anti-Diaphanous Homolog 3 (Drosophila) (DIAPH3) Antibodies

Mouse (Murine) Diaphanous Homolog 3 (Drosophila) (DIAPH3) interaction partners

1. neuronal drebrin A directly interacts with mDia2 formin.

2. 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.

3. 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.

4. mDia2 is regulated through acetylation and deacetylation at lysine 970 in the formin homology 2 domain

5. 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

6. Ineffective erythropoiesis caused by binucleated late-stage erythroblasts in mDia2 hematopoietic specific knockout mice.

7. the interactome of auto-inhibited and constitutively active mDia2, is reported.

8. 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

9. Diaphanous homolog 3 (Diap3) overexpression causes progressive hearing loss and inner hair cell defects in a transgenic mouse model of human deafness.

10. Dia1 and Dia2 are dynamic components of meiotic spindle and pole complex during meiotic maturation of oocytes.

11. Microtubules strongly inhibit actin polymerization by mDia2.

12. 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.

13. 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.

14. 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.

15. the bundling activities of FRL1 and mDia2, while producing phenotypically similar bundles, differ in mechanistic detail

16. the DD/CC region is required for the Rho-independent membrane targeting of the isolated N terminus of mDia1 and mDia2

17. Dia2 plays an important role in formation of lamellipodia.

18. Rac GTPases and their effector mDia2 have important roles in enucleation of mammalian erythroblasts

19. 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.

20. analysis of interactions between mDia isoforms 1, 2, and 3 and RhoA, Rac1, and Cdc42

Human Diaphanous Homolog 3 (Drosophila) (DIAPH3) interaction partners

1. through profilin-1 binding, CLIC4 functions in a RhoA-mDia2-regulated signaling network to integrate cortical actin assembly and membrane protrusion

2. 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.

3. study demonstrated the oncogenic activity of DIAPH3 in the progression of hepatocellular carcinoma and suggested that PDIAPH3 might be a therapeutic target.

4. Members of 3 generations of a family had dominant auditory neuropathy associated with a c.-172G>A point mutation in DIAPH3.

5. DIAPH3 overexpression inhibits the migration and invasion of Triple-negative breast cancer by inhibiting RhoA-GTP expression.

6. mDia2 and CXCR4 associate in blebs upon CXCL12 stimulation. Both CXCR4 and RhoA are required for CXCL12-induced blebbing

7. we use a simple cellular system to examine fundamental features of formin-mediated filopodial assembly, using constitutively active constructs of the formins mDia2 and FMNL3

8. results suggest that inhibition of MT stability arising from DIAPH3 downregulation enhances susceptibility to MT poisons, and that the DIAPH3 network potentially reports taxane sensitivity in human tumors

9. Dia1, Dia2, and Dia3 are involved in ErbB2-dependent capture of microtubules at the cell leading edge and ErbB2-driven guided migration.

10. An mDia2/ROCK signaling axis regulates invasive egress from epithelial ovarian cancer spheroids.

11. TGF-beta promotes association of mDia2 with actin stress fibers, which further drives stress fiber formation and myofibroblast differentiation

12. In human tumours, DIAPH3 down-regulation was associated with aggressive or metastatic disease.

13. isoform-selective actin assembly by DIAPH3 exerts specific and differentially regulated functions during cell adhesion and motility.

14. the amino terminus of mDia2 serves as a coincidence detection module, directing mDia2 to the plasma membrane through interactions with phospholipids and activated Rif

15. These findings reveal a key role for mDia3 and its regulation by Aurora B phosphorylation in achieving proper stable kinetochore microtubule attachment.

16. These studies further suggest that Rho GTPases significantly influence the activity of mDia family formins in driving cellular membrane remodeling through the regulation of actin dynamics.

17. DIP-induced membrane blebbing was dependent on Diaphanous 2 but did not require the activities of either Diaphanous 1 or Actin-Related Protein 2-3 Complex.

18. Data show that Dia2 localizes in the lamella of migrating epithelial cells, where it is involved in the formation of a stable pool of cortical actin and in maintenance of polymerization-competent free filament barbed ends at focal adhesions.

19. 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.

20. active Drf3 lacking the C-terminal regulatory region (Drf3DeltaDAD) induced the formation of filopodia and accumulated at their tips.