Linked Life Data

12763024

Source:http://linkedlifedata.com/resource/pubmed/id/12763024

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-5-23
pubmed:abstractText
The Drosophila non-claret disjunctional (Ncd) kinesin-like protein is required for spindle assembly in oocytes and spindle maintenance in early embryos. Through the action of ATP-dependent microtubule (MT)-binding sites in the head and ATP-independent MT-binding sites in the tail, Ncd may bundle and, perhaps, slide MTs relative to each other. Our previous work on the MT-binding site of the Ncd tail domain demonstrated that this site, like the MT-binding sites of tau, contains basic residues flanked by proline residues and can promote MT assembly and stability. Here, we characterize the interactions of a monomeric Ncd tail protein with subtilisin-digested MTs in order to identify sites on the tubulin dimer that interact with the Ncd tail. The results provide evidence for four such binding sites per tubulin dimer and support the hypothesis that each binding site consists of a cluster of acidic residues in the C-terminal regions of alpha- and beta-tubulin.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
305
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
523-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Identification of Ncd tail domain-binding sites on the tubulin dimer.
pubmed:affiliation
Department of Biology, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061-0406, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't