| A Protumorigenic mDia2-MIRO1 Axis Controls Mitochondrial Positioning and Function in Cancer-Associated Fibroblasts. | A Protumorigenic mDia2-MIRO1 Axis Controls Mitochondrial Positioning and Function in Cancer-Associated Fibroblasts.
Cangkrama M, Liu H, Whipman J, Zubair M, Matsushita M, Di Filippo M, Kopf M, Innocenti M, Werner S., Free PMC Article | 10/22/2022 |
| DIAPH3 deficiency links microtubules to mitotic errors, defective neurogenesis, and brain dysfunction. | DIAPH3 deficiency links microtubules to mitotic errors, defective neurogenesis, and brain dysfunction.
Lau EO, Damiani D, Chehade G, Ruiz-Reig N, Saade R, Jossin Y, Aittaleb M, Schakman O, Tajeddine N, Gailly P, Tissir F., Free PMC Article | 10/30/2021 |
| A paracrine activin A-mDia2 axis promotes squamous carcinogenesis via fibroblast reprogramming. | A paracrine activin A-mDia2 axis promotes squamous carcinogenesis via fibroblast reprogramming.
Cangkrama M, Wietecha M, Mathis N, Okumura R, Ferrarese L, Al-Nuaimi D, Antsiferova M, Dummer R, Innocenti M, Werner S., Free PMC Article | 07/31/2021 |
| neuronal drebrin A directly interacts with mDia2 formin. | Neuronal drebrin A directly interacts with mDia2 formin to inhibit actin assembly.
Ginosyan AA, Grintsevich EE, Reisler E., Free PMC Article | 06/29/2019 |
| The authors report that formins mDia1 and mDia2 dissociate faster under higher ionic strength and when actin concentration is increased. Profilin, known to increase the elongation rate of formin-associated filaments, surprisingly decreases the formin dissociation rate, by bringing formin FH1 domains in transient contact with the barbed end. | Modulation of formin processivity by profilin and mechanical tension.
Cao L, Kerleau M, Suzuki EL, Wioland H, Jouet S, Guichard B, Lenz M, Romet-Lemonne G, Jegou A., Free PMC Article | 05/4/2019 |
| These data identify Diaph3 as a major guard of cortical progenitors, unravel novel functions of Diaphanous formins and add insights into the pathobiology of microcephaly. | Lack of Diaph3 relaxes the spindle checkpoint causing the loss of neural progenitors.
Damiani D, Goffinet AM, Alberts A, Tissir F., Free PMC Article | 09/1/2018 |
| mDia2 is regulated through acetylation and deacetylation at lysine 970 in the formin homology 2 domain | Histone deacetylase 6 regulates cytokinesis and erythrocyte enucleation through deacetylation of formin protein mDia2.
Li X, Mei Y, Yan B, Vitriol E, Huang S, Ji P, Qiu Y., Free PMC Article | 03/17/2018 |
| findings add more complexity to the mDia2 activity cycle by showing that the open conformation may control actin dynamics also through actin-independent regulation of the proteasome | Quantitative Proteomics Illuminates a Functional Interaction between mDia2 and the Proteasome.
Isogai T, van der Kammen R, Bleijerveld OB, Goerdayal SS, Argenzio E, Altelaar AF, Innocenti M. | 11/4/2017 |
| Ineffective erythropoiesis caused by binucleated late-stage erythroblasts in mDia2 hematopoietic specific knockout mice. | Ineffective erythropoiesis caused by binucleated late-stage erythroblasts in mDia2 hematopoietic specific knockout mice.
Mei Y, Zhao B, Yang J, Gao J, Wickrema A, Wang D, Chen Y, Ji P., Free PMC Article | 10/8/2016 |
| the interactome of auto-inhibited and constitutively active mDia2, is reported. | Proteomic analyses uncover a new function and mode of action for mouse homolog of Diaphanous 2 (mDia2).
Isogai T, van der Kammen R, Goerdayal SS, Heck AJ, Altelaar AF, Innocenti M., Free PMC Article | 12/26/2015 |
| mDia2-deficient erythroid cells differentiate normally, though in a delayed manner, but exhibit cytokinesis failure with decreased accumulation of F-actin in the cleavage furrow during late differentiation from proerythroblasts | Loss of a Rho-regulated actin nucleator, mDia2, impairs cytokinesis during mouse fetal erythropoiesis.
Watanabe S, De Zan T, Ishizaki T, Yasuda S, Kamijo H, Yamada D, Aoki T, Kiyonari H, Kaneko H, Shimizu R, Yamamoto M, Goshima G, Narumiya S. | 08/23/2014 |
| Diaphanous homolog 3 (Diap3) overexpression causes progressive hearing loss and inner hair cell defects in a transgenic mouse model of human deafness. | Diaphanous homolog 3 (Diap3) overexpression causes progressive hearing loss and inner hair cell defects in a transgenic mouse model of human deafness.
