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anti-Rat (Rattus) DIAPH1 Antibodies:
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Human Polyclonal DIAPH1 Primary Antibody for WB - ABIN153169
Minin, Kulik, Gyoeva, Li, Goshima, Gelfand: Regulation of mitochondria distribution by RhoA and formins. in Journal of cell science 2006
Show all 4 Pubmed References
Human Polyclonal DIAPH1 Primary Antibody for ICC, IF - ABIN153170
Jewett, Fischer, Mead, Hackstadt: Chlamydial TARP is a bacterial nucleator of actin. in Proceedings of the National Academy of Sciences of the United States of America 2006
Show all 2 Pubmed References
Human Polyclonal DIAPH1 Primary Antibody for IHC, IHC (p) - ABIN4305203
Goel, Sienkiewicz, Picciani, Lee, Bhattacharya: Cochlin induced TREK-1 co-expression and annexin A2 secretion: role in trabecular meshwork cell elongation and motility. in PLoS ONE 2011
We studied the interactions between actin and the FH2 domains of formins Cdc12, Bni1 and mDia1 to understand the factors underlying their different rates of polymerization. All-atom molecular dynamics simulations revealed two factors that influence actin filament elongation and correlate with the rates of elongation
The aim of this study was to investigate the role of DIAPH1 in the physiological response to experimental myocardial I/R in mice. After subjecting wild-type mice to experimental I/R, myocardial DIAPH1 expression was increased, an effect that was echoed following hypoxia/reoxygenation (H/R) in H9C2 and AC16 cells
what was seen for RhoC, mDia1 silencing through RNAi inhibited phagosome formation. Additionally, the coexpression of mDia1 with constitutively active mutant RhoC-G14V or expression of active mutant mDia1-DeltaN3 drastically inhibited the uptake of IgG-Es. These data suggest that RhoC modulates phagosome formation be modifying actin cytoskeletal remodeling via mDia1
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-DIAPH1 Signal Transduction.
Diaphanous-related formin signaling plays a role in heart and vascular development and the maintenance of SMC phenotype.
Liprin-alpha3 uses an alpha-helical region to bind to mDia1, counteracting mouse Dia1 activation by RhoA.
Depleting FMNL1, another Formin family member, resulted in reduced mDia1 expression, while RhoA inhibition did not alter mDia1 expression, which indicated that there was a FMNL1-mDia1-Profilin1 signaling pathway in mouse oocytes.
Mechanistically, mDia1 deficiency led to a downregulation of membrane-associated genes and a specific upregulation of CD14 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.
study examined how mDia functions in axon guidance in vivo and in vitro; findings show mDia plays multiple roles in the proper formation of the neural network
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 and Dia2 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.
Full-length mouse mDia1 (mDia1-FL) forms tightly autoinhibited dimers that can only be partially activated by RhoA.
mDia1 integrates oxidative and signal transduction pathways triggered, at least in part, by receptor for advanced glycation endproducts ligands, thereby regulating pathological neointimal expansion.
mDia1 and WAVE2 are important Src homology 3 domain partners of IRSp53 in forming filopodia.
The results of this study suggested that Rho signaling via mDia and ROCK critically regulates nuclear translocation through F-actin dynamics in tangential migration, whereas this mechanism is dispensable in radial migration.
Diaph1 is highly expressed in glioma, plays a significant role in glioma cell migration, and can influence the expression and activity of MMP2 and MMP9.
In the Title.
Data show that diaphanous related formin 1 protein (Dia1) and diaphanous related formin 2 protein (Dia2) facilitated HIV-1-induced microtubule (MT) stabilization and the intracellular motility of virus particles.
Down-regulation of mDia1 by infection with an adenovirus encoding siRNA or blockade of RAGE-mDia1 binding by transfection with RAGE mutant plasmids into HUVECs abolished these AGE-induced effects.
DIAPH1 mutation is associated with Progressive macrothrombocytopenia and hearing loss.
It is therefore noteworthy that we found DIAPH1 expression also in spiral ganglion neurons and in the barrier between the myelinating glia of the peripheral nervous system and oligodendrocytes that form the myelinating glia of the central nervous system (CNS).
mDia1 was recruited to the zonula adherens (ZA) of established Caco-2 monolayers in response to E-cadherin and RhoA.
Actin dynamics and formins control DNA replication by multiple direct and indirect mechanisms.
DIAPH1 interaction with the RAGE cytoplasmic domain. [review]
Ligand-induced association of RAGE 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(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)-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 protein.
mDia1 is an important regulator of breast cancer cell invasion and that its effects may be mediated by MMP-2 activity.
Findings suggest that regulation of cellular trafficking and microtubule-mediated localization of MT1-MMP 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 Arp2/3 complex in initiating lamellipodia and ruffles.
Capping protein and dia1 functionally coregulate filament barbed-end assembly.
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