Smooth Muscle Myosin Localizes at the Leading Edge and Regulates the Redistribution of Actin-regulatory Proteins during Migration
Airway smooth muscle cell migration plays an essential role in airway development, repair, and remodeling. Smooth muscle myosin II has been traditionally thought to localize in the cytoplasm solely and regulates cell migration by affecting stress fiber formation and focal adhesion assembly. In this...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-07-01
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| Series: | Cells |
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| Online Access: | https://www.mdpi.com/2073-4409/11/15/2334 |
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| author | Ruping Wang Eylon Arbel Dale D. Tang |
| author_facet | Ruping Wang Eylon Arbel Dale D. Tang |
| author_sort | Ruping Wang |
| collection | DOAJ |
| description | Airway smooth muscle cell migration plays an essential role in airway development, repair, and remodeling. Smooth muscle myosin II has been traditionally thought to localize in the cytoplasm solely and regulates cell migration by affecting stress fiber formation and focal adhesion assembly. In this study, we unexpectedly found that 20-kDa myosin light chain (MLC<sub>20</sub>) and myosin-11 (MYH11), important components of smooth muscle myosin, were present at the edge of lamellipodia. The knockdown of MLC<sub>20</sub> or MYH11 attenuated the recruitment of c-Abl, cortactinProfilin-1 (Pfn-1), and Abi1 to the cell edge. Moreover, myosin light chain kinase (MLCK) colocalized with integrin β1 at the tip of protrusion. The inhibition of MLCK attenuated the recruitment of c-Abl, cortactin, Pfn-1, and Abi1 to the cell edge. Furthermore, MLCK localization at the leading edge was reduced by integrin β1 knockdown. Taken together, our results demonstrate that smooth muscle myosin localizes at the leading edge and orchestrates the recruitment of actin-regulatory proteins to the tip of lamellipodia. Mechanistically, integrin β1 recruits MLCK to the leading edge, which catalyzes MLC<sub>20</sub> phosphorylation. Activated myosin regulates the recruitment of actin-regulatory proteins to the leading edge, and promotes lamellipodial formation and migration. |
| first_indexed | 2024-03-09T05:31:16Z |
| format | Article |
| id | doaj.art-5fe54e0e9cb1460ea11adfd18938ceee |
| institution | Directory Open Access Journal |
| issn | 2073-4409 |
| language | English |
| last_indexed | 2024-03-09T05:31:16Z |
| publishDate | 2022-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Cells |
| spelling | doaj.art-5fe54e0e9cb1460ea11adfd18938ceee2023-12-03T12:32:13ZengMDPI AGCells2073-44092022-07-011115233410.3390/cells11152334Smooth Muscle Myosin Localizes at the Leading Edge and Regulates the Redistribution of Actin-regulatory Proteins during MigrationRuping Wang0Eylon Arbel1Dale D. Tang2Department of Molecular and Cellular Physiology, Albany Medical College, Albany, New York, NY 12208, USADepartment of Molecular and Cellular Physiology, Albany Medical College, Albany, New York, NY 12208, USADepartment of Molecular and Cellular Physiology, Albany Medical College, Albany, New York, NY 12208, USAAirway smooth muscle cell migration plays an essential role in airway development, repair, and remodeling. Smooth muscle myosin II has been traditionally thought to localize in the cytoplasm solely and regulates cell migration by affecting stress fiber formation and focal adhesion assembly. In this study, we unexpectedly found that 20-kDa myosin light chain (MLC<sub>20</sub>) and myosin-11 (MYH11), important components of smooth muscle myosin, were present at the edge of lamellipodia. The knockdown of MLC<sub>20</sub> or MYH11 attenuated the recruitment of c-Abl, cortactinProfilin-1 (Pfn-1), and Abi1 to the cell edge. Moreover, myosin light chain kinase (MLCK) colocalized with integrin β1 at the tip of protrusion. The inhibition of MLCK attenuated the recruitment of c-Abl, cortactin, Pfn-1, and Abi1 to the cell edge. Furthermore, MLCK localization at the leading edge was reduced by integrin β1 knockdown. Taken together, our results demonstrate that smooth muscle myosin localizes at the leading edge and orchestrates the recruitment of actin-regulatory proteins to the tip of lamellipodia. Mechanistically, integrin β1 recruits MLCK to the leading edge, which catalyzes MLC<sub>20</sub> phosphorylation. Activated myosin regulates the recruitment of actin-regulatory proteins to the leading edge, and promotes lamellipodial formation and migration.https://www.mdpi.com/2073-4409/11/15/2334myosinleading edgemigrationsmooth muscleactin-associated proteins |
| spellingShingle | Ruping Wang Eylon Arbel Dale D. Tang Smooth Muscle Myosin Localizes at the Leading Edge and Regulates the Redistribution of Actin-regulatory Proteins during Migration Cells myosin leading edge migration smooth muscle actin-associated proteins |
| title | Smooth Muscle Myosin Localizes at the Leading Edge and Regulates the Redistribution of Actin-regulatory Proteins during Migration |
| title_full | Smooth Muscle Myosin Localizes at the Leading Edge and Regulates the Redistribution of Actin-regulatory Proteins during Migration |
| title_fullStr | Smooth Muscle Myosin Localizes at the Leading Edge and Regulates the Redistribution of Actin-regulatory Proteins during Migration |
| title_full_unstemmed | Smooth Muscle Myosin Localizes at the Leading Edge and Regulates the Redistribution of Actin-regulatory Proteins during Migration |
| title_short | Smooth Muscle Myosin Localizes at the Leading Edge and Regulates the Redistribution of Actin-regulatory Proteins during Migration |
| title_sort | smooth muscle myosin localizes at the leading edge and regulates the redistribution of actin regulatory proteins during migration |
| topic | myosin leading edge migration smooth muscle actin-associated proteins |
| url | https://www.mdpi.com/2073-4409/11/15/2334 |
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