Schoen CJ, Burmeister M, Lesperance MM., Free PMC Article | 08/31/2013 |
| Dia1 and Dia2 are dynamic components of meiotic spindle and pole complex during meiotic maturation of oocytes. | Dynamic interaction of formin proteins and cytoskeleton in mouse oocytes during meiotic maturation.
Kwon S, Shin H, Lim HJ. | 08/3/2013 |
| Microtubules strongly inhibit actin polymerization by mDia2. | Differential interactions of the formins INF2, mDia1, and mDia2 with microtubules.
Gaillard J, Ramabhadran V, Neumanne E, Gurel P, Blanchoin L, Vantard M, Higgs HN., Free PMC Article | 04/14/2012 |
| 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. | Enhancement of mDia2 activity by Rho-kinase-dependent phosphorylation of the diaphanous autoregulatory domain.
Staus DP, Taylor JM, Mack CP., Free PMC Article | 11/19/2011 |
| Results show that targeting of mDia2 to the cleavage furrow requires not only its binding to RhoA but also its diaphanous-inhibitory domain, and identify anillin as a novel mDia2 interaction partner. | Rho and anillin-dependent control of mDia2 localization and function in cytokinesis.
Watanabe S, Okawa K, Miki T, Sakamoto S, Morinaga T, Segawa K, Arakawa T, Kinoshita M, Ishizaki T, Narumiya S., Free PMC Article | 02/26/2011 |
| Introduction of the mDia2 inhibitor DIP/WISH/SPIN90 into cells triggers non-apoptotic membrane blebbing. The results infer a role for mDia2 in the maintenance of actin networks supporting the cell cortex. | Dia-interacting protein modulates formin-mediated actin assembly at the cell cortex.
Eisenmann KM, Harris ES, Kitchen SM, Holman HA, Higgs HN, Alberts AS. | 05/20/2010 |
| Activated Cdc42 binds to Drf3/mDia2 in cells in regions associated with the generation of filopodia. | Disruption of the Diaphanous-related formin Drf1 gene encoding mDia1 reveals a role for Drf3 as an effector for Cdc42.
Peng J, Wallar BJ, Flanders A, Swiatek PJ, Alberts AS. | 11/12/2009 |
| mDia2 degradation by ubiquitin-mediated proteolysis is required for completion of mitosis | Ubiquitin-mediated degradation of the formin mDia2 upon completion of cell division.
DeWard AD, Alberts AS., Free PMC Article | 05/26/2009 |
| analysis of interactions between mDia isoforms 1, 2, and 3 and RhoA, Rac1, and Cdc42 | Specificity of interactions between mDia isoforms and Rho proteins.
Lammers M, Meyer S, Kühlmann D, Wittinghofer A., Free PMC Article | 01/21/2010 |
| These results demonstrate that mDia2 is essential in mammalian cell cytokinesis and that mDia2-induced F-actin forms a scaffold for the contractile ring and maintains its position in the middle of a dividing cell. | mDia2 induces the actin scaffold for the contractile ring and stabilizes its position during cytokinesis in NIH 3T3 cells.
Watanabe S, Ando Y, Yasuda S, Hosoya H, Watanabe N, Ishizaki T, Narumiya S., Free PMC Article | 01/21/2010 |
| In vitro rheologic assays were used to deconvolve the dynamic cross-linking activity from the bundling activity of formin FRL1 and the closely related mDia1 and mDia2. | The filamentous actin cross-linking/bundling activity of mammalian formins.
Esue O, Harris ES, Higgs HN, Wirtz D. | 01/21/2010 |
| Rac GTPases and their effector mDia2 have important roles in enucleation of mammalian erythroblasts | Enucleation of cultured mouse fetal erythroblasts requires Rac GTPases and mDia2.
Ji P, Jayapal SR, Lodish HF. | 01/21/2010 |
| Dia2 plays an important role in formation of lamellipodia. | Novel roles of formin mDia2 in lamellipodia and filopodia formation in motile cells.
Yang C, Czech L, Gerboth S, Kojima S, Scita G, Svitkina T., Free PMC Article | 01/21/2010 |
| the DD/CC region is required for the Rho-independent membrane targeting of the isolated N terminus of mDia1 and mDia2 | The diaphanous inhibitory domain/diaphanous autoregulatory domain interaction is able to mediate heterodimerization between mDia1 and mDia2.
Copeland SJ, Green BJ, Burchat S, Papalia GA, Banner D, Copeland JW. | 01/21/2010 |