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The heavy chain has its day: regulation of myosin-II assembly.

ABSTRACT: Nonmuscle myosin-II is an actin-based motor that converts chemical energy into force and movement, and thus functions as a key regulator of the eukaryotic cytoskeleton. Although it is established that phosphorylation on the regulatory light chain increases the actin-activated MgATPase activity of the motor and promotes myosin-II filament assembly, studies have begun to characterize alternative mechanisms that regulate filament assembly and disassembly. These investigations have revealed that all three nonmuscle myosin-II isoforms are subject to additional regulatory controls, which impact diverse cellular processes. In this review, we discuss current knowledge on mechanisms that regulate the oligomerization state of nonmuscle myosin-II filaments by targeting the myosin heavy chain.

SUBMITTER: Dulyaninova NG

PROVIDER: S-EPMC4201608 | biostudies-literature | 2013 Jul-Aug

REPOSITORIES: biostudies-literature

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The heavy chain has its day: regulation of myosin-II assembly.

Dulyaninova Natalya G NG Bresnick Anne R AR

Bioarchitecture 20130701 4

Nonmuscle myosin-II is an actin-based motor that converts chemical energy into force and movement, and thus functions as a key regulator of the eukaryotic cytoskeleton. Although it is established that phosphorylation on the regulatory light chain increases the actin-activated MgATPase activity of the motor and promotes myosin-II filament assembly, studies have begun to characterize alternative mechanisms that regulate filament assembly and disassembly. These investigations have revealed that all ...[more]

PMID: 24002531

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