| Literature DB >> 34314591 |
Marina Garrido-Casado1, Gloria Asensio-Juárez1, Miguel Vicente-Manzanares1.
Abstract
Nonmuscle myosin II (NMII) is a multimeric protein complex that generates most mechanical force in eukaryotic cells. NMII function is controlled at three main levels. The first level includes events that trigger conformational changes that extend the complex to enable its assembly into filaments. The second level controls the ATPase activity of the complex and its binding to microfilaments in extended NMII filaments. The third level includes events that modulate the stability and contractility of the filaments. They all work in concert to finely control force generation inside cells. NMII is a common endpoint of mechanochemical signaling pathways that control cellular responses to physical and chemical extracellular cues. Specific phosphorylations modulate NMII activation in a context-dependent manner. A few kinases control these phosphorylations in a spatially, temporally, and lineage-restricted fashion, enabling functional adaptability to the cellular microenvironment. Here, we review mechanisms that control NMII activity in the context of cell migration and division.Entities:
Keywords: division; force; kinase; migration; motility; myosin II
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Year: 2021 PMID: 34314591 DOI: 10.1146/annurev-cellbio-042721-105528
Source DB: PubMed Journal: Annu Rev Cell Dev Biol ISSN: 1081-0706 Impact factor: 13.827