Disease relevance of Fak56D

• Furthermore, immunoblotting analysis using anti-Y397 demonstrated intense FAK activity at the Y397/SH2-binding site in hemocytes treated with E. coli [1].

High impact information on Fak56D

• Furthermore, when expressed in NIH 3T3 cells, DFak56 both localizes to focal contacts and displays the characteristic elevation of phosphotyrosine content in response to plating the cells on fibronectin [2].
• Consistent with a role in cell migration, we also observe that DFak56 is abundant in the border cells of developing egg chambers before the onset of, and during, their migration [2].
• During embryogenesis, DFak56 is broadly expressed, and it becomes elevated in the gut and central nervous system at later stages [2].
• Moreover, Fak56D genetically interacts with myospheroid, which encodes an integrin beta subunit [3].
• In addition, we found that CdGAPr is also required for optic stalk formation and genetically interacts with Fak56D [3].

Chemical compound and disease context of Fak56D

• Here we report data concerning the focal adhesion kinase (FAK) tyrosine phosphorylation status in hemocytes in response to E. coli [1].

Biological context of Fak56D

• These phenotypes were completely rescued by Fak56D transgene expression in the SG cells but not in photoreceptor cells [3].
• FAK is a main component of the focal adhesion signaling that regulates various cellular events, including cell migration and morphology [3].
• Focal adhesion kinase controls morphogenesis of the Drosophila optic stalk [3].
• As is the case for FAK, tyrosine phosphorylation of DFak56 is increased upon plating Drosophila embryo cells on extracellular matrix proteins [4].
• Overexpression of DFak56 in the wing imaginal disc results in wing blistering in adults, a phenotype also observed with both position-specific integrin loss of function and position-specific integrin overexpression [4].

Anatomical context of Fak56D

• In a screen for genes involved in optic stalk formation, we identified Fak56D encoding a Drosophila homolog of mammalian focal adhesion kinase (FAK) [3].
• 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 [5].
• We demonstrate that E. coli-triggering stimulates a significant increase in tyrosine phosphorylation of FAK in hemocytes [1].

Associations of Fak56D with chemical compounds

• DFak56 has intrinsic tyrosine kinase activity and is phosphorylated on tyrosine in vivo [4].
• One such pathway requires the slbo gene, which encodes Drosophila C/EBP, a basic region/leucine zipper transcriptional activator that is required for elevated expression of a number of downstream targets, including DE-cadherin and focal adhesion kinase (FAK) [6].

Other interactions of Fak56D

• We demonstrate that Drosphila Wnt4 is required for cell movement and FAK regulation during ovarian morphogenesis [7].

Analytical, diagnostic and therapeutic context of Fak56D

• In situ hybridization and immunofluorescence staining analysis showed that DFak56 is ubiquitously expressed with particularly high levels within the developing central nervous system [4].
• By using polymerase chain reaction (PCR), we amplified about 1.3 kb fragment spanning intron 5-10, located in the position of Tyr kinase (TyK) domain of Dfak gene from Drosophila melanogaster species group, and observed size difference among the amplified DNA fragments from different species [8].

References