Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9-10
pubmed:dateCreated
2008-9-9
pubmed:abstractText
Lasp family proteins contain an amino-terminal LIM domain, two actin-binding nebulin repeats and a carboxyl-terminal SH3 domain. Vertebrate Lasp-1 localizes to focal adhesions and the leading edge of migrating cells, and is required for cell migration. To assess the in vivo function of Lasp, we generated a null mutant in Drosophila Lasp. Lasp(1) is homozygous viable, but male sterile. In Lasp mutants the stem cell niche is no longer anchored to the apical tip of the testis, and actin cone migration is perturbed resulting in improper spermatid individualization. Hub cell mislocalization can by phenocopied by expressing Lasp or betaPS integrin RNAi transgenes in somatic cells, and Lasp genetically interacts with betaPS integrin, demonstrating that Lasp functions together with integrins in hub cells to anchor the stem cell niche. Finally, we show that the stem cell niche is maintained even if it is not properly localized.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1872-6356
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
125
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
768-76
pubmed:meshHeading
pubmed:articleTitle
Lasp anchors the Drosophila male stem cell niche and mediates spermatid individualization.
pubmed:affiliation
Department of Biology, McGill University, 1205 Dr. Penfield Avenue, Montreal, QC, Canada H3A 1B1.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't