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Nonmuscle myosin-IIA (NMHC-IIA) heavy chain phosphorylation has gained recognition as an important feature of myosin-II regulation. In previous work, we showed that phosphorylation on S1943 promotes myosin-IIA filament disassembly in vitro and enhances EGF-stimulated lamellipod extension of breast tumor cells. However, the contribution of NMHC-IIA S1943 phosphorylation to the modulation of invasive cellular behavior and metastasis has not been examined. Stable expression of phosphomimetic (S1943E) or non-phosphorylatable (S1943A) NMHC-IIA in breast cancer cells revealed that S1943 phosphorylation enhances invadopodia function, and is critical for matrix degradation in vitro and experimental metastasis in vivo. These studies demonstrate a novel link between NMHC-IIA S1943 phosphorylation, the regulation of extracellular matrix degradation and tumor cell invasion and metastasis. Copyright © 2018 Elsevier Inc. All rights reserved.


Laura E Norwood Toro, Yarong Wang, John S Condeelis, Joan G Jones, Jonathan M Backer, Anne R Bresnick. Myosin-IIA heavy chain phosphorylation on S1943 regulates tumor metastasis. Experimental cell research. 2018 Sep 15;370(2):273-282

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PMID: 29953877

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