Castrillon, D. H. & Wasserman, S. A. Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene. Development 120, 3367-3377

Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235-9038.
Development (Impact Factor: 6.46). 01/1995; 120(12):3367-77.
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We show that the Drosophila gene diaphanous is required for cytokinesis. Males homozygous for the dia1 mutation are sterile due to a defect in cytokinesis in the germline. Females trans-heterozygous for dia1 and a deficiency are sterile and lay eggs with defective eggshells; failure of cytokinesis is observed in the follicle cell layer. Null alleles are lethal. Death occurs at the onset of pupation due to the absence of imaginal discs. Mitotic figures in larval neuroblasts were found to be polyploid, apparently due to a defect in cytokinesis. The predicted 123 x 10(3) M(r) protein contains two domains shared by the formin proteins, encoded by the limb deformity gene in the mouse. These formin homology domains, which we have termed FH1 and FH2, are also found in Bni1p, the product of a Saccharomyces cerevisiae gene required for normal cytokinesis in diploid yeast cells.

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Available from: Steven A Wasserman, Apr 17, 2015
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    • "Formins control membrane-associated F-actin and membrane dependent processes and structures such as contractile ring in cytokinesis, endosomal dynamics, phagocytosis as well as protrusions such as filopodia and lamellipodia (Chesarone et al., 2010). In Drosophila embryos, Dia functionally associates with the cytokinetic furrow (Castrillon and Wasserman, 1994), with mitotic pseudocleavage furrow in syncytial embryos and the furrow canal during cellularization (Afshar et al., 2000; Padash Barmchi et al., 2005; Grosshans et al., 2005), cell contacts during cell intercalation (Levayer et al., 2011), with adherens junctions in the epidermis (Homem and Peifer, 2008) and controls apical secretion (Massarwa et al., 2009). The activity of Dia is controlled by Rho1 (also called RhoA) that releases an autoinhibitory intramolecular interaction (Li and Higgs, 2003; Grosshans et al., 2005). "
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    ABSTRACT: During Drosophila embryogenesis the first epithelium with defined cortical compartments is established during cellularization. Actin polymerization is required for the separation of lateral and basal domains as well as suppression of tubular extensions in the basal domain. The actin nucleator mediating this function is unknown. We found that the formin diaphanous (dia) is required for establishing and maintaining distinct lateral and basal domains during cellularization. In dia mutant embryos lateral marker proteins, such as Discs-large (Dlg) and Armadillo/beta-Catenin (Arm) spread into the basal compartment. Furthermore, high-resolution and live-imaging analysis of dia mutant embryos revealed an increased number of membrane extensions and endocytic activity at the basal domain, indicating a suppressing function of dia on membrane invaginations. Dia function may be based on an antagonistic interaction with the F-BAR protein Cip4/Toca-1, a known activator of the WASP/WAVE-Arp2/3 pathway. Dia and Cip4 physically and functionally interact and overexpression of Cip4 phenocopies dia loss-of-function. In vitro, Cip4 inhibits mainly actin nucleation by Dia. Thus, our data support a model in which linear actin filaments induced by Dia stabilize cortical compartmentalization by antagonizing WASP/WAVE-Arp2/3 induced membrane turnover.
    Journal of Cell Science 02/2013; 126(8). DOI:10.1242/jcs.118422 · 5.43 Impact Factor
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    • "The only known ovarian-resistance/ maintenance related gene within the area of interest Xq13–26 Case Reports in Genetics is the Drosophila melanogaster homologue DIAPH2 (DIA). Aberrations in DIAPH2 are known to result in sterility in both male and female Drosophila, but its function in humans is not well defined [18]. DIAPH2 regulates cytokinesis, which has a direct influence on oogenesis and follicle maturation. "
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    ABSTRACT: We describe a familial pattern of gonosomal-autosomal translocation between the X and 18 chromosomes, balanced and unbalanced forms, in male and female siblings. The proposita was consulted for hypergonadotropic hypogonadism. Karyotype analysis revealed a balanced 46, X, t(X;18)(q22.3;q23) genotype. The sister of the proband presented with oligomenorrhea with irregular menses and possesses an unbalanced form of the translocation 46, X, der(X), t(X;18)(q22.3;q23). The brother of the proband was investigated and was found to possess the balanced form of the same translocation, resulting in disrupted spermatogenesis. Maternal investigation revealed the progenitor karyotype 46, X, t(X;18)(q22.3;q23). Maternal inheritance and various genomic events contributed to the resultant genotypes. Primary infertility was initially diagnosed in all progeny; however, the male individual recently fathered twins. We briefly review the mechanisms associated with X;18 translocations and describe a pattern of inheritance, where breakpoints and translocation of the Xq22.3;18q23 regions have resulted in variable fertility.
    10/2012; 2012:681747. DOI:10.1155/2012/681747
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    • "Until the end of the last millennium, yeast and metazoan FH2 proteins have been implicated in numerous cellular processes, often related to cytoskeletal, in particular microtubule-related activities (e.g., mitosis [74], cytoplasmic streaming [78], or cytokinesis [79]). However, they have been also localized the to cell nucleus [80, 81] and implicated in several signaling pathways whose ultimate outcome is the regulation of gene expression [82]. "
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    ABSTRACT: Formins (FH2 proteins) are an evolutionarily conserved family of eukaryotic proteins, sharing the common FH2 domain. While they have been, until recently, understood mainly as actin nucleators, formins are also engaged in various additional aspects of cytoskeletal organization and signaling, including, but not limited to, the crosstalk between the actin and microtubule networks. A surprising diversity of domain organizations has been discovered among the FH2 proteins, and specific domain setups have been found in plants. Seed plants have two clades of formins, one of them (Class I) containing mostly transmembrane proteins, while members of the other one (Class II) may be anchored to membranes via a putative membrane-binding domain related to the PTEN antioncogene. Thus, plant formins present good candidates for possible mediators of coordination of the cortical actin and microtubule cytoskeletons, as well as their attachment to the plasma membrane, that is, aspects of cell cortex organization likely to be important for cell and tissue morphogenesis. Although experimental studies of plant formin function are hampered by the large number of formin genes and their functional redundancy, recent experimental work has already resulted in some remarkable insights into the function of FH2 proteins in plants.
    09/2012; 2012(6):712605. DOI:10.6064/2012/712605
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