Paxillin is a focal adhesion scaffolding protein, which has been proposed to play a role in focal adhesion dynamics. We have isolated a cDNA clone of the Drosophila homologue of paxillin. Comparison of the Drosophila paxillin sequence with those of vertebrate paxillins shows strong conservation of the LIM domains and LD repeats. Using the Drosophila genomic sequence we have identified two partial curated transcripts and deduced the structure of the paxillin gene. No homologues of other members of the paxillin family such as HIC-5 or leupaxin are to be found in the Drosophila genome. Surprisingly paxillin mRNA is expressed in a restricted pattern during embryogenesis. In particular it is strongly expressed in cells and tissues undergoing cell shape changes or cell migration. Many of the sites of expression are also known to be sites of integrin function or FAK expression. The data support a role for paxillin as an adapter and/or signaling protein during developmental processes involving integrin-mediated adhesion.