High impact information on by

• Collectively, our data suggest that tensin relays signals from the extracellular matrix to the cytoskeleton through interaction with integrin, and through the modulation of the JNK signal transduction pathway during Drosophila wing development [1].
• At focal adhesion sites, tensin participates in the protein complex that establishes transmembrane linkage between the extracellular matrix and cytoskeletal actin filaments [1].
• Interestingly, by(1)-the mutant allele of the gene blistery (by)-also showed a blistered wing phenotype, but failed to complement the wing blister phenotype of the Drosophila tensin mutants, and contains Y62N/T163R point mutations in Drosophila tensin coding sequences [1].
• We report the functional characterization of the Drosophila ortholog of tensin, a protein implicated in linking integrins to the cytoskeleton and signaling pathways [2].
• To investigate further the role of the dPI3K pathway in regulating dS6K activation, we also used dsRNAi (double-stranded RNA-mediated interference) to decrease expression of dPI3K and the PtdIns(3,4,5) P (3) phosphatase dPTEN ( Drosophila phosphatase and tensin homologue deleted on chromosome 10) in Kc167 and S2 cells [3].

Biological context of by

• A tensin null was generated and is viable with wing blisters, a phenotype characteristic of loss of integrin adhesion [2].

Anatomical context of by

• Tensin is an actin-binding protein that is localized in focal adhesions [1].

Associations of by with chemical compounds

• Tensin stabilizes integrin adhesive contacts in Drosophila [2].

References