ArticleMolecular biology of the cell2002
Disruption of C-terminal cytoplasmic domain of betaPS integrin subunit has dominant negative properties in developing Drosophila.
Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- Drosophila vinculin is more harmful when hyperactive than absent, and can circumvent integrin to form adhesion complexes.Journal of cell science · 2016Article
- Article
- Misshapen decreases integrin levels to promote epithelial motility and planar polarity in Drosophila.The Journal of cell biology · 2013Article
- Matrix adhesion polarizes heart progenitor induction in the invertebrate chordate Ciona intestinalis.Development (Cambridge, England) · 2013Article
- Identification of integrin beta subunit mutations that alter affinity for extracellular matrix ligand.The Journal of biological chemistry · 2011Article
- Fibroblast growth factor signalling controls successive cell behaviours during mesoderm layer formation in Drosophila.Development (Cambridge, England) · 2011Article
- Noninvasive measurements of integrin microclustering under altered membrane cholesterol levels.Biophysical journal · 2010Article
- Tenectin is a novel alphaPS2betaPS integrin ligand required for wing morphogenesis and male genital looping in Drosophila.Developmental biology · 2010Article
- Analysis of conserved residues in the betapat-3 cytoplasmic tail reveals important functions of integrin in multiple tissues.Developmental dynamics : an official publication of the American Association of Anatomists · 2010Article
- Integrin alpha chains exhibit distinct temporal and spatial localization patterns in epithelial cells of the Drosophila ovary.Developmental dynamics : an official publication of the American Association of Anatomists · 2008Article
- Differences in regulation of Drosophila and vertebrate integrin affinity by talin.Molecular biology of the cell · 2008Article
- Nuclear localization of the ERK MAP kinase mediated by Drosophila alphaPS2betaPS integrin and importin-7.Molecular biology of the cell · 2007Article
- Mutations in the Drosophila alphaPS2 integrin subunit uncover new features of adhesion site assembly.Developmental biology · 2007Article
- General in vivo assay for the study of integrin cell membrane receptor microclustering.Analytical chemistry · 2007Article
- Identification of integrin beta subunit mutations that alter heterodimer function in situ.Molecular biology of the cell · 2004Article
- Genetic interaction between integrins and moleskin, a gene encoding a Drosophila homolog of importin-7.Genetics · 2002Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
We have analyzed a set of new and existing strong mutations in the myospheroid gene, which encodes the betaPS integrin subunit of Drosophila. In addition to missense and other null mutations, three mutants behave as antimorphic alleles, indicative of dominant negative properties. Unlike null alleles, the three antimorphic mutants are synthetically lethal in double heterozygotes with an inflated (alphaPS2) null allele, and they fail to complement very weak, otherwise viable alleles of myospheroid. Two of the antimorphs result from identical splice site lesions, which create a frameshift in the C-terminal half of the cytoplasmic domain of betaPS. The third antimorphic mutation is caused by a stop codon just before the cytoplasmic splice site. These mutant betaPS proteins can support cell spreading in culture, especially under conditions that appear to promote integrin activation. Analyses of developing animals indicate that the dominant negative properties are not a result of inefficient surface expression, or simple competition between functional and nonfunctional proteins. These data indicate that mutations disrupting the C-terminal cytoplasmic domain of integrin beta subunits can have dominant negative effects in situ, at normal levels of expression, and that this property does not necessarily depend on a specific new protein sequence or structure. The results are discussed with respect to similar vertebrate beta subunit cytoplasmic mutations.
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