scholarly journals Poc1B and Sas-6 Function Together during the Atypical Centriole Formation in Drosophila melanogaster

Cells ◽  
2019 ◽  
Vol 8 (8) ◽  
pp. 841 ◽  
Author(s):  
Kyoung H. Jo ◽  
Ankit Jaiswal ◽  
Sushil Khanal ◽  
Emily L. Fishman ◽  
Alaina N. Curry ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Centriole Duplication ◽  
Sperm Development ◽  
Initiation Stage ◽  
Precise Role

Insects and mammals have atypical centrioles in their sperm. However, it is unclear how these atypical centrioles form. Drosophila melanogaster sperm has one typical centriole called the giant centriole (GC) and one atypical centriole called the proximal centriole-like structure (PCL). During early sperm development, centriole duplication factors such as Ana2 and Sas-6 are recruited to the GC base to initiate PCL formation. The centriolar protein, Poc1B, is also recruited at this initiation stage, but its precise role during PCL formation is unclear. Here, we show that Poc1B recruitment was dependent on Sas-6, that Poc1B had effects on cellular and PCL Sas-6, and that Poc1B and Sas-6 were colocalized in the PCL/centriole core. These findings suggest that Sas-6 and Poc1B interact during PCL formation. Co-overexpression of Ana2 and Sas-6 induced the formation of ectopic particles that contained endogenous Poc1 proteins and were composed of PCL-like structures. These structures were disrupted in Poc1 mutant flies, suggesting that Poc1 proteins stabilize the PCL-like structures. Lastly, Poc1B and Sas-6 co-overexpression also induced the formation of PCL-like structures, suggesting that they can function together during the formation of the PCL. Overall, our findings suggest that Poc1B and Sas-6 function together during PCL formation.

scholarly journals Asterless is required for centriole length control and sperm development

2016 ◽  
Vol 213 (4) ◽  
pp. 435-450 ◽  
Author(s):  
Brian J. Galletta ◽  
Katherine C. Jacobs ◽  
Carey J. Fagerstrom ◽  
Nasser M. Rusan
Keyword(s):  
Drosophila Melanogaster ◽  
Basal Body ◽  
Somatic Tissue ◽  
Mitotic Spindles ◽  
Independent Function ◽  
Centriole Duplication ◽  
Sperm Development ◽  
Pericentriolar Material ◽  
Shed Light

Centrioles are the foundation of two organelles, centrosomes and cilia. Centriole numbers and functions are tightly controlled, and mutations in centriole proteins are linked to a variety of diseases, including microcephaly. Loss of the centriole protein Asterless (Asl), the Drosophila melanogaster orthologue of Cep152, prevents centriole duplication, which has limited the study of its nonduplication functions. Here, we identify populations of cells with Asl-free centrioles in developing Drosophila tissues, allowing us to assess its duplication-independent function. We show a role for Asl in controlling centriole length in germline and somatic tissue, functioning via the centriole protein Cep97. We also find that Asl is not essential for pericentriolar material recruitment or centrosome function in organizing mitotic spindles. Lastly, we show that Asl is required for proper basal body function and spermatid axoneme formation. Insights into the role of Asl/Cep152 beyond centriole duplication could help shed light on how Cep152 mutations lead to the development of microcephaly.

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.

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 Are Unpaired Chromosomes Spermicidal?: A Maximum-Likelihood Analysis of Segregation and Meiotic Drive in Drosophila melanogaster Males Deficient for the Ribosomal-DNA

Genetics ◽  
1999 ◽  
Vol 151 (1) ◽  
pp. 251-262 ◽  
Author(s):  
Leonard G Robbins
Keyword(s):  
Drosophila Melanogaster ◽  
Maximum Likelihood ◽  
Physical State ◽  
Meiotic Drive ◽  
Direct Connection ◽  
Maximum Likelihood Analysis ◽  
Likelihood Analysis ◽  
Sperm Development ◽  
Sperm Survival ◽  
Sperm Chromosomes

