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

Rajalakshmi Veeranan-Karmegam, Devi Prasad Boggupalli, Guojun Liu, Graydon B. Gonsalvez

Research output: Contribution to journalArticle

9 Scopus citations


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 melanogaster 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 newly discovered isoform of Tropomyosin 1, referred to asTm1C, directly interacts with Khc and functions in concert with this microtubule motor to localize osk mRNA. Apart from osk mRNA localization, 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.

Original languageEnglish (US)
Pages (from-to)4252-4264
Number of pages13
JournalJournal of Cell Science
Issue number22
Publication statusPublished - Jan 1 2016



  • Actin
  • Cell polarity
  • Molecular motor
  • RNA localization

ASJC Scopus subject areas

  • Cell Biology

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