gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Diaphanous homolog 3

mDia2, DIAPH3, DRF3
Top mentioned proteins: Actin, cytochrome b5 reductase, Rhodopsin, RhoA, CAN
Papers using mDia2 antibodies
Correlative light and electron microscopy of the cytoskeleton of cultured cells
Pellman David, In PLoS Biology, 1997
... Full-length mDia2 was cloned into pEGFP-C1 vector (Clontech).
Papers on mDia2
Cell type-dependent mechanisms for formin-mediated assembly of filopodia.
Higgs et al., Hannover, Germany. In Mol Biol Cell, Jan 2016
We test this model using constitutively active constructs of two formins, FMNL3 and mDia2.
Small-molecule agonists of mammalian Diaphanous-related (mDia) formins reveal an effective glioblastoma anti-invasion strategy.
Eisenmann et al., Grand Rapids, United States. In Mol Biol Cell, Dec 2015
We used the formin inhibitor SMIFH2 and mDia agonists IMM-01/-02 and mDia2-DAD peptides, which disrupt autoinhibition, to examine the roles of mDia inactivation versus activation in GBM cell migration and invasion in vitro and in an ex vivo brain slice invasion model.
Functional hierarchy of redundant actin assembly factors revealed by fine-grained registration of intrinsic image fluctuations.
Danuser et al., Boston, United States. In Cell Syst, Aug 2015
Recruitment of Arp2/3, VASP, cofilin, and the formin mDia2 then promotes sustained exponential growth of the network.
Regulation of microtubule dynamics by DIAPH3 influences amoeboid tumor cell mechanics and sensitivity to taxanes.
Freeman et al., Los Angeles, United States. In Sci Rep, 2014
Here, we show that loss of Diaphanous-related formin-3 (DIAPH3), frequently associated with metastatic breast and prostate cancers, correlates with increased sensitivity to taxanes.
Small molecule inhibitor of formin homology 2 domains (SMIFH2) reveals the roles of the formin family of proteins in spindle assembly and asymmetric division in mouse oocytes.
Namgoong et al., South Korea. In Plos One, 2014
Knockdown of the mDia2 formins caused a similar decrease in oocyte maturation and abnormal spindle morphology, mimicking the phenotype of SMIFH2-treated cells.
Novel localization of formin mDia2: importin β-mediated delivery to and retention at the cytoplasmic side of the nuclear envelope.
Bershadsky et al., Singapore, Singapore. In Biol Open, 2014
Here, we show that Diaphanous-related formin-3 (mDia2) localizes to the cytoplasmic side of the nuclear envelope.
Rho GTPases in erythroid maturation.
Zheng et al., Cincinnati, United States. In Curr Opin Hematol, 2014
mDia2, a Rho effector known to play a role in enucleation, was also found essential for erythroblast cytokinesis as its deficiency in mice caused failure of primitive erythropoiesis and embryonic death.
An integrin-linked machinery of cytoskeletal regulation that enables experimental tumor initiation and metastatic colonization.
Weinberg et al., Cambridge, United States. In Cancer Cell, 2013
Recently extravasated metastatic cancer cells use the Rif/mDia2 actin-nucleating/polymerizing machinery in order to extend integrin β1-containing, filopodium-like protrusions (FLPs), which enable them to interact productively with the surrounding extracellular matrix; this process governs the initial proliferation of these cancer cells.
Mechanotransduction and YAP-dependent matrix remodelling is required for the generation and maintenance of cancer-associated fibroblasts.
Sahai et al., London, United Kingdom. In Nat Cell Biol, 2013
YAP regulates the expression of several cytoskeletal regulators, including ANLN and DIAPH3, and controls the protein levels of MYL9 (also known as MLC2).
Differing and isoform-specific roles for the formin DIAPH3 in plasma membrane blebbing and filopodia formation.
Fackler et al., Heidelberg, Germany. In Cell Res, 2012
isoform-selective actin assembly by DIAPH3 exerts specific and differentially regulated functions during cell adhesion and motility.
Differential interactions of the formins INF2, mDia1, and mDia2 with microtubules.
Higgs et al., Grenoble, France. In Mol Biol Cell, 2011
Microtubules strongly inhibit actin polymerization by mDia2.
Enhancement of mDia2 activity by Rho-kinase-dependent phosphorylation of the diaphanous autoregulatory domain.
Mack et al., Chapel Hill, United States. In Biochem J, 2011
Results indicate that ROCK-dependent phosphorylation of the mDia2 DAD is an important determinant of mDia2 activity and that this signalling mechanism affects actin polymerization and smooth muscle cell-specific gene expression.
Aurora B regulates formin mDia3 in achieving metaphase chromosome alignment.
Mao et al., New York City, United States. In Dev Cell, 2011
These findings reveal a key role for mDia3 and its regulation by Aurora B phosphorylation in achieving proper stable kinetochore microtubule attachment.
Mechanisms of plasma membrane targeting of formin mDia2 through its amino terminal domains.
Svitkina et al., Philadelphia, United States. In Mol Biol Cell, 2011
the amino terminus of mDia2 serves as a coincidence detection module, directing mDia2 to the plasma membrane through interactions with phospholipids and activated Rif
WAVE and Arp2/3 jointly inhibit filopodium formation by entering into a complex with mDia2.
Innocenti et al., Frankfurt am Main, Germany. In Nat Cell Biol, 2008
Results suggest that WAVE and the Arp2/3 complex jointly orchestrate different types of actin-based plasma membrane protrusions by promoting ruffling and inhibiting mDia2-induced filopodia.
Enucleation of cultured mouse fetal erythroblasts requires Rac GTPases and mDia2.
Lodish et al., Cambridge, United States. In Nat Cell Biol, 2008
Rac GTPases and their effector mDia2 have important roles in enucleation of mammalian erythroblasts
Filopodia are required for cortical neurite initiation.
Gertler et al., Cambridge, United States. In Nat Cell Biol, 2007
Here, we report that neuritogenesis in Ena/VASP-null neurons can be rescued by restoring filopodia formation through ectopic expression of the actin nucleating protein mDia2.
Podosome and sealing zone: specificity of the osteoclast model.
Destaing et al., Lyon, France. In Eur J Cell Biol, 2006
This process is repressed by an inhibitory pathway involving the GTPase Rho, its effector mDIA2 and the recently discovered tubulin deacetylase HDAC6.
Dispatch. GTPase signalling: new functions for Diaphanous-related formins.
Olson, Philadelphia, United States. In Curr Biol, 2003
Two recent reports have unveiled previously unappreciated activities of Drf3 (mDia2), eliciting cytoskeletal rearrangements at the behest of Cdc42, and of DRF2 (hDia2C), regulating endosome dynamics for RhoD.
RhoD, Src, and hDia2C in endosome motility.
Randazzo, Bethesda, United States. In Dev Cell, 2003
A recent report from Marino Zerial and colleagues examining RhoD identifies mDia2C, a novel splice variant of mDia2, and Src as components of the regulatory machinery influencing actin-dependent endosome movement.
share on facebooktweetadd +1mail to friends