scholarly journals Centrobin is essential for C-tubule assembly and flagellum development in Drosophila melanogaster spermatogenesis

2018 ◽  
Vol 217 (7) ◽  
pp. 2365-2372 ◽  
Author(s):  
Jose Reina ◽  
Marco Gottardo ◽  
Maria G. Riparbelli ◽  
Salud Llamazares ◽  
Giuliano Callaini ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Sensory Neurons ◽  
Basal Body ◽  
Cell Types ◽  
Basal Bodies ◽  
Phosphorylation Sites ◽  
Body Function ◽  
Mother And Daughter ◽  
The Right ◽  
Different Cell Types

Centrobin homologues identified in different species localize on daughter centrioles. In Drosophila melanogaster sensory neurons, Centrobin (referred to as CNB in Drosophila) inhibits basal body function. These data open the question of CNB’s role in spermatocytes, where daughter and mother centrioles become basal bodies. In this study, we report that in these cells, CNB localizes equally to mother and daughter centrioles and is essential for C-tubules to attain the right position and remain attached to B-tubules as well as for centrioles to grow in length. CNB appears to be dispensable for meiosis, but flagellum development is severely compromised in Cnb mutant males. Remarkably, three N-terminal POLO phosphorylation sites that are critical for CNB function in neuroblasts are dispensable for spermatogenesis. Our results underpin the multifunctional nature of CNB that plays different roles in different cell types in Drosophila, and they identify CNB as an essential component for C-tubule assembly and flagellum development in Drosophila spermatogenesis.

scholarly journals Drosophila chibby is required for basal body formation and ciliogenesis but not for Wg signaling

2012 ◽  
Vol 197 (2) ◽  
pp. 313-325 ◽  
Author(s):  
Camille Enjolras ◽  
Joëlle Thomas ◽  
Brigitte Chhin ◽  
Elisabeth Cortier ◽  
Jean-Luc Duteyrat ◽  
...  
Keyword(s):  
Wnt Signaling ◽  
Basal Body ◽  
Coiled Coil ◽  
Cell Types ◽  
Sensory Transduction ◽  
Basal Bodies ◽  
Neuronal Cilia ◽  
Complex Process ◽  
Specific Proteins ◽  
And Function

Centriole-to–basal body conversion, a complex process essential for ciliogenesis, involves the progressive addition of specific proteins to centrioles. CHIBBY (CBY) is a coiled-coil domain protein first described as interacting with β-catenin and involved in Wg-Int (WNT) signaling. We found that, in Drosophila melanogaster, CBY was exclusively expressed in cells that require functional basal bodies, i.e., sensory neurons and male germ cells. CBY was associated with the basal body transition zone (TZ) in these two cell types. Inactivation of cby led to defects in sensory transduction and in spermatogenesis. Loss of CBY resulted in altered ciliary trafficking into neuronal cilia, irregular deposition of proteins on spermatocyte basal bodies, and, consequently, distorted axonemal assembly. Importantly, cby1/1 flies did not show Wingless signaling defects. Hence, CBY is essential for normal basal body structure and function in Drosophila, potentially through effects on the TZ. The function of CBY in WNT signaling in vertebrates has either been acquired during vertebrate evolution or lost in Drosophila.

scholarly journals Előprogramozott gének

2017 ◽  
Vol 158 (34) ◽  
pp. 1323-1330
Author(s):  
János Szabad
Keyword(s):  
Gene Expression ◽  
Genetic Information ◽  
Cell Types ◽  
Epigenetic Mechanisms ◽  
Base Pairs ◽  
Control Gene Expression ◽  
Protein Molecules ◽  
Chromatin Compactness ◽  
The Right ◽  
Different Cell Types

Abstract: Cells feel good and carry on perfect functions when they contain the right types of proteins in the right concentration, at the right time and sites. There are mechanisms that ensure the right level of gene expression in the different cell types: the formation of protein molecules based on the DNA-encoded genetic information. Gene expression can also be regulated through the compactness of chromatin, i.e. the accessibility of the genes. The chromosomes are repositories of the genetic information – the sequence of base pairs – and also of the so-called epigenetic mechanisms that control gene expression through the regulation of chromatin compactness. The epigenetic mechanisms operate through DNA methylation and/or the regulation of chromatin compactness. The present overview takes a look into the phenomenon of epigenesis. It summarizes how genetic crosses reveal the involvement of epigenesis, explains its meaning and impact on life of the organisms. An understanding of epigenesis provides guidance to improve our life. Orv Hetil. 2017; 158(34): 1323–1330.

