The heavy chain has its day

regulation of myosin-II assembly

Research output: Contribution to journalArticle

38 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)77-85
Number of pages9
JournalBioarchitecture
Volume3
Issue number4
StatePublished - 2013
Externally publishedYes

Fingerprint

Myosin Type II
Actins
Myosin Heavy Chains
Cytoskeleton
Protein Isoforms
Motor Activity
Phosphorylation
Light

ASJC Scopus subject areas

  • Medicine(all)

Cite this

The heavy chain has its day : regulation of myosin-II assembly. / Dulianinova, Natalia; Bresnick, Anne R.

In: Bioarchitecture, Vol. 3, No. 4, 2013, p. 77-85.

Research output: Contribution to journalArticle

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