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J Biol Chem, Vol. 274, Issue 41, 29196-29201, October 8, 1999

Cloning and Characterization of Dfak56, a Homolog of Focal Adhesion Kinase, in Drosophila melanogaster

Jiro Fujimoto, Kazunobu Sawamoto^§, Masataka Okabe^§, Yasumitsu Takagi, Tohru Tezuka, Shingo Yoshikawa, Haruko Ryo^§§, Hideyuki Okano^§, and Tadashi Yamamoto

From the  Department of Oncology, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan, the ^§ Division of Neuroanatomy, Department of Neuroscience, Biomedical Research Center, Osaka University Graduate School of Medicine and Core Research for Evolutional Science and Technology, Japan Science and Technology Corporation, Osaka 565-0871, Japan, the ^§§ Department of Radiation Biology and Medical Genetics, Osaka University Graduate School of Medicine, Osaka 565-0871, Japan, the  Hirohashi Cell Configuration Project, Exploratory Research for Advanced Technology, Japan Science and Technology Corporation, Tsukuba 300-2635, Japan, and the  Department of Molecular Neurobiology, Institute of Basic Medical Sciences, University of Tsukuba, Tsukuba 305-0006, Japan

The focal adhesion kinase (FAK) protein-tyrosine kinase plays important roles in cell adhesion in vertebrates. Using polymerase chain reaction-based cloning strategy, we cloned a Drosophila gene that is homologous to the vertebrate FAK family of protein-tyrosine kinases. We designated this gene Dfak56 and characterized its gene product. The overall protein structure and deduced amino acid sequence of Dfak56 show significant similarity to those of FAK and PYK2. Dfak56 has in vitro autophosphorylation activity at tyrosine residues. Expression of the Dfak56 mRNA and the protein was observed in the central nervous system and the muscle-epidermis attachment site in the embryo, where Drosophila position-specific integrins are localized. The results suggest that like FAK in vertebrates, Dfak56 functions downstream of integrins. Dfak56 was tyrosine-phosphorylated upon integrin-dependent attachment of the cell to the extracellular matrix. We conclude that the Dfak56 tyrosine kinase is involved in integrin-mediated cell adhesion signaling and thus is a functional homolog of vertebrate FAK.

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