scholarly journals Ana3 is a conserved protein required for the structural integrity of centrioles and basal bodies

2009 ◽  
Vol 187 (3) ◽  
pp. 355-363 ◽  
Author(s):  
Naomi R. Stevens ◽  
Jeroen Dobbelaere ◽  
Alan Wainman ◽  
Fanni Gergely ◽  
Jordan W. Raff
Keyword(s):  
Drosophila Melanogaster ◽  
Structural Integrity ◽  
Basal Bodies ◽  
Centriole Duplication ◽  
The Core ◽  
Mammalian Homologue ◽  
Conserved Core

Recent studies have identified a conserved “core” of proteins that are required for centriole duplication. A small number of additional proteins have recently been identified as potential duplication factors, but it is unclear whether any of these proteins are components of the core duplication machinery. In this study, we investigate the function of one of these proteins, Drosophila melanogaster Ana3. We show that Ana3 is present in centrioles and basal bodies, but its behavior is distinct from that of the core duplication proteins. Most importantly, we find that Ana3 is required for the structural integrity of both centrioles and basal bodies and for centriole cohesion, but it is not essential for centriole duplication. We show that Ana3 has a mammalian homologue, Rotatin, that also localizes to centrioles and basal bodies and appears to be essential for cilia function. Thus, Ana3 defines a conserved family of centriolar proteins and plays an important part in ensuring the structural integrity of centrioles and basal bodies.

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.

scholarly journals The rosy locus in Drosophila melanogaster: xanthine dehydrogenase and eye pigments.

Genetics ◽  
1991 ◽  
Vol 129 (4) ◽  
pp. 1099-1109 ◽  
Author(s):  
A G Reaume ◽  
D A Knecht ◽  
A Chovnick
Keyword(s):  
Drosophila Melanogaster ◽  
Structural Integrity ◽  
Present Report ◽  
Specific Interaction ◽  
Pigment Granule ◽  
Ultrastructural Localization ◽  
Xanthine Dehydrogenase ◽  
Pigment Formation ◽  
Antibody Staining ◽  
Pigment Granules

Abstract The rosy gene in Drosophila melanogaster codes for the enzyme xanthine dehydrogenase (XDH). Mutants that have no enzyme activity are characterized by a brownish eye color phenotype reflecting a deficiency in the red eye pigment. Xanthine dehydrogenase is not synthesized in the eye, but rather is transported there. The present report describes the ultrastructural localization of XDH in the Drosophila eye. Three lines of evidence are presented demonstrating that XDH is sequestered within specific vacuoles, the type II pigment granules. Histochemical and antibody staining of frozen sections, as well as thin layer chromatography studies of several adult genotypes serve to examine some of the factors and genic interactions that may be involved in transport of XDH, and in eye pigment formation. While a specific function for XDH in the synthesis of the red, pteridine eye pigments remains unknown, these studies present evidence that: (1) the incorporation of XDH into the pigment granules requires specific interaction between a normal XDH molecule and one or more transport proteins; (2) the structural integrity of the pigment granule itself is dependent upon the presence of a normal balance of eye pigments, a notion advanced earlier.

scholarly journals Drosophila Ana2 is a conserved centriole duplication factor

2010 ◽  
Vol 188 (3) ◽  
pp. 313-323 ◽  
Author(s):  
Naomi R. Stevens ◽  
Jeroen Dobbelaere ◽  
Kathrin Brunk ◽  
Anna Franz ◽  
Jordan W. Raff
Keyword(s):  
Drosophila Melanogaster ◽  
Caenorhabditis Elegans ◽  
De Novo ◽  
Protein Family ◽  
Centriole Duplication

In Caenorhabditis elegans, five proteins are required for centriole duplication: SPD-2, ZYG-1, SAS-5, SAS-6, and SAS-4. Functional orthologues of all but SAS-5 have been found in other species. In Drosophila melanogaster and humans, Sak/Plk4, DSas-6/hSas-6, and DSas-4/CPAP—orthologues of ZYG-1, SAS-6, and SAS-4, respectively—are required for centriole duplication. Strikingly, all three fly proteins can induce the de novo formation of centriole-like structures when overexpressed in unfertilized eggs. Here, we find that of eight candidate duplication factors identified in cultured fly cells, only two, Ana2 and Asterless (Asl), share this ability. Asl is now known to be essential for centriole duplication in flies, but no equivalent protein has been found in worms. We show that Ana2 is the likely functional orthologue of SAS-5 and that it is also related to the vertebrate STIL/SIL protein family that has been linked to microcephaly in humans. We propose that members of the SAS-5/Ana2/STIL family of proteins are key conserved components of the centriole duplication machinery.

