Linked Life Data

10340703

Source:http://linkedlifedata.com/resource/pubmed/id/10340703

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-8-12
pubmed:abstractText
The mechanisms controlling cytokinesis during yeast budding and animal cell fission appear quite different, yet both require members of the septin protein family. Mammalian homologs of this novel family of GTPases have been identified but little is known about their properties or functions. Using an antibody specific for the mammalian septin H5, we show that this protein is expressed at distinct levels in a variety of tissues. Tissue expression levels in different tissues did not coincide with those of the only previously characterized mammalian septin Nedd5. H5, like Nedd5, localizes to the cleavage furrow in mitotic fibroblast cells but in non-mitotic cells these proteins associate with actin filaments in different ways. Nedd5 predominantly localizes with stress fibers, but only associates with central portions of the microfilament bundles. In contrast, H5 associates with the entire length of the stress fibers and the cortical actin network. Conditions that disrupt the actin cytoskeleton also disrupt the filamentous patterns of both Nedd5 and H5, resulting in a punctate cytoplasmic pattern. Cell fractionation revealed that H5 co-fractionated with actin, while Nedd5 was predominantly restricted to the membrane fraction. Co-immunoprecipitation experiments revealed that although H5 will co-precipitate with Nedd5, the precipitation is not quantitative. Taken together, these results not only show that H5 behaves like a septin, but also demonstrate that individual septin proteins have distinct properties, suggesting that they may play different roles in cytokinesis and in other stages of the cell cycle.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0886-1544
pubmed:author
pubmed:issnType
Print
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
52-62
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Characterization of the mammalian septin H5: distinct patterns of cytoskeletal and membrane association from other septin proteins.
pubmed:affiliation
The Hospital for Sick Children and Department of Biochemistry, University of Toronto, Ontario, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't