AbstractMeiosis in Drosophila melanogaster males is achiasmate and requires special systems to ensure normal segregation. Several situations that yield frequent nondisjunction also produce high levels of chromatin-dependent sperm lethality, suggesting the possibility of a simple and direct connection between defective disjunction and defective sperm development. One hypothesis that has been offered is that pairing not only ensures disjunction, but also changes the physical state of chromosomes so that they can be packaged in sperm. Here, I present an analysis of extensive data on disjunction and sperm survival in rDNA-deficient males collected by B. McKee and D. Lindsley. This analysis demonstrates that, although nondisjunction and sperm lethality are indeed correlated, the basis of this is not the presence of unpaired chromosomes in the sperm. Chromosomes that have failed to disjoin are not themselves spermicidal.

scholarly journals Two Polo-like kinase 4 binding domains in Asterless perform distinct roles in regulating kinase stability

2015 ◽  
Vol 208 (4) ◽  
pp. 401-414 ◽  
Author(s):  
Joseph E. Klebba ◽  
Brian J. Galletta ◽  
Jonathan Nye ◽  
Karen M. Plevock ◽  
Daniel W. Buster ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Drosophila Melanogaster ◽  
Binding Domain ◽  
Terminal Region ◽  
Scaffolding Protein ◽  
Binding Partner ◽  
Centriole Duplication ◽  
Binding Domains ◽  
C Terminus ◽  
N Terminus

Plk4 (Polo-like kinase 4) and its binding partner Asterless (Asl) are essential, conserved centriole assembly factors that induce centriole amplification when overexpressed. Previous studies found that Asl acts as a scaffolding protein; its N terminus binds Plk4’s tandem Polo box cassette (PB1-PB2) and targets Plk4 to centrioles to initiate centriole duplication. However, how Asl overexpression drives centriole amplification is unknown. In this paper, we investigated the Asl–Plk4 interaction in Drosophila melanogaster cells. Surprisingly, the N-terminal region of Asl is not required for centriole duplication, but a previously unidentified Plk4-binding domain in the C terminus is required. Mechanistic analyses of the different Asl regions revealed that they act uniquely during the cell cycle: the Asl N terminus promotes Plk4 homodimerization and autophosphorylation during interphase, whereas the Asl C terminus stabilizes Plk4 during mitosis. Therefore, Asl affects Plk4 in multiple ways to regulate centriole duplication. Asl not only targets Plk4 to centrioles but also modulates Plk4 stability and activity, explaining the ability of overexpressed Asl to drive centriole amplification.

Centriole Duplication and Inheritance in Drosophila melanogaster

2012 ◽  
pp. 3-31 ◽  
Author(s):  
Tomer Avidor-Reiss ◽  
Jayachandran Gopalakrishnan ◽  
Stephanie Blachon ◽  
Andrey Polyanovsky
Keyword(s):  
Drosophila Melanogaster ◽  
Centriole Duplication

scholarly journals A genetic screen in Drosophila reveals an unexpected role for the KIP1 ubiquitination-promoting complex in male fertility

PLoS Genetics ◽  
2020 ◽  
Vol 16 (12) ◽  
pp. e1009217
Author(s):  
Weizhe Li ◽  
Jinqing Liang ◽  
Patricia Outeda ◽  
Stacey Turner ◽  
Barbara T. Wakimoto ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Male Fertility ◽  
Adaptor Protein ◽  
Sperm Storage ◽  
Genetic Screen ◽  
Mature Sperm ◽  
Forward Genetic Screen ◽  
Abnormal Sperm ◽  
Sperm Development ◽  
Tail Tip

A unifying feature of polycystin-2 channels is their localization to both primary and motile cilia/flagella. In Drosophila melanogaster, the fly polycystin-2 homologue, Amo, is an ER protein early in sperm development but the protein must ultimately cluster at the flagellar tip in mature sperm to be fully functional. Male flies lacking appropriate Amo localization are sterile due to abnormal sperm motility and failure of sperm storage. We performed a forward genetic screen to identify additional proteins that mediate ciliary trafficking of Amo. Here we report that Drosophila homologues of KPC1 and KPC2, which comprise the mammalian KIP1 ubiquitination-promoting complex (KPC), form a conserved unit that is required for the sperm tail tip localization of Amo. Male flies lacking either KPC1 or KPC2 phenocopy amo mutants and are sterile due to a failure of sperm storage. KPC is a heterodimer composed of KPC1, an E3 ligase, and KPC2 (or UBAC1), an adaptor protein. Like their mammalian counterparts Drosophila KPC1 and KPC2 physically interact and they stabilize one another at the protein level. In flies, KPC2 is monoubiquitinated and phosphorylated and this modified form of the protein is located in mature sperm. Neither KPC1 nor KPC2 directly interact with Amo but they are detected in proximity to Amo at the tip of the sperm flagellum. In summary we have identified a new complex that is involved in male fertility in Drosophila melanogaster.

scholarly journals Genetic analysis of Stellate elements of Drosophila melanogaster.

