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

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 aDrosophila gene that is homologous to the vertebrate FAK family of protein-tyrosine kinases. We designated this geneDfak56...

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Bibliographic Details
Published in:The Journal of biological chemistry 1999-10, Vol.274 (41), p.29196-29201
Main Authors: Fujimoto, Jiro, Sawamoto, Kazunobu, Okabe, Masataka, Takagi, Yasumitsu, Tezuka, Tohru, Yoshikawa, Shingo, Ryo, Haruko, Okano, Hideyuki, Yamamoto, Tadashi
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Cell Adhesion - genetics
Cell Adhesion Molecules - chemistry
Cell Adhesion Molecules - genetics
Cloning, Molecular
Dfak56 gene
Drosophila melanogaster
Drosophila melanogaster - enzymology
Drosophila Proteins
Extracellular Matrix - metabolism
Fluorescent Antibody Technique
focal adhesion kinase
Focal Adhesion Kinase 1
Focal Adhesion Protein-Tyrosine Kinases
Gene Expression Regulation, Developmental
Gene Expression Regulation, Enzymologic
In Situ Hybridization
Integrins - metabolism
Molecular Sequence Data
Phosphoproteins - analysis
Phosphorylation
Phosphotyrosine - analysis
Protein-Tyrosine Kinases - chemistry
Protein-Tyrosine Kinases - genetics
RNA, Messenger - metabolism
Sequence Alignment
Signal Transduction
Space life sciences
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Summary: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 aDrosophila gene that is homologous to the vertebrate FAK family of protein-tyrosine kinases. We designated this geneDfak56 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 Drosophilaposition-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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.274.41.29196