Duplicated proteasome subunit genes in Drosophila and their roles in spermatogenesis

Belote, John M.; Zhong, Lei

doi:10.1038/hdy.2009.23

Cited by 56 publications

(59 citation statements)

References 47 publications

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“…We found that expression of shRNAs targeting Prosb5, a catalytic subunit of the proteasome (Belote and Zhong 2009;Finley 2009), led to an increase in Ub G76V -GFP reporter protein, as shown by quantitation of GFP levels (Figure 7, A-C), indicating successful proteasome inhibition. Proteasome inhibition also led to arrest of egg chamber growth and eventual egg chamber degeneration (Figure 7, A and B, and Figure S3).…”

Section: Analysis Of Proteasome Function At Ring Canalsmentioning

confidence: 98%

Actin Cytoskeletal Organization in Drosophila Germline Ring Canals Depends on Kelch Function in a Cullin-RING E3 Ligase

2015

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The Drosophila Kelch protein is required to organize the ovarian ring canal cytoskeleton. Kelch binds and cross-links F-actin in vitro, and it also functions with Cullin 3 (Cul3) as a component of a ubiquitin E3 ligase. How these two activities contribute to cytoskeletal remodeling in vivo is not known. We used targeted mutagenesis to investigate the mechanism of Kelch function. We tested a model in which Cul3-dependent degradation of Kelch is required for its function, but we found no evidence to support this hypothesis. However, we found that mutant Kelch deficient in its ability to interact with Cul3 failed to rescue the kelch cytoskeletal defects, suggesting that ubiquitin ligase activity is the principal activity required in vivo. We also determined that the proteasome is required with Kelch to promote the ordered growth of the ring canal cytoskeleton. These results indicate that Kelch organizes the cytoskeleton in vivo by targeting a protein substrate for degradation by the proteasome.

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Section: Analysis Of Proteasome Function At Ring Canalsmentioning

confidence: 98%

Actin Cytoskeletal Organization in Drosophila Germline Ring Canals Depends on Kelch Function in a Cullin-RING E3 Ligase

2015

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“…There are over 20 times more testes-specific duplicate paralogues (590 paralogues) than head-specific duplicate paralogues (27 paralogues). In Drosophila, spermatogenesis uses a unique transcriptional programme that requires numerous genes that are expressed exclusively in the testes and male germline, many of which have originated from recent gene duplication events [40,42,43,47]. Stalk-eyed flies appear to have evolved a similar, or possibly greater, level of genetic diversity to function during this process.…”

Section: Stalk-eyed Fly Genomicsmentioning

confidence: 99%

“…These genes are required for progression of the meiotic cell cycle, and mutations in the genes result in meiotic arrest and sterility [44,45]. Similarly, the proteasome, a complex that controls protein degradation, also contains numerous testes-specific components that have originated recently, via gene duplication, within Drosophila [46,47]. Not only is much of spermatogenesis regulated by testes-specific duplicates, but there are several cases of recurrent duplication in which a given gene has undergone multiple independent duplications and acquired testes-specific expression in different lineages [46][47][48][49].…”

Section: Genetic Architecture Of Sexual Dimorphism and Sexual Conflictmentioning

confidence: 99%

Gene duplication, tissue-specific gene expression and sexual conflict in stalk-eyed flies (Diopsidae)

Baker

Narechania

Johns

et al. 2012

Phil. Trans. R. Soc. B

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Gene duplication provides an essential source of novel genetic material to facilitate rapid morphological evolution. Traits involved in reproduction and sexual dimorphism represent some of the fastest evolving traits in nature, and gene duplication is intricately involved in the origin and evolution of these traits. Here, we review genomic research on stalk-eyed flies (Diopsidae) that has been used to examine the extent of gene duplication and its role in the genetic architecture of sexual dimorphism. Stalk-eyed flies are remarkable because of the elongation of the head into long stalks, with the eyes and antenna laterally displaced at the ends of these stalks. Many species are strongly sexually dimorphic for eyespan, and these flies have become a model system for studying sexual selection. Using both expressed sequence tag and next-generation sequencing, we have established an extensive database of gene expression in the developing eye-antennal imaginal disc, the adult head and testes. Duplicated genes exhibit narrower expression patterns than nonduplicated genes, and the testes, in particular, provide an abundant source of gene duplication. Within somatic tissue, duplicated genes are more likely to be differentially expressed between the sexes, suggesting gene duplication may provide a mechanism for resolving sexual conflict.

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“…They found that the 20S core PSMA1/α6-subunit of purifi ed sperm proteasomes is distinct from purifi ed egg and muscle proteasomes (Yokota et al 2011 ). Tissue specifi c α-subunits are not commonplace, but several are expressed in the testis of Drosophila (α3T, α4T2, and α6T) (Belote and Zhong 2009 ). Among these testis-specifi c α-subunits, α6T is reported to be crucial for spermatogenesis and fertility (Belote and Zhong 2009 ).…”

Section: Ascidian Fertilizationmentioning

confidence: 99%

“…Tissue specifi c α-subunits are not commonplace, but several are expressed in the testis of Drosophila (α3T, α4T2, and α6T) (Belote and Zhong 2009 ). Among these testis-specifi c α-subunits, α6T is reported to be crucial for spermatogenesis and fertility (Belote and Zhong 2009 ). The α6-subunit of H. roretzi contains a cluster of acidic amino acid residues and the removal of this cluster may mimic the state of dephosphorylation of the α6-subunit which may affect function and localization of the sperm proteasome (Yokota et al 2011 ).…”

Section: Ascidian Fertilizationmentioning

confidence: 99%

Sperm Proteasome as a Putative Egg Coat Lysin in Mammals

Miles

Šutovský

2014

Sexual Reproduction in Animals and Plants

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During animal and human fertilization, the fertilizing spermatozoon creates and passes through a fertilization slit in the vitelline coat (VC) of the oocyte. It has been hypothesized that the penetration of the mammalian VC, the zona pellucida (ZP), is aided by a proteolytic enzyme capable of locally degrading ZP proteins. This putative "zona lysin" is predicted to reside within the sperm head acrosome and be released or exposed by ZP-induced acrosomal exocytosis. Evidence has been accumulating in favor of the 26S proteasome, the ubiquitin-dependent multi-subunit protease acting as the putative vitelline coat/zona lysin in humans and animals. To confi rm this hypothesis, three criteria must be met: (1) the sperm receptor on the ZP must be ubiquitinated, (2) proteasomes must be present, exposed, and enzymatically active in the sperm acrosome, and (3) sperm proteasomes must be able to degrade the sperm receptor on the egg coat/ZP during fertilization. This review discusses recent data from a number of mammalian and nonmammalian models addressing these predictions. These data shed light on the mechanisms controlling sperm interactions with VC and on the evolutionary conservation of the proteasome-assisted fertilization mechanisms.

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Duplicated proteasome subunit genes in Drosophila and their roles in spermatogenesis

Cited by 56 publications

References 47 publications

Actin Cytoskeletal Organization in Drosophila Germline Ring Canals Depends on Kelch Function in a Cullin-RING E3 Ligase

Actin Cytoskeletal Organization in Drosophila Germline Ring Canals Depends on Kelch Function in a Cullin-RING E3 Ligase

Gene duplication, tissue-specific gene expression and sexual conflict in stalk-eyed flies (Diopsidae)

Sperm Proteasome as a Putative Egg Coat Lysin in Mammals

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