Tropomyosin Isoforms Specify Functionally Distinct Actin Filament Populations In Vitro
Identifieur interne : 000126 ( Main/Exploration ); précédent : 000125; suivant : 000127Tropomyosin Isoforms Specify Functionally Distinct Actin Filament Populations In Vitro
Auteurs : Gergana Gateva [Finlande] ; Elena Kremneva [Finlande] ; Theresia Reindl [Allemagne] ; Tommi Kotila [Finlande] ; Konstantin Kogan [Finlande] ; Laurène Gressin [France] ; Peter W. Gunning [Australie] ; Dietmar J. Manstein [Allemagne] ; Alphée Michelot [France] ; Pekka Lappalainen [Finlande]Source :
- Current Biology [ 0960-9822 ] ; 2017.
Abstract
Actin filaments assemble into a variety of networks to provide force for diverse cellular processes [
Url:
DOI: 10.1016/j.cub.2017.01.018
PubMed: 28216317
PubMed Central: 5344678
Affiliations:
- Allemagne, Australie, Finlande, France
- Auvergne-Rhône-Alpes, Basse-Saxe, Provence-Alpes-Côte d'Azur, Rhône-Alpes, Uusimaa
- Grenoble, Hanovre, Helsinki, Marseille
- Université d'Helsinki
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Le document en format XML
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<series><title level="j">Current Biology</title>
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<front><div type="abstract" xml:lang="en"><title>Summary</title>
<p>Actin filaments assemble into a variety of networks to provide force for diverse cellular processes [<xref rid="bib1" ref-type="bibr">1</xref>
]. Tropomyosins are coiled-coil dimers that form head-to-tail polymers along actin filaments and regulate interactions of other proteins, including actin-depolymerizing factor (ADF)/cofilins and myosins, with actin [<xref rid="bib2" ref-type="bibr">2</xref>
, <xref rid="bib3" ref-type="bibr">3</xref>
, <xref rid="bib4" ref-type="bibr">4</xref>
, <xref rid="bib5" ref-type="bibr">5</xref>
]. In mammals, >40 tropomyosin isoforms can be generated through alternative splicing from four <italic>tropomyosin</italic>
genes. Different isoforms display non-redundant functions and partially non-overlapping localization patterns, for example within the stress fiber network [<xref rid="bib6" ref-type="bibr">6</xref>
, <xref rid="bib7" ref-type="bibr">7</xref>
]. Based on cell biological studies, it was thus proposed that tropomyosin isoforms may specify the functional properties of different actin filament populations [<xref rid="bib2" ref-type="bibr">2</xref>
]. To test this hypothesis, we analyzed the properties of actin filaments decorated by stress-fiber-associated tropomyosins (Tpm1.6, Tpm1.7, Tpm2.1, Tpm3.1, Tpm3.2, and Tpm4.2). These proteins bound F-actin with high affinity and competed with α-actinin for actin filament binding. Importantly, total internal reflection fluorescence (TIRF) microscopy of fluorescently tagged proteins revealed that most tropomyosin isoforms cannot co-polymerize with each other on actin filaments. These isoforms also bind actin with different dynamics, which correlate with their effects on actin-binding proteins. The long isoforms Tpm1.6 and Tpm1.7 displayed stable interactions with actin filaments and protected filaments from ADF/cofilin-mediated disassembly, but did not activate non-muscle myosin IIa (NMIIa). In contrast, the short isoforms Tpm3.1, Tpm3.2, and Tpm4.2 displayed rapid dynamics on actin filaments and stimulated the ATPase activity of NMIIa, but did not efficiently protect filaments from ADF/cofilin. Together, these data provide experimental evidence that tropomyosin isoforms segregate to different actin filaments and specify functional properties of distinct actin filament populations.</p>
</div>
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</TEI>
<affiliations><list><country><li>Allemagne</li>
<li>Australie</li>
<li>Finlande</li>
<li>France</li>
</country>
<region><li>Auvergne-Rhône-Alpes</li>
<li>Basse-Saxe</li>
<li>Provence-Alpes-Côte d'Azur</li>
<li>Rhône-Alpes</li>
<li>Uusimaa</li>
</region>
<settlement><li>Grenoble</li>
<li>Hanovre</li>
<li>Helsinki</li>
<li>Marseille</li>
</settlement>
<orgName><li>Université d'Helsinki</li>
</orgName>
</list>
<tree><country name="Finlande"><region name="Uusimaa"><name sortKey="Gateva, Gergana" sort="Gateva, Gergana" uniqKey="Gateva G" first="Gergana" last="Gateva">Gergana Gateva</name>
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<name sortKey="Kogan, Konstantin" sort="Kogan, Konstantin" uniqKey="Kogan K" first="Konstantin" last="Kogan">Konstantin Kogan</name>
<name sortKey="Kotila, Tommi" sort="Kotila, Tommi" uniqKey="Kotila T" first="Tommi" last="Kotila">Tommi Kotila</name>
<name sortKey="Kremneva, Elena" sort="Kremneva, Elena" uniqKey="Kremneva E" first="Elena" last="Kremneva">Elena Kremneva</name>
<name sortKey="Lappalainen, Pekka" sort="Lappalainen, Pekka" uniqKey="Lappalainen P" first="Pekka" last="Lappalainen">Pekka Lappalainen</name>
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<country name="Allemagne"><region name="Basse-Saxe"><name sortKey="Reindl, Theresia" sort="Reindl, Theresia" uniqKey="Reindl T" first="Theresia" last="Reindl">Theresia Reindl</name>
</region>
<name sortKey="Manstein, Dietmar J" sort="Manstein, Dietmar J" uniqKey="Manstein D" first="Dietmar J." last="Manstein">Dietmar J. Manstein</name>
</country>
<country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Gressin, Laurene" sort="Gressin, Laurene" uniqKey="Gressin L" first="Laurène" last="Gressin">Laurène Gressin</name>
</region>
<name sortKey="Michelot, Alphee" sort="Michelot, Alphee" uniqKey="Michelot A" first="Alphée" last="Michelot">Alphée Michelot</name>
</country>
<country name="Australie"><noRegion><name sortKey="Gunning, Peter W" sort="Gunning, Peter W" uniqKey="Gunning P" first="Peter W." last="Gunning">Peter W. Gunning</name>
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</record>
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