MICAL2 is essential for myogenic lineage commitment
Contractile myofiber units are mainly composed of thick myosin and thin actin (F-actin) filaments. F-Actin interacts with Microtubule Associated Monooxygenase, Calponin And LIM Domain Containing 2 (MICAL2). Indeed, MICAL2 modifies actin subunits and promotes actin filament turnover by severing them...
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| Veröffentlicht in: | Cell death & disease 2020-08, Vol.11 (8), p.654-654, Article 654 |
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| creator | Giarratana, Nefele Conti, Filippo La Rovere, Rita Gijsbers, Rik Carai, Paolo Duelen, Robin Vervliet, Tim Bultynck, Geert Ronzoni, Flavio Piciotti, Roberto Costamagna, Domiziana Fulle, Stefania Barravecchia, Ivana Angeloni, Debora Torrente, Yvan Sampaolesi, Maurilio |
| description | Contractile myofiber units are mainly composed of thick myosin and thin actin (F-actin) filaments. F-Actin interacts with Microtubule Associated Monooxygenase, Calponin And LIM Domain Containing 2 (MICAL2). Indeed, MICAL2 modifies actin subunits and promotes actin filament turnover by severing them and preventing repolymerization. In this study, we found that MICAL2 increases during myogenic differentiation of adult and pluripotent stem cells (PSCs) towards skeletal, smooth and cardiac muscle cells and localizes in the nucleus of acute and chronic regenerating muscle fibers. In vivo delivery of Cas9–Mical2 guide RNA complexes results in muscle actin defects and demonstrates that MICAL2 is essential for skeletal muscle homeostasis and functionality. Conversely, MICAL2 upregulation shows a positive impact on skeletal and cardiac muscle commitments. Taken together these data demonstrate that modulations of MICAL2 have an impact on muscle filament dynamics and its fine-tuned balance is essential for the regeneration of muscle tissues. |
| doi_str_mv | 10.1038/s41419-020-02886-z |
| format | Article |
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F-Actin interacts with Microtubule Associated Monooxygenase, Calponin And LIM Domain Containing 2 (MICAL2). Indeed, MICAL2 modifies actin subunits and promotes actin filament turnover by severing them and preventing repolymerization. In this study, we found that MICAL2 increases during myogenic differentiation of adult and pluripotent stem cells (PSCs) towards skeletal, smooth and cardiac muscle cells and localizes in the nucleus of acute and chronic regenerating muscle fibers. In vivo delivery of Cas9–Mical2 guide RNA complexes results in muscle actin defects and demonstrates that MICAL2 is essential for skeletal muscle homeostasis and functionality. Conversely, MICAL2 upregulation shows a positive impact on skeletal and cardiac muscle commitments. Taken together these data demonstrate that modulations of MICAL2 have an impact on muscle filament dynamics and its fine-tuned balance is essential for the regeneration of muscle tissues.</description><identifier>ISSN: 2041-4889</identifier><identifier>EISSN: 2041-4889</identifier><identifier>DOI: 10.1038/s41419-020-02886-z</identifier><identifier>PMID: 32811811</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>42/100 ; 42/109 ; 631/337 ; 631/80/304 ; 64 ; 64/60 ; Actin ; Actin Cytoskeleton - metabolism ; Actin Cytoskeleton - physiology ; Actins - metabolism ; Actins - physiology ; Animals ; Antibodies ; Biochemistry ; Biomedical and Life Sciences ; Calponin ; Cardiac muscle ; Cell Biology ; Cell Culture ; Cell Differentiation - physiology ; Cytoskeletal Proteins - metabolism ; Cytoskeletal Proteins - physiology ; Cytoskeleton - metabolism ; Female ; Filaments ; Homeostasis ; Immunology ; Life Sciences ; Male ; Mice ; Mice, Inbred C57BL ; Monooxygenase ; Muscle contraction ; Muscle Contraction - physiology ; Muscle Development - physiology ; Muscle, Skeletal - metabolism ; Muscle, Smooth - physiology ; Myosin ; Myosins - metabolism ; Myosins - physiology ; Pluripotency ; Ribonucleic acid ; RNA ; Skeletal muscle ; Stem cells</subject><ispartof>Cell death & disease, 2020-08, Vol.11 (8), p.654-654, Article 654</ispartof><rights>The Author(s) 2020</rights><rights>The Author(s) 2020. 