Format

Send to

Choose Destination
See comment in PubMed Commons below
Small GTPases. 2014;5:e29513. doi: 10.4161/sgtp.29513. Epub 2014 Jun 10.

Formins as effector proteins of Rho GTPases.

Author information

1
Center of Advanced European Studies and Research (caesar); Group Physical Biochemistry; Bonn, Germany.

Abstract

Formin proteins were recognized as effectors of Rho GTPases some 15 years ago. They contribute to different cellular actin cytoskeleton structures by their ability to polymerize straight actin filaments at the barbed end. While not all formins necessarily interact with Rho GTPases, a subgroup of mammalian formins, termed Diaphanous-related formins or DRFs, were shown to be activated by small GTPases of the Rho superfamily. DRFs are autoinhibited in the resting state by an N- to C-terminal interaction that renders the central actin polymerization domain inactive. Upon the interaction with a GTP-bound Rho, Rac, or Cdc42 GTPase, the C-terminal autoregulation domain is displaced from its N-terminal recognition site and the formin becomes active to polymerize actin filaments. In this review we discuss the current knowledge on the structure, activation, and function of formin-GTPase interactions for the mammalian formin families Dia, Daam, FMNL, and FHOD. We describe both direct and indirect interactions of formins with GTPases, which lead to formin activation and cytoskeletal rearrangements. The multifaceted function of formins as effector proteins of Rho GTPases thus reflects the diversity of the actin cytoskeleton in cells.

KEYWORDS:

Cdc42; Daam1; Daam2; FHOD1; FHOD3; FMNL1; FMNL2; FMNL3; ROCK; Rac; Rho; filopodia; formin; lamellipodium; mDia1; mDia2; mDia3; stress fiber

PMID:
24914801
PMCID:
PMC4111664
DOI:
10.4161/sgtp.29513
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Taylor & Francis Icon for PubMed Central
    Loading ...
    Support Center