Actin-filament disassembly: it takes two to shrink them fast

Moritz Winterhoff; Jan Faix

doi:10.1016/j.cub.2015.04.050

Actin-filament disassembly: it takes two to shrink them fast

Curr Biol. 2015 Jun 1;25(11):R450-2. doi: 10.1016/j.cub.2015.04.050.

Authors

Moritz Winterhoff¹, Jan Faix²

Affiliations

¹ Institute for Biophysical Chemistry, Hannover Medical School, Carl-Neuberg Str. 1, 30625 Hannover, Germany.
² Institute for Biophysical Chemistry, Hannover Medical School, Carl-Neuberg Str. 1, 30625 Hannover, Germany. Electronic address: [email protected].

PMID: 26035785
DOI: 10.1016/j.cub.2015.04.050

Abstract

Actin-filament disassembly is indispensable for replenishing the pool of polymerizable actin and allows continuous dynamic remodelling of the actin cytoskeleton. A new study now reveals that ADF/cofilin preferentially dismantles branched networks and provides new insights into the collaborative work of ADF/cofilin and Aip1 on filament disassembly at the molecular level.

MeSH terms

Actin Cytoskeleton / metabolism*
Actin Depolymerizing Factors / metabolism*
Microfilament Proteins / metabolism*

Substances

Actin Depolymerizing Factors
Microfilament Proteins
actin interacting protein 1