Does the Actin Network Architecture Leverage Myosin-I Functions?
The actin cytoskeleton plays crucial roles in cell morphogenesis and functions. The main partners of cortical actin are molecular motors of the myosin superfamily. Although our understanding of myosin functions is heavily based on myosin-II and its ability to dimerize, the largest and most ancient c...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-06-01
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| Series: | Biology |
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| Online Access: | https://www.mdpi.com/2079-7737/11/7/989 |
| _version_ | 1797433801489514496 |
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| author | Julien Pernier Kristine Schauer |
| author_facet | Julien Pernier Kristine Schauer |
| author_sort | Julien Pernier |
| collection | DOAJ |
| description | The actin cytoskeleton plays crucial roles in cell morphogenesis and functions. The main partners of cortical actin are molecular motors of the myosin superfamily. Although our understanding of myosin functions is heavily based on myosin-II and its ability to dimerize, the largest and most ancient class is represented by myosin-I. Class 1 myosins are monomeric, actin-based motors that regulate a wide spectrum of functions, and whose dysregulation mediates multiple human diseases. We highlight the current challenges in identifying the “pantograph” for myosin-I motors: we need to reveal how conformational changes of myosin-I motors lead to diverse cellular as well as multicellular phenotypes. We review several mechanisms for scaling, and focus on the (re-) emerging function of class 1 myosins to remodel the actin network architecture, a higher-order dynamic scaffold that has potential to leverage molecular myosin-I functions. Undoubtfully, understanding the molecular functions of myosin-I motors will reveal unexpected stories about its big partner, the dynamic actin cytoskeleton. |
| first_indexed | 2024-03-09T10:21:51Z |
| format | Article |
| id | doaj.art-03779f775618496f992bb169e0d68cf1 |
| institution | Directory Open Access Journal |
| issn | 2079-7737 |
| language | English |
| last_indexed | 2024-03-09T10:21:51Z |
| publishDate | 2022-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biology |
| spelling | doaj.art-03779f775618496f992bb169e0d68cf12023-12-01T21:54:21ZengMDPI AGBiology2079-77372022-06-0111798910.3390/biology11070989Does the Actin Network Architecture Leverage Myosin-I Functions?Julien Pernier0Kristine Schauer1Institute for Integrative Biology of the Cell (I2BC), Centre National de la Recherche Scientifique (CNRS), Commissariat à L’Énergie Atomique et aux Énergies Alternatives (CEA), Université Paris-Saclay, 91198 Gif-sur-Yvette, FranceTumor Cell Dynamics Unit, Inserm U1279, Gustave Roussy Institute, Université Paris-Saclay, 94800 Villejuif, FranceThe actin cytoskeleton plays crucial roles in cell morphogenesis and functions. The main partners of cortical actin are molecular motors of the myosin superfamily. Although our understanding of myosin functions is heavily based on myosin-II and its ability to dimerize, the largest and most ancient class is represented by myosin-I. Class 1 myosins are monomeric, actin-based motors that regulate a wide spectrum of functions, and whose dysregulation mediates multiple human diseases. We highlight the current challenges in identifying the “pantograph” for myosin-I motors: we need to reveal how conformational changes of myosin-I motors lead to diverse cellular as well as multicellular phenotypes. We review several mechanisms for scaling, and focus on the (re-) emerging function of class 1 myosins to remodel the actin network architecture, a higher-order dynamic scaffold that has potential to leverage molecular myosin-I functions. Undoubtfully, understanding the molecular functions of myosin-I motors will reveal unexpected stories about its big partner, the dynamic actin cytoskeleton.https://www.mdpi.com/2079-7737/11/7/989actinmyosin-Imonomeric motormechanical transductionmembrane tensioncholesterol transport |
| spellingShingle | Julien Pernier Kristine Schauer Does the Actin Network Architecture Leverage Myosin-I Functions? Biology actin myosin-I monomeric motor mechanical transduction membrane tension cholesterol transport |
| title | Does the Actin Network Architecture Leverage Myosin-I Functions? |
| title_full | Does the Actin Network Architecture Leverage Myosin-I Functions? |
| title_fullStr | Does the Actin Network Architecture Leverage Myosin-I Functions? |
| title_full_unstemmed | Does the Actin Network Architecture Leverage Myosin-I Functions? |
| title_short | Does the Actin Network Architecture Leverage Myosin-I Functions? |
| title_sort | does the actin network architecture leverage myosin i functions |
| topic | actin myosin-I monomeric motor mechanical transduction membrane tension cholesterol transport |
| url | https://www.mdpi.com/2079-7737/11/7/989 |
| work_keys_str_mv | AT julienpernier doestheactinnetworkarchitectureleveragemyosinifunctions AT kristineschauer doestheactinnetworkarchitectureleveragemyosinifunctions |