Ontology highlight
ABSTRACT:
SUBMITTER: Kuhn S
PROVIDER: S-EPMC4432619 | biostudies-literature | 2015
REPOSITORIES: biostudies-literature
Kühn Sonja S Erdmann Constanze C Kage Frieda F Block Jennifer J Schwenkmezger Lisa L Steffen Anika A Rottner Klemens K Geyer Matthias M
Nature communications 20150512
Formins are actin polymerization factors that elongate unbranched actin filaments at the barbed end. Rho family GTPases activate Diaphanous-related formins through the relief of an autoregulatory interaction. The crystal structures of the N-terminal domains of human FMNL1 and FMNL2 in complex with active Cdc42 show that Cdc42 mediates contacts with all five armadillo repeats of the formin with specific interactions formed by the Rho-GTPase insert helix. Mutation of three residues within Rac1 res ...[more]