2017
DOI: 10.1016/j.yexcr.2017.05.014
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Non diaphanous formin delphilin acts as a barbed end capping protein

Abstract: Formins are multi domain proteins present ubiquitously in all eukaryotes from lower fungi to higher vertebrates. Formins are characterized by the presence of formin homology domain-2 (FH2) and formin homology domain-1 (FH1). There are fifteen different formins present in mouse and human. Among these metazoan formins, Delphilin is a unique formin having two PDZ domains at the N-terminus and FH1, FH2 domain at the C-terminus respectively. In this study we observed that Delphilin binds to actin filaments, and Del… Show more

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Cited by 12 publications
(20 citation statements)
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“…Consistent with weak side binding, at saturation only one mDelFFC dimer was bound per 20 actin monomers. Another group reported much tighter binding ( Dutta et al. , 2017 ).…”
Section: Resultsmentioning
confidence: 99%
“…Consistent with weak side binding, at saturation only one mDelFFC dimer was bound per 20 actin monomers. Another group reported much tighter binding ( Dutta et al. , 2017 ).…”
Section: Resultsmentioning
confidence: 99%
“…However, in control experiments without actin, LmForminA and LmForminB proteins remained in the supernatant fraction (fig.3A, B, respectively). Results indicate that LmForminA and LmForminB protein have an F-actin binding ability in the in vitro condition with the FH2 domain similar to other well-characterized formins(Shimada et al, 2004;Dutta et al, 2017).The dissociation constant of LmForminA and LmForminB binds with F-actin actin were determined by analyzing the SDS-PAGE gel of co-sedimentation assay. The fraction of bound LmFormins with F-actin curve fitting shows the KD value 1.84 µM and 0.2 µM for LmForminA and LmForminB, respectively (fig.S5C, D).…”
mentioning
confidence: 84%
“…Post-harvest cells were resuspended in the lysis buffer (50 mM Tris-Cl pH 8.0, 100 mM NaCl, 30 mM Imidazole pH 8.0, 1 mM DTT, 0.2% IGEPAL (Sigma-Aldrich), 0.2% Thesit (Sigma-Aldrich), protease inhibitor cocktail followed by sonication (1 minute’s pulse with 5 second interval) and centrifuged at 12,000 rpm for 15 minutes. 50% Ni-NTA beads (Qiagen) were added with the supernatant, then washed with wash buffer (50 mM Tris-Cl pH 8.0, 100 mM NaCl, 30 mM imidazole pH 8.0) and eluted with elution buffer (50 mM Tris-Cl pH 8.0, 100 mM NaCl, 300Mm imidazole pH 8.0 pH 8.0 and 5% glycerol (Sigma-Aldrich) (Dutta et al, 2017). Purified protein dialysis in TNEG5 buffer (20 mM Tris pH 8.0, 100 mM NaCl, 1 mM EDTA, 5% Glycerol) at 4 °C.…”
Section: Experimental Methodsmentioning
confidence: 99%
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“…The rate of subunit addition mediated by a formin is thus dictated by the probability that an incoming actin monomer will find the FH2-barbed end complex in an open conformation, a property known as the Bgating factor ( Vavylonis et al 2006). The extent to which an FH2 dimer gates elongation varies widely among formin isoforms: FH2 dimers of the Schizosaccharomyces pombe formin Cdc12p and the mammalian formin Delphilin inhibit elongation by approximately 99% (Dutta et al 2017;Kovar et al 2003Kovar et al , 2006Silkworth et al 2018), suggesting that these formins strongly favor a closed conformation, whereas mouse mDia1 slows elongation only modestly (i.e., by about 5-10%), indicating that its FH2 domain frequently populates an open conformation (Kovar et al 2006). The equilibrium between open and closed conformations is formin-specific, and FH2 dimers from other formins produce intermediate effects on elongation (Gurel et al 2015;Kovar et al 2006;Thompson et al 2013).…”
Section: Actin Filament Assembly Mediated By Fh2 Domainsmentioning
confidence: 99%