A novel isoform of Drosophila non-muscle Tropomyosin interacts with Kinesin-1 and functions in mRNA localization

Abstract

Recent studies have revealed that diverse cell types use mRNA localization as a means to establish polarity. Despite the prevalence of this phenomenon, much less is known regarding the mechanism by which mRNAs are localized. The Drosophila oocyte provides a useful model for examining the process of mRNA localization. oskar (osk) mRNA is localized at the posterior of the oocyte, thus restricting the expression of Oskar protein to this site. The localization of osk mRNA is microtubule-dependent and requires the plus-end directed motor, Kinesin-1. Unlike most Kinesin-1 cargoes, localization of osk mRNA requires the Kinesin heavy chain (Khc) motor subunit, but not the Kinesin light chain (Klc) adaptor. In this report, we demonstrate that a novel isoform of Tropomyosin, referred to as Tm1C, directly interacts with Khc and functions in concert with this microtubule motor to localize osk mRNA. In contrast to osk, several additional Khc-dependent processes in the oocyte are unaffected upon loss of Tm1C. Our results therefore suggest that the Tm1C-Khc interaction is specific for the osk localization pathway.