A new isoform of Drosophila non-muscle Tropomyosin 1 interacts with Kinesin-1 and functions in oskar mRNA localization
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 th...
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| Veröffentlicht in: | Journal of cell science 2016-11, Vol.129 (22), p.4252-4264 |
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| creator | Veeranan-Karmegam, Rajalakshmi Boggupalli, Devi Prasad Liu, Guojun Gonsalvez, Graydon B |
| description | 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 as Tm1C, 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. |
| doi_str_mv | 10.1242/jcs.194332 |
| format | Article |
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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 as Tm1C, 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.</description><identifier>ISSN: 0021-9533</identifier><identifier>EISSN: 1477-9137</identifier><identifier>DOI: 10.1242/jcs.194332</identifier><identifier>PMID: 27802167</identifier><language>eng</language><publisher>England: The Company of Biologists Ltd</publisher><subject>Animals ; Drosophila melanogaster ; Drosophila melanogaster - metabolism ; Drosophila Proteins - genetics ; Female ; Germ Cells ; Green Fluorescent Proteins - metabolism ; Kinesin - metabolism ; Muscles - metabolism ; Mutation - genetics ; Protein Binding ; Protein Isoforms - metabolism ; Protein Transport ; RNA Transport ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; Tropomyosin - metabolism</subject><ispartof>Journal of cell science, 2016-11, Vol.129 (22), p.4252-4264</ispartof><rights>2016. Published by The Company of Biologists Ltd.</rights><rights>2016. 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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 as Tm1C, 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.</description><subject>Animals</subject><subject>Drosophila melanogaster</subject><subject>Drosophila melanogaster - metabolism</subject><subject>Drosophila Proteins - genetics</subject><subject>Female</subject><subject>Germ Cells</subject><subject>Green Fluorescent Proteins - metabolism</subject><subject>Kinesin - metabolism</subject><subject>Muscles - metabolism</subject><subject>Mutation - genetics</subject><subject>Protein Binding</subject><subject>Protein Isoforms - metabolism</subject><subject>Protein Transport</subject><subject>RNA Transport</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>Tropomyosin - metabolism</subject><issn>0021-9533</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1LxDAQhoMoun5c_AGSowjVTNI07UVY_EZRED2HNJu60TZZk1ZZf71ZVkVvnubwPrzMzIPQLpBDoDk9etbxEKqcMbqCRpALkVXAxCoaEUIhqzhjG2gzxmdCiKCVWEcbVJQpKsQIvY2xM-_YRt_40GHf4NPgo59Nbauw8y7rhqhbgx-Cn_lu7qN1GLB1vQlK9xG_236Kr60zKcgAKzfBzeB0b72LCcM-vqiAu_vbMW69Vq39UItsG601qo1m52tuocfzs4eTy-zm7uLqZHyTaSZ4nwnFBS-KilBBFVVEcy7KSVk3tDa6gFKLmgFTBauZ0QJKw2oOnJK80SQHo9gWOl72zoa6MxNtXB9UK2fBdirMpVdW_k2cncon_yY5gKCEpoL9r4LgXwcTe9nZqE3bKmf8ECWURclyqMr8HyjjSUFeFQk9WKI6PTsG0_xsBEQunMrkVC6dJnjv9w0_6LdE9gmmB54J</recordid><startdate>20161115</startdate><enddate>20161115</enddate><creator>Veeranan-Karmegam, Rajalakshmi</creator><creator>Boggupalli, Devi Prasad</creator><creator>Liu, Guojun</creator><creator>Gonsalvez, Graydon B</creator><general>The Company of Biologists Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7SS</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-4458-8497</orcidid></search><sort><creationdate>20161115</creationdate><title>A new isoform of Drosophila non-muscle Tropomyosin 1 interacts with Kinesin-1 and functions in oskar mRNA localization</title><author>Veeranan-Karmegam, Rajalakshmi ; Boggupalli, Devi Prasad ; Liu, Guojun ; Gonsalvez, Graydon B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-7a5756690272a2a0c5578d8bf2bec618c7b313a63b3ec718e3b515204fc041ea3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Animals</topic><topic>Drosophila melanogaster</topic><topic>Drosophila melanogaster - metabolism</topic><topic>Drosophila Proteins - genetics</topic><topic>Female</topic><topic>Germ Cells</topic><topic>Green Fluorescent Proteins - metabolism</topic><topic>Kinesin - metabolism</topic><topic>Muscles - metabolism</topic><topic>Mutation - genetics</topic><topic>Protein Binding</topic><topic>Protein Isoforms - metabolism</topic><topic>Protein Transport</topic><topic>RNA Transport</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - metabolism</topic><topic>Tropomyosin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Veeranan-Karmegam, Rajalakshmi</creatorcontrib><creatorcontrib>Boggupalli, Devi Prasad</creatorcontrib><creatorcontrib>Liu, Guojun</creatorcontrib><creatorcontrib>Gonsalvez, Graydon B</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Entomology Abstracts (Full archive)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of cell science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Veeranan-Karmegam, Rajalakshmi</au><au>Boggupalli, Devi Prasad</au><au>Liu, Guojun</au><au>Gonsalvez, Graydon B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A new isoform of Drosophila non-muscle Tropomyosin 1 interacts with Kinesin-1 and functions in oskar mRNA localization</atitle><jtitle>Journal of cell science</jtitle><addtitle>J Cell Sci</addtitle><date>2016-11-15</date><risdate>2016</risdate><volume>129</volume><issue>22</issue><spage>4252</spage><epage>4264</epage><pages>4252-4264</pages><issn>0021-9533</issn><eissn>1477-9137</eissn><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 as Tm1C, 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. 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| subjects | Animals Drosophila melanogaster Drosophila melanogaster - metabolism Drosophila Proteins - genetics Female Germ Cells Green Fluorescent Proteins - metabolism Kinesin - metabolism Muscles - metabolism Mutation - genetics Protein Binding Protein Isoforms - metabolism Protein Transport RNA Transport RNA, Messenger - genetics RNA, Messenger - metabolism Tropomyosin - metabolism |
| title | A new isoform of Drosophila non-muscle Tropomyosin 1 interacts with Kinesin-1 and functions in oskar mRNA localization |
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