Role of DZIP1–CBY–FAM92 transition zone complex in the basal body to membrane attachment and ciliary budding

2020 ◽  
Vol 48 (3) ◽  
pp. 1067-1075
Author(s):  
Jean-André Lapart ◽  
Amélie Billon ◽  
Jean-Luc Duteyrat ◽  
Joëlle Thomas ◽  
Bénédicte Durand
Keyword(s):  
Transition Zone ◽  
Basal Body ◽  
Cell Types ◽  
Molecular Assembly ◽  
Bud Formation ◽  
Wide Range ◽  
Membrane Attachment ◽  
Functional Hierarchy ◽  
Complex Architecture ◽  
Different Cell Types

Cilia play important signaling or motile functions in various organisms. In Human, cilia dysfunctions are responsible for a wide range of diseases, called ciliopathies. Cilia assembly is a tightly controlled process, which starts with the conversion of the centriole into a basal body, leading to the formation of the ciliary bud that protrudes inside a ciliary vesicle and/or ultimately at the cell surface. Ciliary bud formation is associated with the assembly of the transition zone (TZ), a complex architecture of proteins of the ciliary base which plays critical functions in gating proteins in and out of the ciliary compartment. Many proteins are involved in the assembly of the TZ, which shows structural and functional variations in different cell types or organisms. In this review, we discuss how a particular complex, composed of members of the DZIP1, CBY and FAM92 families of proteins, is required for the initial stages of cilia assembly leading to ciliary bud formation and how their functional hierarchy contributes to TZ assembly. Moreover, we summarize how evidences in Drosophila reveal functional differences of the DZIP1–CBY–FAM92 complex in the different ciliated tissues of this organism. Whereas it is essential for proper TZ assembly in the two types of ciliated tissues, it is involved in stable anchoring of basal bodies to the plasma membrane in male germ cells. Overall, the DZIP1–CBY–FAM92 complex reveals a molecular assembly pathway required for the initial stages of ciliary bud formation and that is conserved from Drosophila to Human.

scholarly journals Genetic regulation and pattern formation: A study of the yellow locus in Drosophila melanogaster

1974 ◽  
Vol 24 (1) ◽  
pp. 19-26 ◽  
Author(s):  
William G. Nash ◽  
Rhoda J. Yarkin
Keyword(s):  
Drosophila Melanogaster ◽  
Pattern Formation ◽  
Genetic Regulation ◽  
Phenotypic Expression ◽  
Type A ◽  
Cell Types ◽  
Wild Type ◽  
Unique Pattern ◽  
Distinct Cell ◽  
Different Cell Types

SUMMARYMany of the yellow alleles found in Drosophila melanogaster result in a unique pattern of phenotypic expression. These patterns follow the morphologically distinct cell types of the cuticle, so that for one allele all the bristles of the head and thorax might be mutant, while most of the fly appears wild type. A comparison of many different y mutants demonstrates that the yellow phenotype is expressed independently in most if not all the different cell types which form the cuticle. Control of this expression appears to reside at the yellow locus itself.

scholarly journals Cep97 Is Required For Centriole Structural Integrity And Cilia Formation In Drosophila

2019 ◽  
Author(s):  
Jeroen Dobbelaere ◽  
Marketa Schmidt-Cernohorska ◽  
Martina Huranova ◽  
Dea Slade ◽  
Alexander Dammermann
Keyword(s):  
Drosophila Melanogaster ◽  
Basal Body ◽  
Structural Integrity ◽  
Cultured Cells ◽  
Full Length ◽  
Proper Function ◽  
Basal Bodies ◽  
Cell Divisions ◽  
Cilia Formation

SUMMARYCentrioles are highly elaborate microtubule-based structures responsible for the formation of centrosomes and cilia. Despite considerable variation across species and tissues, within any given tissue their size is essentially constant [1, 2]. While the diameter of the centriole cylinder is set by the dimensions of the inner scaffolding structure of the cartwheel [3], how centriole length is set so precisely and stably maintained over many cell divisions is not well understood. Cep97 and CP110 are conserved proteins that localize to the distal end of centrioles and have been reported to limit centriole elongation in vertebrates [4, 5]. Here, we examine Cep97 function in Drosophila melanogaster. We show that Cep97 is essential for formation of full-length centrioles in multiple tissues of the fly. We further identify the microtubule deacetylase Sirt2 as a Cep97 proximity interactor. Deletion of Sirt2 likewise affects centriole size. Interestingly, so does deletion of the acetylase Atat1, indicating that loss of stabilizing acetyl marks impairs centriole integrity. Cep97 and CP110 were originally identified as inhibitors of cilia formation in vertebrate cultured cells [6] and loss of CP110 is a widely used marker of basal body maturation. In contrast, in Drosophila Cep97 is only transiently removed from basal bodies and loss of Cep97 strongly impairs ciliogenesis. Collectively, our results support a model whereby Cep97 functions as part of a protective cap that acts together with the microtubule acetylation machinery to maintain centriole stability, essential for proper function in cilium biogenesis.

