Myosin-IIA heavy chain phosphorylation on S1943 regulates tumor metastasis

Laura E. Norwood Toro, Yarong Wang, John S. Condeelis, Joan G. Jones, Jonathan M. Backer, Anne R. Bresnick

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

Nonmuscle myosin-IIA (NMHC-IIA) heavy chain phosphorylation has gained recognition as an important feature of myosin-II regulation. In previous work, we showed that phosphorylation on S1943 promotes myosin-IIA filament disassembly in vitro and enhances EGF-stimulated lamellipod extension of breast tumor cells. However, the contribution of NMHC-IIA S1943 phosphorylation to the modulation of invasive cellular behavior and metastasis has not been examined. Stable expression of phosphomimetic (S1943E) or non-phosphorylatable (S1943A) NMHC-IIA in breast cancer cells revealed that S1943 phosphorylation enhances invadopodia function, and is critical for matrix degradation in vitro and experimental metastasis in vivo. These studies demonstrate a novel link between NMHC-IIA S1943 phosphorylation, the regulation of extracellular matrix degradation and tumor cell invasion and metastasis.

Original languageEnglish (US)
Pages (from-to)273-282
Number of pages10
JournalExperimental Cell Research
Volume370
Issue number2
DOIs
StatePublished - Sep 15 2018

Keywords

  • Invadopodia
  • Invasion
  • Matrix degradation
  • Myosin-II
  • Phosphorylation

ASJC Scopus subject areas

  • Cell Biology

Fingerprint Dive into the research topics of 'Myosin-IIA heavy chain phosphorylation on S1943 regulates tumor metastasis'. Together they form a unique fingerprint.

  • Cite this