Regulation of cytoskeletal dynamics by actin-monomer-binding proteins.
The actin cytoskeleton is a vital component of several key cellular and developmental processes in eukaryotes. Many proteins that interact with filamentous and/or monomeric actin regulate the structure and dynamics of the actin cytoskeleton. Actin-filament-binding proteins control the nucleation, assembly, disassembly and crosslinking of actin filaments, whereas actin-monomer-binding proteins regulate the size, localization and dynamics of the large pool of unpolymerized actin in cells. In this article, we focus on recent advances in understanding how the six evolutionarily conserved actin-monomer-binding proteins - profilin, ADF/cofilin, twinfilin, Srv2/CAP, WASP/WAVE and verprolin/WIP - interact with actin monomers and regulate their incorporation into filament ends. We also present a model of how, together, these ubiquitous actin-monomer-binding proteins contribute to cytoskeletal dynamics and actin-dependent cellular processes.
Paavilainen
Ville O
VO
Program in Cellular Biotechnology, Institute of Biotechnology, PO Box 56, University of Helsinki, Helsinki 00014, Finland.
Bertling
Enni
E
Falck
Sandra
S
Lappalainen
Pekka
P
D000199:Actins / Q000502:physiology*; D000818:Animals; D003599:Cytoskeleton / Q000502:physiology*; D008840:Microfilament Proteins / Q000502:physiology*; D008954:Models, Biological; D017434:Protein Structure, Tertiary
D000199:Actins; D008840:Microfilament Proteins