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. 1994 Nov 22;91(24):11447–11451. doi: 10.1073/pnas.91.24.11447

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

P J Gotwals 1, L I Fessler 1, M Wehrli 1, R O Hynes 1
PMCID: PMC45248  PMID: 7972082

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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