Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2008-7-21
pubmed:abstractText
Fission yeast expresses two kinesin 8s, klp5+ and klp6+, which are important for diverse cellular functions: mitosis, meiosis, and the maintenance of normal cell morphology. During vegetative growth these motors display complex localization patterns, moving from the cytoplasm during interphase to the kinetochores in early mitosis, the interpolar spindle in anaphase B, and then back into the cytoplasm. We have expressed GFP-tagged alleles of domains from these motors, seeking the signals required for their localizations. The tail of Klp5p localized to the interphase nucleus, more specifically to telomeres. Addition of the neck re-directed this fragment to microtubules in the cytoplasm. Klp6-tail and the neck-tail domains of both motors localized at microtubule ends. Klp6-neck-tail localized to the spindle in early mitosis but to the pole-proximal ends of the spindle in anaphase B. The Klp5-motor and motor-neck localized to microtubules, often causing them to bundle. Over-expression of Klp6-motor or motor-neck resulted in shorter microtubules. These localization patterns were no different when constructs were expressed in strains lacking either or both of the endogenous, full-length proteins. Our results indicate that the localization signals for these kinesins are not derived from simple amino acid sequences but from complex interactions among multiple domains of each motor.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-10398680, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-10607565, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-10611960, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-11063680, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-11739790, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-11870212, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-11967147, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-12426374, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-12894167, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-12975346, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-13679514, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-14573463, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-1503765, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-15189985, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-15252134, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-15479732, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-15665379, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-15843429, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-15928044, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-16079915, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-16481395, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-16906145, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-16906148, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-17184986, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-2005825, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-3198697, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-7744953, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-8332516, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-8416984, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-9034194, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-9060472, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-9281582, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-9348288, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-9693366, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-9763447, http://linkedlifedata.com/resource/pubmed/commentcorrection/18553361-9852950
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1097-0169
pubmed:author
pubmed:copyrightInfo
(c) 2008 Wiley-Liss, Inc.
pubmed:issnType
Electronic
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
626-40
pubmed:dateRevised
2011-9-26
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Novel interactions of fission yeast kinesin 8 revealed through in vivo expression of truncation alleles.
pubmed:affiliation
Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, Colorado 80309-0347, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural