GMF as an Actin Network Remodeling Factor

Trends Cell Biol. 2018 Sep;28(9):749-760. doi: 10.1016/j.tcb.2018.04.008. Epub 2018 May 18.

Abstract

Glia maturation factor (GMF) has recently been established as a regulator of the actin cytoskeleton with a unique role in remodeling actin network architecture. Conserved from yeast to mammals, GMF is one of five members of the ADF-H family of actin regulatory proteins, which includes ADF/cofilin, Abp1/Drebrin, Twinfilin, and Coactosin. GMF does not bind actin, but instead binds the Arp2/3 complex with high affinity. Through this association, GMF catalyzes the debranching of actin filament networks and inhibits actin nucleation by Arp2/3 complex. Here, we discuss GMF's emerging role in controlling actin filament spatial organization and dynamics underlying cell motility, endocytosis, and other biological processes. Further, we attempt to reconcile these functions with its earlier characterization as a cell differentiation factor.

Keywords: ADF-H; Actin; Arp2/3 complex; cell motility; lamellipodia.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Actins / metabolism*
  • Amino Acid Sequence
  • Animals
  • Disease
  • Endocytosis
  • Glia Maturation Factor / chemistry
  • Glia Maturation Factor / metabolism*
  • Humans
  • Signal Transduction
  • Time Factors

Substances

  • Actins
  • Glia Maturation Factor