Genetics ◽  
1994 ◽  
Vol 138 (4) ◽  
pp. 1181-1197 ◽  
Author(s):  
G Palumbo ◽  
S Bonaccorsi ◽  
L G Robbins ◽  
S Pimpinelli
Keyword(s):  
Drosophila Melanogaster ◽  
Y Chromosome ◽  
Copy Number ◽  
Meiotic Drive ◽  
Genetic System ◽  
Male Meiosis ◽  
Meiotic Abnormalities ◽  
Y Chromosomes ◽  
Sperm Development ◽  
Dependent Failure

Abstract Repeated elements are remarkably important for male meiosis and spermiogenesis in Drosophila melanogaster. Pairing of the X and Y chromosomes is mediated by the ribosomal RNA genes of the Y chromosome and X chromosome heterochromatin, spermiogenesis depends on the fertility factors of the Y chromosome. Intriguingly, a peculiar genetic system of interaction between the Y-linked crystal locus and the X-linked Stellate elements seem to be also involved in male meiosis and spermiogenesis. Deletion of the crystal element of the Y, via an interaction with the Stellate elements of the X, causes meiotic abnormalities, gamete-genotype dependent failure of sperm development (meiotic drive), and deposition of protein crystals in spermatocytes. The current hypothesis is that the meiotic abnormalities observed in cry- males is due to an induced overexpression of the normally repressed Ste elements. An implication of this hypothesis is that the strength of the abnormalities would depend on the amount of the Ste copies. To test this point we have genetically and cytologically examined the relationship of Ste copy number and organization to meiotic behavior in cry- males. We found that heterochromatic as well as euchromatic Ste repeats are functional and that the abnormality in chromosome condensation and the frequency of nondisjunction are related to Ste copy number. Moreover, we found that meiosis is disrupted after synapsis and that cry-induced meiotic drive is probably not mediated by Ste.

scholarly journals Cep152 interacts with Plk4 and is required for centriole duplication

2010 ◽  
Vol 191 (4) ◽  
pp. 721-729 ◽  
Author(s):  
Emily M. Hatch ◽  
Anita Kulukian ◽  
Andrew J. Holland ◽  
Don W. Cleveland ◽  
Tim Stearns
Keyword(s):  
Cell Cycle ◽  
Drosophila Melanogaster ◽  
The Other ◽  
Early Step ◽  
Centriole Duplication ◽  
Kinase Family ◽  
Centrosome Protein

Centrioles are microtubule-based structures that organize the centrosome and nucleate cilia. Centrioles duplicate once per cell cycle, and duplication requires Plk4, a member of the Polo-like kinase family; however, the mechanism linking Plk4 activity and centriole formation is unknown. In this study, we show in human and frog cells that Plk4 interacts with the centrosome protein Cep152, the orthologue of Drosophila melanogaster Asterless. The interaction requires the N-terminal 217 residues of Cep152 and the crypto Polo-box of Plk4. Cep152 and Plk4 colocalize at the centriole throughout the cell cycle. Overexpression of Cep152 (1–217) mislocalizes Plk4, but both Cep152 and Plk4 are able to localize to the centriole independently of the other. Depletion of Cep152 prevents both normal centriole duplication and Plk4-induced centriole amplification and results in a failure to localize Sas6 to the centriole, an early step in duplication. Cep152 can be phosphorylated by Plk4 in vitro, suggesting that Cep152 acts with Plk4 to initiate centriole formation.

Author response for "Location and arrangement of campaniform sensilla in Drosophila melanogaster"

2020 ◽  
Author(s):  
Gesa F. Dinges ◽  
Alexander S. Chockley ◽  
Till Bockemühl ◽  
Kei Ito ◽  
Alexander Blanke ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Author Response ◽  
Campaniform Sensilla
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