Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The regulation of mDia1 by autoinhibition and its release by Rho*GTP.

The EMBO journal - 7 Dec 2005

Lammers Michael, Rose Rolf, Scrima Andrea, Wittinghofer Alfred

Abstract excerpt

Formins induce the nucleation and polymerisation of unbranched actin filaments via the formin-homology domains 1 and 2. Diaphanous-related formins (Drfs) are regulated by a RhoGTPase-binding domain situated in the amino-terminal (N-terminal) region and a carboxy-terminal Diaphanous-autoregulatory domain (DAD), whose interaction stabilises an autoinhibited inactive conformation. Binding of active Rho releases DAD...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding Sites
Share to Carrier Proteins
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Mutational Analysis

Share to Formins

Share to Guanosine Triphosphate

Share to Protein Structure, Tertiary

Share to rho GTP-Binding Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 16292343
DOI: 10.1038/sj.emboj.7600879
PMCID: PMC1356318

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The regulation of mDia1 by autoinhibition and its release by Rho*GTP.PMID 16292343Read ↗

Structural and mechanistic insights into the interaction between Rho and mammalian Dia.Semantic proximity Read ↗

Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1.Semantic proximity Read ↗

Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain.Semantic proximity Read ↗

Mechanism of activation of the Formin protein Daam1.Semantic proximity Read ↗

On the mechanism of autoinhibition of the RhoA-specific nucleotide exchange factor PDZRhoGEF.Semantic proximity Read ↗

Positive feedback between Dia1, LARG, and RhoA regulates cell morphology and invasion.Semantic proximity Read ↗

[New targets of rho GTPases, mDia and Bnilp, and formin homology protein family].Semantic proximity Read ↗

Uncoupling of inhibitory and shuttling functions of rho GDP dissociation inhibitors.Semantic proximity Read ↗

Rho activation of mDia formins is modulated by an interaction with inverted formin 2 (INF2).Semantic proximity Read ↗

Structure of the FH2 domain of Daam1: implications for formin regulation of actin assembly.Semantic proximity Read ↗

Autoinhibition regulates cellular localization and actin assembly activity of the diaphanous-related formins FRLalpha and mDia1.Semantic proximity Read ↗

Crystal structure of the GTPase domain of rat dynamin 1.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.