CalpB modulates border cell migration in Drosophila egg chambers

BMC Developmental Biology

Géza Ádám⁴  Viktor Dombrádi³  Péter Friedrich¹  Péter Deák²  Éva Kerekes³  Margit Pál²  Anil Chougule⁴  Kálmán Somogyi²  Ferencz Sándor Páldy⁴  Endre Kókai³ 

[1] Institute of Enzymology, Hungarian Academy of Sciences, Budapest, Hungary;Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary;Department of Medical Chemistry, Faculty of Medicine, University of Debrecen, Nagyerdei krt. 98, Debrecen H-4032, Hungary;Institute of Genetics, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary

关键词: Integrins;    Talin;    Calpain;    Focal adhesion;    Proteolysis;    Cell motility;   

Others  :  1086573
DOI  :  10.1186/1471-213X-12-20

 received in 2011-12-19, accepted in 2012-07-24,  发布年份 2012

【 摘 要 】

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.

【 授权许可】

   
2012 Kokai et al.; licensee BioMed Central Ltd.

【 图 表 】

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