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mDia induces circumferential actin filaments around the edge of the synaptic cleft, which contract the presynaptic terminals in a ROCK-dependent manner.
these results uncover a novel role for mDia1 in Abeta-mediated synaptotoxicity and demonstrate that inhibition of MT dynamics and accumulation of PTMs are driving factors for the induction of tau-mediated neuronal damage.
Small Molecule Inhibition of Ligand-Stimulated RAGE (zeige AGER Proteine)-DIAPH1 Signal Transduction.
Diaphanous-related formin (zeige DIAPH3 Proteine) signaling plays a role in heart and vascular development and the maintenance of SMC (zeige DYM Proteine) phenotype.
Liprin-alpha3 (zeige PPFIA3 Proteine) uses an alpha-helical region to bind to mDia1, counteracting mouse Dia1 (zeige CYB5R3 Proteine) activation by RhoA (zeige RHOA Proteine).
Depleting FMNL1 (zeige FMNL1 Proteine), another Formin (zeige FMN1 Proteine) family member, resulted in reduced mDia1 expression, while RhoA (zeige RHOA Proteine) inhibition did not alter mDia1 expression, which indicated that there was a FMNL1 (zeige FMNL1 Proteine)-mDia1-Profilin1 (zeige PFN1 Proteine) signaling pathway in mouse oocytes.
Mechanistically, mDia1 deficiency led to a downregulation of membrane-associated genes and a specific upregulation of CD14 (zeige CD14 Proteine) messenger RNA in granulocytes, but not in other lineages.
Mammalian diaphanous-related formin 1 regulates GSK3beta-dependent microtubule dynamics required for T cell migratory polarization.
mDia1 can efficiently put actin filaments under mechanical tension.
The active form of mDia1 localized to the apical membrane in exocrine pancreas cells; introduction of an active form of mDia1 leads to a marked increase in actin bundle density along the secretory vesicle lumen perimeter.
mDia1 was recruited to the zonula adherens (ZA) of established Caco-2 monolayers in response to E-cadherin (zeige CDH1 Proteine) and RhoA (zeige RHOA Proteine).
Actin dynamics and formins control DNA replication by multiple direct and indirect mechanisms.
DIAPH1 interaction with the RAGE (zeige AGER Proteine) cytoplasmic domain. [review]
Ligand-induced association of RAGE (zeige AGER Proteine) homodimers on the cell surface increases the molecular dimension of the receptor, recruiting DIAPH1 and activating signaling pathways.
The authors describe a novel patient-derived DIAPH1 mutation (c.3610C>T) in two unrelated families, which results in early termination prior to a basic amino acid motif (RRKR(1204-1207)) at the DAD C-terminus. The mutant DIA1 (zeige CYB5R3 Proteine)(R1204X) disrupted the autoinhibitory DID-DAD interaction and was constitutively active.
The description of a novel disorder of platelet formation and hearing loss extends the repertoire of DIAPH1-related disease, and provides new insight into the autoregulation of DIAPH1 activity.
Studies indicate that diaphanous related formin 1 (DIAPH1) is essentially involved in microtubules (MTs (zeige TIMM8A Proteine))-dependent early adhesion of colon cancer cells.
A 51-year-old patient in a Korean family with ADNSHL was examined by pure-tone audiometry, and genetic analysis of DIAPH1 was performed. A novel variant, p.I530S (c.1589T > G), was identified in the DIAPH1 gene, and the mutation was located in the highly conserved coiled-coil domain of the DIA1 (zeige CYB5R3 Proteine) protein.
mDia1 is an important regulator of breast cancer cell invasion and that its effects may be mediated by MMP-2 (zeige MMP2 Proteine) activity.
Findings suggest that regulation of cellular trafficking and microtubule-mediated localization of MT1-MMP (zeige MMP14 Proteine) by mDia1 is likely important in breast cancer invasion through the expression of cancer stem cell genes.
This gene is a homolog of the Drosophila diaphanous gene, and has been linked to autosomal dominant, fully penetrant, nonsyndromic sensorineural progressive low-frequency hearing loss. Actin polymerization involves proteins known to interact with diaphanous protein in Drosophila and mouse. It has therefore been speculated that this gene may have a role in the regulation of actin polymerization in hair cells of the inner ear. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
diaphanous homolog 1 (Drosophila)
, diaphanous homolog 1
, diaphanous homolog 2
, protein diaphanous homolog 1
, protein diaphanous homolog 1-like
, diaphanous-related formin-1