The ultrastructure of the flagellar root system of Isochrysis galbana (Prymnesiophyta)

1991 ◽  
Vol 71 (1) ◽  
pp. 137-152 ◽  
Author(s):  
T. Hori ◽  
J. C. Green
Keyword(s):  
Fine Structure ◽  
Root System ◽  
Basal Body ◽  
Isochrysis Galbana ◽  
Ventral Side ◽  
Basal Bodies ◽  
Right Hand ◽  
General Arrangement ◽  
The Right

The fine structure of the flagellar root system of Isochrysis galbana Parke (Prymnesiophyta) has been investigated and a reconstruction is presented. Associated with the left basal body and arising close to the base of the haptonema there is a root composed of a ribbon of approximately five microtubules running peripherally towards the ventral side of the cell. Near the basal body it is also associated with two additional bundles of microtubules which diverge from it and from each other passing deep into the cell.On the right-hand side of the right basal body there is a root consisting of four microtubules (2+2) which runs peripherally in a dorsal direction. Another root, consisting of a single microtubule only, originates close to the distal connecting band between the basal bodies, and passes around the ventral side of the left basal body before following a course deep into the cell. In addition, several fibrous bands connect the bases of the flagella and haptonema. The general arrangement of the root system of 1. galbana is comparable with many other members of the Prymnesiophyta, but attention is drawn to a number of important differences, particularly between Isochrysis and some other members of the order Isochrysidales. The results are discussed in the context of the evolution, phylogeny and taxonomy of the Prymnesiophyta.On the right-hand side of the right basal body there is a root consisting of four microtubules (2+2) which runs peripherally in a dorsal direction. Another root, consisting of a single microtubule only, originates close to the distal connecting band between the basal bodies, and passes around the ventral side of the left basal body before following a curse deep into the cell.

scholarly journals The two human centrin homologues have similar but distinct functions at Tetrahymena basal bodies

2012 ◽  
Vol 23 (24) ◽  
pp. 4766-4777 ◽  
Author(s):  
Tyson Vonderfecht ◽  
Michael W. Cookson ◽  
Thomas H. Giddings ◽  
Christina Clarissa ◽  
Mark Winey
Keyword(s):  
Body Composition ◽  
Basal Body ◽  
Binding Proteins ◽  
Tetrahymena Thermophila ◽  
Sequence Similarity ◽  
Body Orientation ◽  
Basal Bodies ◽  
Body Function

Centrins are a ubiquitous family of small Ca2+-binding proteins found at basal bodies that are placed into two groups based on sequence similarity to the human centrins 2 and 3. Analyses of basal body composition in different species suggest that they contain a centrin isoform from each group. We used the ciliate protist Tetrahymena thermophila to gain a better understanding of the functions of the two centrin groups and to determine their potential redundancy. We have previously shown that the Tetrahymena centrin 1 (Cen1), a human centrin 2 homologue, is required for proper basal body function. In this paper, we show that the Tetrahymena centrin 2 (Cen2), a human centrin 3 homologue, has functions similar to Cen1 in basal body orientation, maintenance, and separation. The two are, however, not redundant. A further examination of human centrin 3 homologues shows that they function in a manner distinct from human centrin 2 homologues. Our data suggest that basal bodies require a centrin from both groups in order to function correctly.

Study of the Molecular Architecture of Keratin Filaments by Electron Microscopy

1982 ◽  
Vol 40 ◽  
pp. 118-119
Author(s):  
U. Aebi ◽  
P. Rew ◽  
T.-T. Sun
Keyword(s):  
Electron Microscopy ◽  
Structural Organization ◽  
Cell Types ◽  
Structural Features ◽  
Molecular Architecture ◽  
The Past ◽  
Keratin Filaments ◽  
Different Types ◽  
10 Nm Filaments ◽  
Different Cell Types

Various types of intermediate-sized (10-nm) filaments have been found and described in many different cell types during the past few years. Despite the differences in the chemical composition among the different types of filaments, they all yield common structural features: they are usually up to several microns long and have a diameter of 7 to 10 nm; there is evidence that they are made of several 2 to 3.5 nm wide protofilaments which are helically wound around each other; the secondary structure of the polypeptides constituting the filaments is rich in ∞-helix. However a detailed description of their structural organization is lacking to date.

