AI Article Synopsis
- Plasma membrane-associated platforms (PMAPs) form in specific areas of the plasma membrane through scaffolds like ERC1 and Liprin-α1, and their assembly affects cell movement and invasion.
- Silencing the kinase DYRK3 in invasive breast cancer cells reduces their motility and capacity to invade, while increasing DYRK3 levels also impacts movement negatively.
- DYRK3 overexpression leads to less stable lamellipodia by increasing phosphorylation of Liprin-α1, indicating that a balance between DYRK3 and Liprin-α1 is necessary for cell stability and movement in tumors.
Article Abstract
Plasma membrane-associated platforms (PMAPs) form at specific sites of plasma membrane by scaffolds including ERC1 and Liprin-α1. We identify a mechanism regulating PMAPs assembly, with consequences on motility/invasion. Silencing Ser/Thr kinase DYRK3 in invasive breast cancer cells inhibits their motility and invasive capacity. Similar effects on motility were observed by increasing DYRK3 levels, while kinase-dead DYRK3 had limited effects. DYRK3 overexpression inhibits PMAPs formation and has negative effects on stability of lamellipodia and adhesions in migrating cells. Liprin-α1 depletion results in unstable lamellipodia and impaired cell motility. DYRK3 causes increased Liprin-α1 phosphorylation. Increasing levels of Liprin-α1 rescue the inhibitory effects of DYRK3 on cell spreading, suggesting that an equilibrium between Liprin-α1 and DYRK3 levels is required for lamellipodia stability and tumor cell motility. Our results show that DYRK3 is relevant to tumor cell motility, and identify a PMAP target of the kinase, highlighting a new mechanism regulating cell edge dynamics.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10952033 | PMC |
| http://dx.doi.org/10.1016/j.isci.2024.109440 | DOI Listing |
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