivity of cin8 mutants to calcofluor and SDS. However, it rendered cells more resistant to the microtubule depolymerizing drugs benomyl and thiabendazole (TBZ). Our findings reveal a novel interaction between mitotic motor proteins and the cell wall and suggest that the induction of signaling pathways aimed at maintaining the cell wall suppresses phenotypes of mutations in microtubule-associated motor proteins through stabilization of microtubules.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0378-1097
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
244
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
379-83
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Mutations in the yeast kinesin-like Cin8p are alleviated by osmotic support.
pubmed:affiliation
Department of Biology, The City University of New York, Brooklyn College, 2900 Bedford Avenue, Brooklyn, NY 11210, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural