Tropomyosin Isoforms Specify Functionally Distinct Actin Filament Populations In Vitro.
Identifieur interne : 000105 ( PubMed/Checkpoint ); précédent : 000104; suivant : 000106Tropomyosin 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 : CB [ 1879-0445 ] ; 2017.
Abstract
Actin filaments assemble into a variety of networks to provide force for diverse cellular processes [1]. 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 [2-5]. In mammals, >40 tropomyosin isoforms can be generated through alternative splicing from four tropomyosin genes. Different isoforms display non-redundant functions and partially non-overlapping localization patterns, for example within the stress fiber network [6, 7]. Based on cell biological studies, it was thus proposed that tropomyosin isoforms may specify the functional properties of different actin filament populations [2]. 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.
DOI: 10.1016/j.cub.2017.01.018
PubMed: 28216317
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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Manstein</name><affiliation wicri:level="3"><nlm:affiliation>Institute for Biophysical Chemistry, Hannover Medical School, 30625 Hannover, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute for Biophysical Chemistry, Hannover Medical School, 30625 Hannover</wicri:regionArea><placeName><region type="land" nuts="2">Basse-Saxe</region><settlement type="city">Hanovre</settlement></placeName></affiliation></author><author><name sortKey="Michelot, Alphee" sort="Michelot, Alphee" uniqKey="Michelot A" first="Alphée" last="Michelot">Alphée Michelot</name><affiliation wicri:level="1"><nlm:affiliation>Aix-Marseille University, CNRS, IBDM, 13284 Marseille, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Aix-Marseille University, CNRS, IBDM, 13284 Marseille</wicri:regionArea><wicri:noRegion>13284 Marseille</wicri:noRegion><placeName><settlement type="city">Marseille</settlement><region type="région" nuts="2">Provence-Alpes-Côte d'Azur</region></placeName></affiliation></author><author><name sortKey="Lappalainen, Pekka" sort="Lappalainen, Pekka" uniqKey="Lappalainen P" first="Pekka" last="Lappalainen">Pekka Lappalainen</name><affiliation wicri:level="4"><nlm:affiliation>Institute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland. Electronic address: pekka.lappalainen@helsinki.fi.</nlm:affiliation><country xml:lang="fr">Finlande</country><wicri:regionArea>Institute of Biotechnology, University of Helsinki, P.O. 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Box 56, 00014 Helsinki, Finland.</nlm:affiliation><country xml:lang="fr">Finlande</country><wicri:regionArea>Institute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki</wicri:regionArea><orgName type="university">Université d'Helsinki</orgName><placeName><settlement type="city">Helsinki</settlement><region type="région" nuts="2">Uusimaa</region></placeName></affiliation></author><author><name sortKey="Kremneva, Elena" sort="Kremneva, Elena" uniqKey="Kremneva E" first="Elena" last="Kremneva">Elena Kremneva</name><affiliation wicri:level="4"><nlm:affiliation>Institute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland.</nlm:affiliation><country xml:lang="fr">Finlande</country><wicri:regionArea>Institute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki</wicri:regionArea><orgName type="university">Université d'Helsinki</orgName><placeName><settlement type="city">Helsinki</settlement><region type="région" nuts="2">Uusimaa</region></placeName></affiliation></author><author><name sortKey="Reindl, Theresia" sort="Reindl, Theresia" uniqKey="Reindl T" first="Theresia" last="Reindl">Theresia Reindl</name><affiliation wicri:level="3"><nlm:affiliation>Institute for Biophysical Chemistry, Hannover Medical School, 30625 Hannover, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute for Biophysical Chemistry, Hannover Medical School, 30625 Hannover</wicri:regionArea><placeName><region type="land" nuts="2">Basse-Saxe</region><settlement type="city">Hanovre</settlement></placeName></affiliation></author><author><name sortKey="Kotila, Tommi" sort="Kotila, Tommi" uniqKey="Kotila T" first="Tommi" last="Kotila">Tommi Kotila</name><affiliation wicri:level="4"><nlm:affiliation>Institute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland.</nlm:affiliation><country xml:lang="fr">Finlande</country><wicri:regionArea>Institute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki</wicri:regionArea><orgName type="university">Université d'Helsinki</orgName><placeName><settlement type="city">Helsinki</settlement><region type="région" nuts="2">Uusimaa</region></placeName></affiliation></author><author><name sortKey="Kogan, Konstantin" sort="Kogan, Konstantin" uniqKey="Kogan K" first="Konstantin" last="Kogan">Konstantin Kogan</name><affiliation wicri:level="4"><nlm:affiliation>Institute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland.