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

Dia-interacting protein modulates formin-mediated actin assembly at the cell cortex.

Current biology : CB - 3 Apr 2007

Eisenmann Kathryn M, Harris Elizabeth S, Kitchen Susan M, Holman Holly A, Higgs Henry N, Alberts Arthur S

Abstract excerpt

BACKGROUND: Mammalian Diaphanous (mDia)-related formins and the N-WASP-activated Arp2/3 complex initiate the assembly of filamentous actin. Dia-interacting protein (DIP) binds via its amino-terminal SH3 domain to the proline-rich formin homology 1 (FH1) domain of mDia1 and mDia2 and to the N-WASp proline-rich region. RESULTS: Here, we investigated an interaction between a conserved leucine-rich region (LRR) in...

Read the complete abstract on PubMed

Topics

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

Share to Actin Cytoskeleton
Share to Actin-Related Protein 2-3 Complex

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Actins

Share to cdc42 GTP-Binding Protein

Share to Formins

Share to Muscle Proteins

Share to Pseudopodia

Share to RNA, Small Interfering

Source

Identifiers

PMID: 17398099
DOI: 10.1016/j.cub.2007.03.024

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dia-interacting protein modulates formin-mediated actin assembly at the cell cortex.PMID 17398099Read ↗

Formin’ cellular structuresSemantic proximity Read ↗

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

Dia1 and IQGAP1 interact in cell migration and phagocytic cup formation.Semantic proximity Read ↗

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

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

Mammalian diaphanous-related formin Dia1 controls the organization of E-cadherin-mediated cell-cell junctionsSemantic proximity Read ↗

The activities of the C-terminal regions of the formin protein disheveled-associated activator of morphogenesis (DAAM) in actin dynamics.Semantic proximity Read ↗

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

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

Diaphanous regulates myosin and adherens junctions to control cell contractility and protrusive behavior during morphogenesis.Semantic proximity Read ↗

Functions of actin-interacting protein 1 (AIP1)/WD repeat protein 1 (WDR1) in actin filament dynamics and cytoskeletal regulation.Semantic proximity Read ↗

Mechanisms of plasma membrane targeting of formin mDia2 through its amino terminal domainsSemantic proximity Read ↗

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