dictyNews
Electronic Edition
Volume 44, number 11
April 13, 2018
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Abstracts
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14-3-3 proteins tune non-muscle myosin-II assembly
West-Foyle H, Kothari P, Osborne J, Robinson DN.
J. Biol. Chem, in press
The 14-3-3 family comprises a group of small proteins that are essential,
ubiquitous, and highly conserved across eukaryotes. Overexpression of
the 14-3-3s sigma, epsilon, zeta, and eta correlates with high metastatic
potential in multiple cancer types. In Dictyostelium, 14-3-3 promotes
myosin II turnover in the cell cortex and modulates cortical tension, cell
shape, and cytokinesis. In light of the important roles of 14-3-3 proteins
across a broad range of eukaryotic species, we sought to determine how
14-3-3 proteins interact with myosin II. Here, conducting in vitro and in
vivo studies of both Dictyostelium (one 14-3-3 and one myosin II) and
human proteins (seven 14-3-3s and three non-muscle myosin IIs), we
investigated the mechanism by which 14-3-3 proteins regulate myosin II
assembly. Using in vitro assembly assays with purified myosin II tail
fragments and 14-3-3, we demonstrate that this interaction is direct and
phosphorylation-independent. All seven human 14-3-3s also altered
assembly of at least one paralog of myosin II. Our findings indicate a
mechanism of myosin II assembly regulation that is mechanistically
conserved across a billion years of evolution from amoebas to humans.
We predict that altered 14-3-3 expression in humans inhibits the tumor
suppressor myosin II, contributing to the changes in cell mechanics
observed in many metastatic cancers.
submitted by: Doug Robinson [[log in to unmask]]
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