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Background  Calpains are calcium regulated intracellular cysteine proteases implicated in a variety of physiological functions and pathological conditions. The  Drosophila melanogaster  genome contains only two genes,  CalpA  and  CalpB  coding for canonical, active calpain enzymes. The movement of the border cells in  Drosophila  egg chambers is a well characterized model of the eukaryotic cell migration. Using this genetically pliable model we can investigate the physiological role of calpains in cell motility.    Results  We demonstrate at the whole organism level that  CalpB  is implicated in cell migration, while the structurally related  CalpA  paralog can not fulfill the same function. The downregulation of the  CalpB  gene by mutations or RNA interference results in a delayed migration of the border cells in  Drosophila  egg chambers. This phenotype is significantly enhanced when the focal adhesion complex genes encoding for α-PS2 integrin (  if ), β-PS integrin (  mys ) and talin (  rhea ) are silenced. The reduction of  CalpB  activity diminishes the release of integrins from the rear end of the border cells. The delayed migration and the reduced integrin release phenotypes can be suppressed by expressing wild-type talin-head in the border cells but not talin-head R367A , a mutant form which is not able to bind β-PS integrin. CalpB can cleave talin  in vitro,  and the two proteins coimmunoprecipitate from  Drosophila  extracts.    Conclusions  The physiological function of  CalpB  in border cell motility has been demonstrated in  vivo . The genetic interaction between the  CalpB  and the  if ,  mys,  as well as  rhea  genes, the involvement of active talin head-domains in the process, and the fact that CalpB and talin interact with each other collectively suggest that the limited proteolytic cleavage of talin is one of the possible mechanisms through which CalpB regulates cell migration.

CalpB modulates border cell migration in Drosophila egg chambers