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Small Molecule Inhibition of Ligand-Stimulated RAGE (show AGER ELISA Kits)-DIAPH1 Signal Transduction.
Diaphanous-related formin (show DIAPH3 ELISA Kits) signaling plays a role in heart and vascular development and the maintenance of SMC (show DYM ELISA Kits) phenotype.
Liprin-alpha3 (show PPFIA3 ELISA Kits) uses an alpha-helical region to bind to mDia1, counteracting mouse Dia1 (show CYB5R3 ELISA Kits) activation by RhoA (show RHOA ELISA Kits).
Depleting FMNL1 (show FMNL1 ELISA Kits), another Formin (show FMN1 ELISA Kits) family member, resulted in reduced mDia1 expression, while RhoA (show RHOA ELISA Kits) inhibition did not alter mDia1 expression, which indicated that there was a FMNL1 (show FMNL1 ELISA Kits)-mDia1-Profilin1 (show PFN1 ELISA Kits) signaling pathway in mouse oocytes.
Mechanistically, mDia1 deficiency led to a downregulation of membrane-associated genes and a specific upregulation of CD14 (show CD14 ELISA Kits) 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.
Dia1 (show CYB5R3 ELISA Kits) and Dia2 (show DIAPH3 ELISA Kits) are dynamic components of meiotic spindle and pole complex during meiotic maturation of oocytes.
Actin-capping protein is a novel regulator of microtubule stability that functions by antagonizing mDia1 activity toward actin filaments.
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 (show CYB5R3 ELISA Kits) protein.
mDia1 is an important regulator of breast cancer cell invasion and that its effects may be mediated by MMP-2 (show MMP2 ELISA Kits) activity.
Findings suggest that regulation of cellular trafficking and microtubule-mediated localization of MT1-MMP (show MMP14 ELISA Kits) by mDia1 is likely important in breast cancer invasion through the expression of cancer stem cell genes.
Loss-of-function variants in DIAPH1 is associated with syndromic microcephaly, blindness, and early onset seizures.
functional complementation experiments and optogenetics to show that mDia1 cooperates with the Arp2 (show ACTR2 ELISA Kits)/3 complex in initiating lamellipodia and ruffles.
Capping protein and dia1 (show CYB5R3 ELISA Kits) functionally coregulate filament barbed-end assembly.
mDia1 displaced from the barbed end by CapZ Actin Capping Protein can randomly slide along the actin filament and later return.
Data indicate that diaphanous homolog 1 (Drosophila) protein (DIAPH1) stabilizes microtubules and reduces microtubule dynamics.
Patients with a homozygous nonsense DIAPH1 alteration (p.Gln778*) have MCP (show CD46 ELISA Kits) as well as reduced height and weight.
the RhoA (show RHOA ELISA Kits)-regulated formin (show FMN1 ELISA Kits) Dia1 (show CYB5R3 ELISA Kits) is involved in entosis downstream of LPAR2 (show LPAR2 ELISA Kits)
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