Structural Analysis of Basal Bodies of The Isolated Oral Apparatus of Tetrahymena Pyriformis

1970 ◽  
Vol 6 (3) ◽  
pp. 679-700
Author(s):  
J. WOLFE
Keyword(s):  
Structural Analysis ◽  
Cell Membrane ◽  
Basal Body ◽  
Structural Integrity ◽  
Tetrahymena Pyriformis ◽  
Basal Plate ◽  
Basal Bodies ◽  
The Third ◽  
Ionic Detergent

The oral apparatus of Tetrahymena pyriformis was isolated using a non-ionic detergent to disrupt the cell membrane. The mouth consists largely of basal bodies and microfilaments. Each basal body is attached to the mouth by a basal plate which is integrated into the meshwork of microfilaments that confers upon the oral apparatus its structural integrity. Each basal body is composed of 9 triplet microtubules. Two of the 3 tubules, subfibres ‘A’ and ‘B’ are composed of filamentous rows of globules with a spacing of 4.5nm. The third tubule, subfibre ‘C’, is only one-third the length of the basal body.

scholarly journals The Centrioles, Centrosomes, Basal Bodies, and Cilia of Drosophila melanogaster

Genetics ◽  
2017 ◽  
Vol 206 (1) ◽  
pp. 33-53 ◽  
Author(s):  
Ramona Lattao ◽  
Levente Kovács ◽  
David M. Glover
Keyword(s):  
Drosophila Melanogaster ◽  
Basal Bodies

scholarly journals Reciprocal action of Casein Kinase Iε on core planar polarity proteins regulates clustering and asymmetric localisation

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Helen Strutt ◽  
Jessica Gamage ◽  
David Strutt
Keyword(s):  
Core Protein ◽  
Intercellular Junctions ◽  
Casein Kinase ◽  
Planar Polarity ◽  
The Core ◽  
Pupal Wing ◽  
Polarity Proteins ◽  
Conserved Core

The conserved core planar polarity pathway is essential for coordinating polarised cell behaviours and the formation of polarised structures such as cilia and hairs. Core planar polarity proteins localise asymmetrically to opposite cell ends and form intercellular complexes that link the polarity of neighbouring cells. This asymmetric segregation is regulated by phosphorylation through poorly understood mechanisms. We show that loss of phosphorylation of the core protein Strabismus in the Drosophila pupal wing increases its stability and promotes its clustering at intercellular junctions, and that Prickle negatively regulates Strabismus phosphorylation. Additionally, loss of phosphorylation of Dishevelled – which normally localises to opposite cell edges to Strabismus – reduces its stability at junctions. Moreover, both phosphorylation events are independently mediated by Casein Kinase Iε. We conclude that Casein Kinase Iε phosphorylation acts as a switch, promoting Strabismus mobility and Dishevelled immobility, thus enhancing sorting of these proteins to opposite cell edges.

scholarly journals Why? – Successful Pseudomonas aeruginosa clones with a focus on clone C

2020 ◽  
Vol 44 (6) ◽  
pp. 740-762
Author(s):  
Changhan Lee ◽  
Jens Klockgether ◽  
Sebastian Fischer ◽  
Janja Trcek ◽  
Burkhard Tümmler ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Core Genome ◽  
Genomic Island ◽  
Protein Quality ◽  
Temperature Tolerance ◽  
Protein Homeostasis ◽  
Gene Products ◽  
Accessory Genome ◽  
The Core ◽  
Conserved Core

ABSTRACT The environmental species Pseudomonas aeruginosa thrives in a variety of habitats. Within the epidemic population structure of P. aeruginosa, occassionally highly successful clones that are equally capable to succeed in the environment and the human host arise. Framed by a highly conserved core genome, individual members of successful clones are characterized by a high variability in their accessory genome. The abundance of successful clones might be funded in specific features of the core genome or, although not mutually exclusive, in the variability of the accessory genome. In clone C, one of the most predominant clones, the plasmid pKLC102 and the PACGI-1 genomic island are two ubiquitous accessory genetic elements. The conserved transmissible locus of protein quality control (TLPQC) at the border of PACGI-1 is a unique horizontally transferred compository element, which codes predominantly for stress-related cargo gene products such as involved in protein homeostasis. As a hallmark, most TLPQC xenologues possess a core genome equivalent. With elevated temperature tolerance as a characteristic of clone C strains, the unique P. aeruginosa and clone C specific disaggregase ClpG is a major contributor to tolerance. As other successful clones, such as PA14, do not encode the TLPQC locus, ubiquitous denominators of success, if existing, need to be identified.

scholarly journals Comparative RNAi screening identifies a conserved core metazoan actinome by phenotype

2011 ◽  
Vol 194 (5) ◽  
pp. 789-805 ◽  
Author(s):  
Jennifer L. Rohn ◽  
David Sims ◽  
Tao Liu ◽  
Marina Fedorova ◽  
Frieder Schöck ◽  
...  
Keyword(s):  
Rna Interference ◽  
Rna Splicing ◽  
Actin Binding ◽  
Nuclear Actin ◽  
Systematic Method ◽  
The Core ◽  
Binding Domains ◽  
Genome Wide ◽  
Number Of Genes ◽  
Conserved Core

Although a large number of actin-binding proteins and their regulators have been identified through classical approaches, gaps in our knowledge remain. Here, we used genome-wide RNA interference as a systematic method to define metazoan actin regulators based on visual phenotype. Using comparative screens in cultured Drosophila and human cells, we generated phenotypic profiles for annotated actin regulators together with proteins bearing predicted actin-binding domains. These phenotypic clusters for the known metazoan “actinome” were used to identify putative new core actin regulators, together with a number of genes with conserved but poorly studied roles in the regulation of the actin cytoskeleton, several of which we studied in detail. This work suggests that although our search for new components of the core actin machinery is nearing saturation, regulation at the level of nuclear actin export, RNA splicing, ubiquitination, and other upstream processes remains an important but unexplored frontier of actin biology.

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