Drosophila PS1 integrin is a laminin receptor and differs in ligand specificity from PS2

Philip J. Gotwals, Liselotte I. Fessler, Marcel Wehrli, Richard O. Hynes

Research output: Contribution to journalArticle

67 Citations (Scopus)

Abstract

We have expressed Drosophila position-specific (PS) integrins on the surfaces of Schneider S2 cells and tested for adhesion and spreading on various matrix molecules. We report that PS1 integrin is a laminin receptor and that PS1 and PS2 integrins promote cell spreading on two different Drosophila extracellular matrix molecules, laminin and tiggrin, respectively. The differing ligand specificities of these two integrins, combined with data on the in vivo expression patterns of the integrins and their ligands, lead to a model for the structure of integrin-dependent attachments in the pupal wings and embryonic muscles of Drosophila.

Original languageEnglish (US)
Pages (from-to)11447-11451
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume91
Issue number24
DOIs
StatePublished - Nov 22 1994
Externally publishedYes

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Laminin Receptors
Integrins
Drosophila
Ligands
Laminin
Cell Adhesion
Extracellular Matrix
Muscles

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Drosophila PS1 integrin is a laminin receptor and differs in ligand specificity from PS2. / Gotwals, Philip J.; Fessler, Liselotte I.; Wehrli, Marcel; Hynes, Richard O.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 91, No. 24, 22.11.1994, p. 11447-11451.

Research output: Contribution to journalArticle

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