</nlm:affiliation><country xml:lang="fr">Finlande</country><wicri:regionArea>Institute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki</wicri:regionArea><orgName type="university">Université d'Helsinki</orgName><placeName><settlement type="city">Helsinki</settlement><region type="région" nuts="2">Uusimaa</region></placeName></affiliation></author><author><name sortKey="Gressin, Laurene" sort="Gressin, Laurene" uniqKey="Gressin L" first="Laurène" last="Gressin">Laurène Gressin</name><affiliation wicri:level="1"><nlm:affiliation>Biosciences and Biotechnology Institute of Grenoble, LPCV/CNRS/CEA/UGA/INRA, 38054 Grenoble, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Biosciences and Biotechnology Institute of Grenoble, LPCV/CNRS/CEA/UGA/INRA, 38054 Grenoble</wicri:regionArea><wicri:noRegion>38054 Grenoble</wicri:noRegion><placeName><settlement type="city">Grenoble</settlement><region type="region" nuts="2">Auvergne-Rhône-Alpes</region><region type="old region" nuts="2">Rhône-Alpes</region></placeName></affiliation></author><author><name sortKey="Gunning, Peter W" sort="Gunning, Peter W" uniqKey="Gunning P" first="Peter W" last="Gunning">Peter W. Gunning</name><affiliation wicri:level="1"><nlm:affiliation>Oncology Research Unit, School of Medical Sciences, UNSW Australia, Sydney, NSW 2052, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Oncology Research Unit, School of Medical Sciences, UNSW Australia, Sydney, NSW 2052</wicri:regionArea><wicri:noRegion>NSW 2052</wicri:noRegion></affiliation></author><author><name sortKey="Manstein, Dietmar J" sort="Manstein, Dietmar J" uniqKey="Manstein D" first="Dietmar J" last="Manstein">Dietmar J. Manstein</name><affiliation wicri:level="3"><nlm:affiliation>Institute for Biophysical Chemistry, Hannover Medical School, 30625 Hannover, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute for Biophysical Chemistry, Hannover Medical School, 30625 Hannover</wicri:regionArea><placeName><region type="land" nuts="2">Basse-Saxe</region><settlement type="city">Hanovre</settlement></placeName></affiliation></author><author><name sortKey="Michelot, Alphee" sort="Michelot, Alphee" uniqKey="Michelot A" first="Alphée" last="Michelot">Alphée Michelot</name><affiliation wicri:level="1"><nlm:affiliation>Aix-Marseille University, CNRS, IBDM, 13284 Marseille, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Aix-Marseille University, CNRS, IBDM, 13284 Marseille</wicri:regionArea><wicri:noRegion>13284 Marseille</wicri:noRegion><placeName><settlement type="city">Marseille</settlement><region type="région" nuts="2">Provence-Alpes-Côte d'Azur</region></placeName></affiliation></author><author><name sortKey="Lappalainen, Pekka" sort="Lappalainen, Pekka" uniqKey="Lappalainen P" first="Pekka" last="Lappalainen">Pekka Lappalainen</name><affiliation wicri:level="4"><nlm:affiliation>Institute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland. Electronic address: pekka.lappalainen@helsinki.fi.</nlm:affiliation><country xml:lang="fr">Finlande</country><wicri:regionArea>Institute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki</wicri:regionArea><orgName type="university">Université d'Helsinki</orgName><placeName><settlement type="city">Helsinki</settlement><region type="région" nuts="2">Uusimaa</region></placeName></affiliation></author></analytic><series><title level="j">Current biology : CB</title><idno type="eISSN">1879-0445</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Actin filaments assemble into a variety of networks to provide force for diverse cellular processes [1]. 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 [2-5]. In mammals, >40 tropomyosin isoforms can be generated through alternative splicing from four tropomyosin genes. Different isoforms display non-redundant functions and partially non-overlapping localization patterns, for example within the stress fiber network [6, 7]. Based on cell biological studies, it was thus proposed that tropomyosin isoforms may specify the functional properties of different actin filament populations [2]. 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.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">28216317</PMID><DateCreated><Year>2017</Year><Month>02</Month><Day>20</Day></DateCreated><DateRevised><Year>2017</Year><Month>03</Month><Day>19</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0445</ISSN><JournalIssue CitedMedium="Internet"><Volume>27</Volume><Issue>5</Issue><PubDate><Year>2017</Year><Month>Mar</Month><Day>06</Day></PubDate></JournalIssue><Title>Current biology : CB</Title><ISOAbbreviation>Curr. Biol.