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  • Grabbe, CarolineUmeå universitet,Umeå centrum för molekylär patogenes (UCMP) (Medicinska fakulteten) (author)

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

  • Article/chapterEnglish2004

Publisher, publication year, extent ...

  • The Company of Biologists,2004
  • printrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:umu-17928
  • https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-17928URI
  • https://doi.org/10.1242/dev.01462DOI

Supplementary language notes

  • Language:English
  • Summary in:English

Part of subdatabase

Classification

  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • 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.

Subject headings and genre

  • Animals
  • Blotting; Southern
  • Blotting; Western
  • Cell Membrane/metabolism
  • Cytoskeleton/metabolism
  • DNA/metabolism
  • Down-Regulation
  • Drosophila
  • Drosophila Proteins
  • Drosophila melanogaster
  • Focal Adhesion Kinase 1
  • Focal Adhesion Protein-Tyrosine Kinases
  • Gene Deletion
  • Gene Expression Regulation
  • Immunoblotting
  • Integrins/*metabolism
  • Models; Genetic
  • Muscles/embryology
  • Mutation
  • Phenotype
  • Phosphorylation
  • Protein Structure; Tertiary
  • Protein-Tyrosine Kinases/*genetics/*physiology
  • Signal Transduction
  • Transgenes
  • Tyrosine/metabolism

Added entries (persons, corporate bodies, meetings, titles ...)

  • Zervas, Christos G (author)
  • Hunter, Tony (author)
  • Brown, Nicholas H (author)
  • Palmer, RuthUmeå universitet,Umeå centrum för molekylär patogenes (UCMP) (Medicinska fakulteten)(Swepub:umu)rupa0001 (author)
  • Umeå universitetUmeå centrum för molekylär patogenes (UCMP) (Medicinska fakulteten) (creator_code:org_t)

Related titles

  • In:Development: The Company of Biologists131:23, s. 5795-58050950-19911477-9129

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