TY - JOUR
T1 - A new isoform of Drosophila non-muscle Tropomyosin 1 interacts with Kinesin-1 and functions in oskar mRNA localization
AU - Veeranan-Karmegam, Rajalakshmi
AU - Boggupalli, Devi Prasad
AU - Liu, Guojun
AU - Gonsalvez, Graydon B.
N1 - Publisher Copyright:
© 2016.
PY - 2016
Y1 - 2016
N2 - 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.
AB - 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.
KW - Actin
KW - Cell polarity
KW - Molecular motor
KW - RNA localization
UR - http://www.scopus.com/inward/record.url?scp=84995892160&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84995892160&partnerID=8YFLogxK
U2 - 10.1242/jcs.194332
DO - 10.1242/jcs.194332
M3 - Article
C2 - 27802167
AN - SCOPUS:84995892160
SN - 0021-9533
VL - 129
SP - 4252
EP - 4264
JO - Journal of Cell Science
JF - Journal of Cell Science
IS - 22
ER -