期刊
JOURNAL OF CELL BIOLOGY
卷 209, 期 1, 页码 23-32出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201407059
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资金
- MINECO [SAF2011-24953]
- FP7 Marie Curie from the EU [CIG-293719]
- Ramon Areces Foundation [CIVP16A1831]
- Cell Migration Consortium [U54 GM64346]
- Ramon y Cajal Program [RYC-2010-06094]
- [GM 23244]
- [GM037537]
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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