Linked Life Data

19879140

Source:http://linkedlifedata.com/resource/pubmed/id/19879140

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
2009-11-20
pubmed:abstractText
Microtubule (MT) arrays are mechanistic effectors of polarity specification and cell division. Linear bundles in which MTs are bridged laterally are dynamically assembled in systems ranging from differentiated metazoan cells to fungi in a process that remains poorly understood. Often, bundled MTs slide with respect to each other via molecular motors. In interphase cells of the fission yeast Schizosaccharomyces pombe, MT nucleation frequently occurs at preexisting arrays. As the nascent MT lengthens, stable antiparallel MT overlaps are thought to form through competition between motion of the minus-end-directed kinesin Klp2p and braking force exerted by the accumulating lateral crosslinker Ase1p. Here we show that Mia1p/Alp7p, a transforming acidic coiled-coil (TACC) protein, functions as a length-independent MT crosslinker. In cells lacking Mia1p MT-bundling activity, linear arrays frequently disassemble, accompanied by a marked increase in Ase1p off rate and erratic motion of sliding MTs. We propose that the combined action of lateral length-dependent (Ase1p) and terminal length-independent (Mia1p) crosslinkers is crucial for robust assembly and stability of linear MT arrays. Such use of qualitatively distinct crosslinking mechanisms in tandem may point to a general design principle in the engineering of stable cytoskeletal assemblies.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1879-0445
pubmed:author
pubmed:issnType
Electronic
pubmed:day
17
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1861-8
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
The fission yeast TACC protein Mia1p stabilizes microtubule arrays by length-independent crosslinking.
pubmed:affiliation
Temasek Life Sciences Laboratory, 1 Research Link, Singapore 117604, Singapore.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't