</ISOAbbreviation></Journal><ArticleTitle>Tropomyosin Isoforms Specify Functionally Distinct Actin Filament Populations In Vitro.</ArticleTitle><Pagination><MedlinePgn>705-713</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0960-9822(17)30018-0</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.cub.2017.01.018</ELocationID><Abstract><AbstractText>Actin filaments assemble into a variety of networks to provide force for diverse cellular processes [1]. 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 [2-5]. In mammals, >40 tropomyosin isoforms can be generated through alternative splicing from four tropomyosin genes. Different isoforms display non-redundant functions and partially non-overlapping localization patterns, for example within the stress fiber network [6, 7]. Based on cell biological studies, it was thus proposed that tropomyosin isoforms may specify the functional properties of different actin filament populations [2]. 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.</AbstractText><CopyrightInformation>Copyright © 2017 The Author(s). Published by Elsevier Ltd.. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gateva</LastName><ForeName>Gergana</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Institute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kremneva</LastName><ForeName>Elena</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Institute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Reindl</LastName><ForeName>Theresia</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Institute for Biophysical Chemistry, Hannover Medical School, 30625 Hannover, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kotila</LastName><ForeName>Tommi</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Institute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kogan</LastName><ForeName>Konstantin</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Institute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gressin</LastName><ForeName>Laurène</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Biosciences and Biotechnology Institute of Grenoble, LPCV/CNRS/CEA/UGA/INRA, 38054 Grenoble, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gunning</LastName><ForeName>Peter W</ForeName><Initials>PW</Initials><AffiliationInfo><Affiliation>Oncology Research Unit, School of Medical Sciences, UNSW Australia, Sydney, NSW 2052, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Manstein</LastName><ForeName>Dietmar J</ForeName><Initials>DJ</Initials><AffiliationInfo><Affiliation>Institute for Biophysical Chemistry, Hannover Medical School, 30625 Hannover, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Michelot</LastName><ForeName>Alphée</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Aix-Marseille University, CNRS, IBDM, 13284 Marseille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lappalainen</LastName><ForeName>Pekka</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Institute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland. Electronic address: pekka.lappalainen@helsinki.fi.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>02</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Curr Biol</MedlineTA><NlmUniqueID>9107782</NlmUniqueID><ISSNLinking>0960-9822</ISSNLinking></MedlineJournalInfo><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>J Cell Sci. 2015 Jun 1;128(11):2009-19</RefSource><PMID Version="1">25788699</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2015 May 12;112(19):E2447-56</RefSource><PMID Version="1">25918420</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Elife. 2015 Feb 02;4:null</RefSource><PMID 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PubStatus="revised"><Year>2016</Year><Month>12</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2017</Year><Month>01</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>2</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>2</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>2</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28216317</ArticleId><ArticleId IdType="pii">S0960-9822(17)30018-0</ArticleId><ArticleId IdType="doi">10.1016/j.cub.2017.01.018</ArticleId><ArticleId IdType="pmc">PMC5344678</ArticleId></ArticleIdList></PubmedData></pubmed><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></region><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></country><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></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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