Key result
Removal or phosphomimetic mutation of a five-serine motif (1935-1941) in nonmuscle myosin II-B inhibited its assembly and ability to support front-back migratory cell polarization.
Identifies a key molecular determinant (serine 1935) that confers NMII isoform functional specificity in polarized migrating cells.
No immediate clinical impact; extends NMII-B isoform specificity in migration but leaves open cardiovascular relevance.
In this study, we show that the role of nonmuscle myosin II (NMII)-B in front-back migratory cell polarity is controlled by a short stretch of amino acids containing five serines (1935-1941). This motif resides near the junction between the C terminus helical and nonhelical tail domains. Removal of this motif inhibited NMII-B assembly, whereas its insertion into NMII-A endowed an NMII-B-like ability to generate large actomyosin bundles that determine the rear of the cell. Phosphomimetic mutation of the five serines also inhibited NMII-B assembly, rendering it unable to support front-back polarization. Mass spectrometric analysis showed that several of these serines are phosphorylated in live cells. Single-site mutagenesis showed that serine 1935 is a major regulatory site of NMII-B function. These data reveal a novel regulatory mechanism of NMII in polarized migrating cells by identifying a key molecular determinant that confers NMII isoform functional specificity.
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Juanes-García et al. (2015) studied this question. Mutation or removal of amino acids 1935-1941 in NMII-B vs. Wild-type NMII-B was evaluated on NMII-B assembly and front-back polarization. Removal or phosphomimetic mutation of a five-serine motif (1935-1941) in nonmuscle myosin II-B inhibited its assembly and ability to support front-back migratory cell polarization.
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