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A regulatory motif in nonmuscle myosin II-B regulates its role in migratory front-back polarity

AuthorsJuanes-García, Alba; Chapman, Jessica R.; Aguilar-Cuenca, Rocio; Delgado Arévalo, Cristina; Hodges, Jennifer; Whitmore, Leanna A.; Shabanowitz, Jeffrey; Hunt, Donald F.; Horwitz, Alan Rick; Vicente-Manzanares, Miguel
Issue Date2015
PublisherRockefeller University Press
CitationJournal of Cell Biology 209(1): 23-32 (2015)
AbstractIn 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.
Publisher version (URL)https://doi.org/10.1083/jcb.201407059
Identifiersdoi: 10.1083/jcb.201407059
e-issn: 1540-8140
issn: 0021-9525
Appears in Collections:(IBMCC) Artículos
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