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F-Actin interacts with Microtubule Associated Monooxygenase, Calponin And LIM Domain Containing 2 (MICAL2). Indeed, MICAL2 modifies actin subunits and promotes actin filament turnover by severing them and preventing repolymerization. In this study, we found that MICAL2 increases during myogenic differentiation of adult and pluripotent stem cells (PSCs) towards skeletal, smooth and cardiac muscle cells and localizes in the nucleus of acute and chronic regenerating muscle fibers. In vivo delivery of Cas9–Mical2 guide RNA complexes results in muscle actin defects and demonstrates that MICAL2 is essential for skeletal muscle homeostasis and functionality. Conversely, MICAL2 upregulation shows a positive impact on skeletal and cardiac muscle commitments. 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell death & disease</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Giarratana, Nefele</au><au>Conti, Filippo</au><au>La Rovere, Rita</au><au>Gijsbers, Rik</au><au>Carai, Paolo</au><au>Duelen, Robin</au><au>Vervliet, Tim</au><au>Bultynck, Geert</au><au>Ronzoni, Flavio</au><au>Piciotti, Roberto</au><au>Costamagna, Domiziana</au><au>Fulle, Stefania</au><au>Barravecchia, Ivana</au><au>Angeloni, Debora</au><au>Torrente, Yvan</au><au>Sampaolesi, Maurilio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>MICAL2 is essential for myogenic lineage commitment</atitle><jtitle>Cell death & disease</jtitle><stitle>Cell Death Dis</stitle><addtitle>Cell Death Dis</addtitle><date>2020-08-18</date><risdate>2020</risdate><volume>11</volume><issue>8</issue><spage>654</spage><epage>654</epage><pages>654-654</pages><artnum>654</artnum><issn>2041-4889</issn><eissn>2041-4889</eissn><abstract>Contractile myofiber units are mainly composed of thick myosin and thin actin (F-actin) filaments. F-Actin interacts with Microtubule Associated Monooxygenase, Calponin And LIM Domain Containing 2 (MICAL2). Indeed, MICAL2 modifies actin subunits and promotes actin filament turnover by severing them and preventing repolymerization. In this study, we found that MICAL2 increases during myogenic differentiation of adult and pluripotent stem cells (PSCs) towards skeletal, smooth and cardiac muscle cells and localizes in the nucleus of acute and chronic regenerating muscle fibers. In vivo delivery of Cas9–Mical2 guide RNA complexes results in muscle actin defects and demonstrates that MICAL2 is essential for skeletal muscle homeostasis and functionality. Conversely, MICAL2 upregulation shows a positive impact on skeletal and cardiac muscle commitments. Taken together these data demonstrate that modulations of MICAL2 have an impact on muscle filament dynamics and its fine-tuned balance is essential for the regeneration of muscle tissues.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>32811811</pmid><doi>10.1038/s41419-020-02886-z</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0003-0904-1215</orcidid><orcidid>https://orcid.org/0000-0003-4557-9127</orcidid><orcidid>https://orcid.org/0000-0002-2422-3757</orcidid><orcidid>https://orcid.org/0000-0002-5968-4828</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 42/100 42/109 631/337 631/80/304 64 64/60 Actin Actin Cytoskeleton - metabolism Actin Cytoskeleton - physiology Actins - metabolism Actins - physiology Animals Antibodies Biochemistry Biomedical and Life Sciences Calponin Cardiac muscle Cell Biology Cell Culture Cell Differentiation - physiology Cytoskeletal Proteins - metabolism Cytoskeletal Proteins - physiology Cytoskeleton - metabolism Female Filaments Homeostasis Immunology Life Sciences Male Mice Mice, Inbred C57BL Monooxygenase Muscle contraction Muscle Contraction - physiology Muscle Development - physiology Muscle, Skeletal - metabolism Muscle, Smooth - physiology Myosin Myosins - metabolism Myosins - physiology Pluripotency Ribonucleic acid RNA Skeletal muscle Stem cells |
| title | MICAL2 is essential for myogenic lineage commitment |
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