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Background  When the parasitoid wasp  Leptopilina boulardi  lays an egg in a  Drosophila  larva, phagocytic cells called plasmatocytes and specialized cells known as lamellocytes encapsulate the egg. The  Drosophila  β-integrin Myospheroid (Mys) is necessary for lamellocytes to adhere to the cellular capsule surrounding  L. boulardi  eggs. Integrins are heterodimeric adhesion receptors consisting of α and β subunits, and similar to other plasma membrane receptors undergo ligand-dependent endocytosis. In mammalian cells it is known that integrin binding to the extracellular matrix induces the activation of Rac GTPases, and we have previously shown that Rac1 and Rac2 are necessary for a proper encapsulation response in  Drosophila  larvae. We wanted to test the possibility that Myospheroid and Rac GTPases interact during the  Drosophila  anti-parasitoid immune response.    Results  In the current study we demonstrate that Rac1 is required for the proper localization of Myospheroid to the cell periphery of haemocytes after parasitization. Interestingly, the mislocalization of Myospheroid in Rac1 mutants is rescued by hyperthermia, involving the heat shock protein Hsp83. From these results we conclude that Rac1 and Hsp83 are required for the proper localization of Mys after parasitization.    Significance  We show for the first time that the small GTPase Rac1 is required for Mysopheroid localization. Interestingly, the necessity of Rac1 in Mys localization was negated by hyperthermia. This presents a problem, in  Drosophila  we quite often raise larvae at 29°C when using the GAL4/UAS misexpression system. If hyperthermia rescues receptor endosomal recycling defects, raising larvae in hyperthermic conditions may mask potentially interesting phenotypes.

The Rho-Family GTPase Rac1 Regulates Integrin Localization in Drosophila Immunosurveillance Cells