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 Citations (Scopus)

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 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
Volume129
Issue number22
DOIs
StatePublished - Jan 1 2016

Fingerprint

Kinesin
Tropomyosin
Drosophila
Protein Isoforms
Messenger RNA
Oocytes
Microtubules
Drosophila melanogaster
Light

Keywords

  • Actin
  • Cell polarity
  • Molecular motor
  • RNA localization

ASJC Scopus subject areas

  • Cell Biology

Cite this

A new isoform of Drosophila non-muscle Tropomyosin 1 interacts with Kinesin-1 and functions in oskar mRNA localization. / Veeranan-Karmegam, Rajalakshmi; Boggupalli, Devi Prasad; Liu, Guojun; Gonsalvez, Graydon B.

In: Journal of Cell Science, Vol. 129, No. 22, 01.01.2016, p. 4252-4264.

Research output: Contribution to journalArticle

Veeranan-Karmegam, Rajalakshmi ; Boggupalli, Devi Prasad ; Liu, Guojun ; Gonsalvez, Graydon B. / A new isoform of Drosophila non-muscle Tropomyosin 1 interacts with Kinesin-1 and functions in oskar mRNA localization. In: Journal of Cell Science. 2016 ; Vol. 129, No. 22. pp. 4252-4264.
@article{7c4b9393be3f4fc59623c09a63c08c98,
title = "A new isoform of Drosophila non-muscle Tropomyosin 1 interacts with Kinesin-1 and functions in oskar 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 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.",
keywords = "Actin, Cell polarity, Molecular motor, RNA localization",
author = "Rajalakshmi Veeranan-Karmegam and Boggupalli, {Devi Prasad} and Guojun Liu and Gonsalvez, {Graydon B.}",
year = "2016",
month = "1",
day = "1",
doi = "10.1242/jcs.194332",
language = "English (US)",
volume = "129",
pages = "4252--4264",
journal = "Journal of Cell Science",
issn = "0021-9533",
publisher = "Company of Biologists Ltd",
number = "22",

}

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.

PY - 2016/1/1

Y1 - 2016/1/1

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

VL - 129

SP - 4252

EP - 4264

JO - Journal of Cell Science

JF - Journal of Cell Science

SN - 0021-9533

IS - 22

ER -