A regulatory motif in nonmuscle myosin II-B regulates its role in migratory front-back polarity.
J Cell Biol
; 209(1): 23-32, 2015 Apr 13.
Article
em En
| MEDLINE
| ID: mdl-25869664
ABSTRACT
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Polaridade Celular
/
Cadeias Pesadas de Miosina
/
Miosina não Muscular Tipo IIB
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article