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First published online 3 November 2004
doi: 10.1242/dev.01462

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Focal adhesion kinase is not required for integrin function or viability in Drosophila

Caroline Grabbe^1,*, Christos G. Zervas^2,*,, Tony Hunter³, Nicholas H. Brown² and Ruth H. Palmer^1,

¹ Umeå Center for Molecular Pathogenesis, Building 6L, Umeå University, Umeå, 901 87, Sweden
² The Wellcome Trust/Cancer Research UK, Gurdon Institute and Department of Anatomy, University of Cambridge, Tennis Court Road, Cambridge CB2 1QR, UK
³ The Salk Institute, Molecular and Cell Biology Laboratory, 10010 North Torrey Pines Road, La Jolla, CA 92037-1099, USA

Author for correspondence (e-mail: ruth.palmer{at}ucmp.umu.se)

Accepted 14 September 2004

The mammalian focal adhesion kinase (FAK) family of non-receptor protein-tyrosine kinases has been implicated in controlling a multitude of cellular responses to the engagement of cell-surface integrins and G-protein-coupled receptors. The high level of sequence conservation between the mammalian proteins and the Drosophila homologue of FAK, Fak56, suggested that it would have similar functions. However, we show here that Drosophila Fak56 is not essential for integrin functions in adhesion, migration or signaling in vivo. Furthermore, animals lacking Fak56 are viable and fertile, demonstrating that Fak56 is not essential for other developmental or physiological functions. Despite this, overexpressed Fak56 is a potent inhibitor of integrins binding to the extracellular matrix, suggesting that Fak56 may play a subtle role in the negative regulation of integrin adhesion.

Key words: Drosophila, FAK, Integrins, Signal transduction

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