Ciliary coordination in newt lung cells requires microtubule-based linkages between basal bodies: A correlative light and EM study

1992 ◽  
Vol 50 (1) ◽  
pp. 570-571
Author(s):  
Robert Hard ◽  
Gerald Rupp ◽  
Matthew L. Withiam-Leitch ◽  
Lisa Cardamone
Keyword(s):  
Basal Body ◽  
Untreated Control ◽  
Beat Frequency ◽  
Primary Cultures ◽  
Living Cells ◽  
Power Stroke ◽  
Ultrastructural Changes ◽  
Lung Cells ◽  
Basal Bodies ◽  
Ciliated Cells

In a coordinated field of beating cilia, the direction of the power stroke is correlated with the orientation of basal body appendages, called basal feet. In newt lung ciliated cells, adjacent basal feet are interconnected by cold-stable microtubules (basal MTs). In the present study, we investigate the hypothesis that these basal MTs stabilize ciliary distribution and alignment. To accomplish this, newt lung primary cultures were treated with the microtubule disrupting agent, Colcemid. In newt lung cultures, cilia normally disperse in a characteristic fashion as the mucociliary epithelium migrates from the tissue explant. Four arbitrary, but progressive stages of dispersion were defined and used to monitor this redistribution process. Ciliaiy beat frequency, coordination, and dispersion were assessed for 91 hrs in untreated (control) and treated cultures. When compared to controls, cilia dispersed more rapidly and ciliary coordination decreased markedly in cultures treated with Colcemid (2 mM). Correlative LM/EM was used to assess whether these effects of Colcemid were coupled to ultrastructural changes. Living cells were defined as having coordinated or uncoordinated cilia and then were processed for transmission EM.

Processing and Characterization of Recombinant von Willebrand Factor Expressed in Different Cell Types Using a Vaccinia Virus Vector

1992 ◽  
Vol 67 (01) ◽  
pp. 154-160 ◽  
Author(s):  
P Meulien ◽  
M Nishino ◽  
C Mazurier ◽  
K Dott ◽  
G Piétu ◽  
...  
Keyword(s):  
Vaccinia Virus ◽  
Von Willebrand Factor ◽  
Human Fibroblasts ◽  
Active Form ◽  
Cell Types ◽  
Biologically Active ◽  
L Cells ◽  
Von Willebrand ◽  
Different Cell Types ◽  
Willebrand Factor

SummaryThe cloning of the cDNA encoding von Willebrand factor (vWF) has revealed that it is synthesized as a large precursor (pre-pro-vWF) molecule and it is now clear that the prosequence or vWAgll is responsible for the intracellular multimerization of vWF. We have cloned the complete vWF cDNA and expressed it using a recombinant vaccinia virus as vector. We have characterized the structure and function of the recombinant vWF (rvWF) secreted from five different cell types: baby hamster kidney (BHK), Chinese hamster ovary (CHO), human fibroblasts (143B), mouse fibroblasts (L) and primary embryonic chicken cells. Forty-eight hours after infection, the quantity of vWF antigen found in the cell supernatant varied from 3 to 12 U/dl depending on the cell type. By SDS-agarose gel electrophoresis, the percentage of high molecular weight forms of vWF varied from 39 to 49% relative to normal plasma for BHK, CHO, 143B and chicken cells but was less than 10% for L cells. In all cell types, the two anodic subbands of each multimer were missing. The two cathodic subbands were easily detected only in BHK and L cells. By SDS-PAGE of reduced samples, pro-vWF was present in similar quantity to the fully processed vWF subunit in L cells, present in moderate amounts in BHK and CHO and in very low amounts in 143B and chicken cells. rvWF from all cells bound to collagen and to platelets in the presence of ristocetin, the latter showing a high correlation between binding efficiency and degree of multimerization. rvWF from all cells was also shown to bind to purified FVIII and in this case binding appeared to be independent of the degree of multimerization. We conclude that whereas vWF is naturally synthesized only by endothelial cells and megakaryocytes, it can be expressed in a biologically active form from various other cell types.

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