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Non-muscle myosin 2 filaments are processive in cells
Directed transport of cellular components is often dependent on the processive movements of cytoskeletal motors. Myosin 2 motors predominantly engage actin filaments of opposing orientation to drive contractile events, and are therefore not traditionally viewed as processive. However, recent in vitr...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9980172/ https://www.ncbi.nlm.nih.gov/pubmed/36865321 http://dx.doi.org/10.1101/2023.02.24.529920 |
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author | Vitriol, Eric A. Quintanilla, Melissa A. Tidei, Joseph J. Troughton, Lee D. Cody, Abigail Cisterna, Bruno A. Jane, Makenzie L. Oakes, Patrick W. Beach, Jordan R. |
author_facet | Vitriol, Eric A. Quintanilla, Melissa A. Tidei, Joseph J. Troughton, Lee D. Cody, Abigail Cisterna, Bruno A. Jane, Makenzie L. Oakes, Patrick W. Beach, Jordan R. |
author_sort | Vitriol, Eric A. |
collection | PubMed |
description | Directed transport of cellular components is often dependent on the processive movements of cytoskeletal motors. Myosin 2 motors predominantly engage actin filaments of opposing orientation to drive contractile events, and are therefore not traditionally viewed as processive. However, recent in vitro experiments with purified non-muscle myosin 2 (NM2) demonstrated myosin 2 filaments could move processively. Here, we establish processivity as a cellular property of NM2. Processive runs in central nervous system-derived CAD cells are most apparent as processive movements on bundled actin in protrusions that terminate at the leading edge. We find that processive velocities in vivo are consistent with in vitro measurements. NM2 makes these processive runs in its filamentous form against lamellipodia retrograde flow, though anterograde movement can still occur in the absence of actin dynamics. Comparing the processivity of NM2 isoforms, we find that NM2A moves slightly faster than NM2B. Finally, we demonstrate that this is not a cell-specific property, as we observe processive-like movements of NM2 in the lamella and subnuclear stress fibers of fibroblasts. Collectively, these observations further broaden NM2 functionality and the biological processes in which the already ubiquitous motor can contribute. |
format | Online Article Text |
id | pubmed-9980172 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Cold Spring Harbor Laboratory |
record_format | MEDLINE/PubMed |
spelling | pubmed-99801722023-03-03 Non-muscle myosin 2 filaments are processive in cells Vitriol, Eric A. Quintanilla, Melissa A. Tidei, Joseph J. Troughton, Lee D. Cody, Abigail Cisterna, Bruno A. Jane, Makenzie L. Oakes, Patrick W. Beach, Jordan R. bioRxiv Article Directed transport of cellular components is often dependent on the processive movements of cytoskeletal motors. Myosin 2 motors predominantly engage actin filaments of opposing orientation to drive contractile events, and are therefore not traditionally viewed as processive. However, recent in vitro experiments with purified non-muscle myosin 2 (NM2) demonstrated myosin 2 filaments could move processively. Here, we establish processivity as a cellular property of NM2. Processive runs in central nervous system-derived CAD cells are most apparent as processive movements on bundled actin in protrusions that terminate at the leading edge. We find that processive velocities in vivo are consistent with in vitro measurements. NM2 makes these processive runs in its filamentous form against lamellipodia retrograde flow, though anterograde movement can still occur in the absence of actin dynamics. Comparing the processivity of NM2 isoforms, we find that NM2A moves slightly faster than NM2B. Finally, we demonstrate that this is not a cell-specific property, as we observe processive-like movements of NM2 in the lamella and subnuclear stress fibers of fibroblasts. Collectively, these observations further broaden NM2 functionality and the biological processes in which the already ubiquitous motor can contribute. Cold Spring Harbor Laboratory 2023-02-26 /pmc/articles/PMC9980172/ /pubmed/36865321 http://dx.doi.org/10.1101/2023.02.24.529920 Text en https://creativecommons.org/licenses/by-nc-nd/4.0/This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (https://creativecommons.org/licenses/by-nc-nd/4.0/) , which allows reusers to copy and distribute the material in any medium or format in unadapted form only, for noncommercial purposes only, and only so long as attribution is given to the creator. |
spellingShingle | Article Vitriol, Eric A. Quintanilla, Melissa A. Tidei, Joseph J. Troughton, Lee D. Cody, Abigail Cisterna, Bruno A. Jane, Makenzie L. Oakes, Patrick W. Beach, Jordan R. Non-muscle myosin 2 filaments are processive in cells |
title | Non-muscle myosin 2 filaments are processive in cells |
title_full | Non-muscle myosin 2 filaments are processive in cells |
title_fullStr | Non-muscle myosin 2 filaments are processive in cells |
title_full_unstemmed | Non-muscle myosin 2 filaments are processive in cells |
title_short | Non-muscle myosin 2 filaments are processive in cells |
title_sort | non-muscle myosin 2 filaments are processive in cells |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9980172/ https://www.ncbi.nlm.nih.gov/pubmed/36865321 http://dx.doi.org/10.1101/2023.02.24.529920 |
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