Myosin IIB assembly state determines its mechanosensitive dynamics.

Autor:	Schiffhauer ES; Department of Cell Biology, School of Medicine, Johns Hopkins University, Baltimore, MD., Ren Y; Department of Cell Biology, School of Medicine, Johns Hopkins University, Baltimore, MD., Iglesias VA; Department of Electrical and Computer Engineering, Whiting School of Engineering, Johns Hopkins University, Baltimore, MD., Kothari P; Department of Cell Biology, School of Medicine, Johns Hopkins University, Baltimore, MD., Iglesias PA; Department of Cell Biology, School of Medicine, Johns Hopkins University, Baltimore, MD.; Department of Electrical and Computer Engineering, Whiting School of Engineering, Johns Hopkins University, Baltimore, MD., Robinson DN; Department of Cell Biology, School of Medicine, Johns Hopkins University, Baltimore, MD dnr@jhmi.edu.; Department of Pharmacology and Molecular Sciences School of Medicine, Johns Hopkins University, Baltimore, MD.; Department of Medicine, School of Medicine, Johns Hopkins University, Baltimore, MD.; Department of Chemical and Biomolecular Engineering, Whiting School of Engineering, Johns Hopkins University, Baltimore, MD.
Jazyk:	angličtina
Zdroj:	The Journal of cell biology [J Cell Biol] 2019 Mar 04; Vol. 218 (3), pp. 895-908. Date of Electronic Publication: 2019 Jan 17.
DOI:	10.1083/jcb.201806058
Abstrakt:	Dynamical cell shape changes require a highly sensitive cellular system that can respond to chemical and mechanical inputs. Myosin IIs are key players in the cell's ability to react to mechanical inputs, demonstrating an ability to accumulate in response to applied stress. Here, we show that inputs that influence the ability of myosin II to assemble into filaments impact the ability of myosin to respond to stress in a predictable manner. Using mathematical modeling for Dictyostelium myosin II, we predict that myosin II mechanoresponsiveness will be biphasic with an optimum established by the percentage of myosin II assembled into bipolar filaments. In HeLa and NIH 3T3 cells, heavy chain phosphorylation of NMIIB by PKCζ, as well as expression of NMIIA, can control the ability of NMIIB to mechanorespond by influencing its assembly state. These data demonstrate that multiple inputs to the myosin II assembly state integrate at the level of myosin II to govern the cellular response to mechanical inputs. (© 2019 Schiffhauer et al.)
Databáze:	MEDLINE
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