Mutations in the Drosophila αPS2 integrin subunit uncover new features of adhesion site assembly

Danelle Devenport, Thomas A. Bunch, James W. Bloor, Danny L. Brower, Nicholas H. Brown

Research output: Contribution to journalArticle

22 Scopus citations

Abstract

The Drosophila αPS2βPS integrin is required for diverse development events, including muscle attachment. We characterized six unusual mutations in the αPS2 gene that cause a subset of the null phenotype. One mutation changes a residue in αPS2 that is equivalent to the residue in αV that contacts the arginine of RGD. This change severely reduced αPS2βPS affinity for soluble ligand, abolished the ability of the integrin to recruit laminin to muscle attachment sites in the embryo and caused detachment of integrins and talin from the ECM. Three mutations that alter different parts of the αPS2 β-propeller, plus a fourth that eliminated a late phase of αPS2 expression, all led to a strong decrease in αPS2βPS at muscle ends, but, surprisingly, normal levels of talin were recruited. Thus, although talin recruitment requires αPS2βPS, talin levels are not simply specified by the amount of integrin at the adhesive junction. These mutations caused detachment of talin and actin from integrins, suggesting that the integrin-talin link is weaker than the ECM-integrin link.

Original languageEnglish (US)
Pages (from-to)294-308
Number of pages15
JournalDevelopmental biology
Volume308
Issue number2
DOIs
StatePublished - Aug 15 2007
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Developmental Biology
  • Cell Biology

Keywords

  • ECM
  • Integrins
  • Ligand-binding site
  • Muscle development

Fingerprint Dive into the research topics of 'Mutations in the Drosophila αPS2 integrin subunit uncover new features of adhesion site assembly'. Together they form a unique fingerprint.

  • Cite this