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Genomes and Genes | Teru OguraSummaryAffiliation: Kumamoto University Country: Japan Publications
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Publications
Caenorhabditis elegans p97 controls germline-specific sex determination by controlling the TRA-1 level in a CUL-2-dependent mannerYohei Sasagawa
Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
J Cell Sci 122:3663-72. 2009..Our results demonstrate that the C. elegans p97/CDC-48-UFD-1-NPL-4 complex controls the sperm-oocyte switch by regulating CUL-2-mediated TRA-1A proteasome degradation...
Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coliT Ogura
Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
Mol Microbiol 31:833-44. 1999..The biosynthesis of phospholipids and the lipid A moiety of lipopolysaccharide, both of which derive their fatty acyl chains from the same R-3-hydroxyacyl-ACP pool, is regulated by FtsH...- From the common molecular basis of the AAA protein to various energy-dependent and -independent activities of AAA proteinsTeru Ogura
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860 0811, Japan
Biochem Soc Trans 36:68-71. 2008..We have also investigated the roles of C. elegans p97 homologues in aggregation/disaggregation of polyglutamine repeats, and have found that p97 prevents filament formation of polyglutamine proteins in an ATP-independent fashion... - AAA+ superfamily ATPases: common structure--diverse functionT Ogura
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 862 0976, Japan
Genes Cells 6:575-97. 2001..Comparative analyses have also revealed significant similarities and differences in structure and molecular mechanism between AAA+ ATPases and other ring-shaped ATPases... - [AAA family ATPases: ring-shaped chaperones which catalyze energy-dependent conformational changes of proteins]Teru Ogura
Tanpakushitsu Kakusan Koso 47:1182-8. 2002 - [Protein recycling systems in prokaryotic cells]Teru Ogura
Tanpakushitsu Kakusan Koso 49:1047-53. 2004 - [AAA proteins as unfoldases]Teru Ogura
Tanpakushitsu Kakusan Koso 49:1044-6. 2004 - Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPasesTeru Ogura
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 862 0976, Japan
J Struct Biol 146:106-12. 2004..In this review, we will discuss what is known about these critical arginines and what can be concluded about their role in the function of AAA and AAA+ proteins... - Conserved pore residues in the AAA protease FtsH are important for proteolysis and its coupling to ATP hydrolysisTomoko Yamada-Inagawa
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 862 0976, Japan
J Biol Chem 278:50182-7. 2003..These results suggest that Phe228 and Gly230 in the predicted pore region of the FtsH hexamer have important roles in proteolysis and its coupling to ATP hydrolysis... - Flavodoxin, a new fluorescent substrate for monitoring proteolytic activity of FtsH lacking a robust unfolding activityTakashi Okuno
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860 0811, Japan
J Struct Biol 156:115-9. 2006..This newly developed monitoring system will also be applicable for proteolysis by other ATP-dependent proteases... - Spectrometric analysis of degradation of a physiological substrate sigma32 by Escherichia coli AAA protease FtsHTakashi Okuno
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 862 0976, Japan
J Struct Biol 146:148-54. 2004..Although FtsH does not have a robust enough unfoldase activity to unfold a tightly folded proteins such as green fluorescent protein, it can unfold proteins with lower T(m)s such as glutathione S-transferase (T(m) = 52 degrees C)... - An AAA protease FtsH can initiate proteolysis from internal sites of a model substrate, apo-flavodoxinTakashi Okuno
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860 0811, Japan
Genes Cells 11:261-8. 2006.... - Mutational analysis of the functional motifs in the ATPase domain of Caenorhabditis elegans fidgetin homologue FIGL-1: firm evidence for an intersubunit catalysis mechanism of ATP hydrolysis by AAA ATPasesYasufumi Yakushiji
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
J Struct Biol 156:93-100. 2006.... - Caenorhabditis elegans UBX cofactors for CDC-48/p97 control spermatogenesisYohei Sasagawa
Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
Genes Cells 15:1201-15. 2010..Taken together, these results suggest that UBXN-1, UBXN-2 and UBXN-3 are redundant cofactors for CDC-48/p97 and control spermatogenesis via the degradation of TRA-1A... - p97 Homologs from Caenorhabditis elegans, CDC-48.1 and CDC-48.2, suppress the aggregate formation of huntingtin exon1 containing expanded polyQ repeatShingo Nishikori
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
Genes Cells 13:827-38. 2008..1 and CDC-48.2. Taken together, these results suggest that p97 plays a protective role in neurodegenerative disorders by directly suppressing the protein aggregation as a molecular chaperone... 
Positive cooperativity of the p97 AAA ATPase is critical for essential functionsShingo Nishikori
Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto, Japan
J Biol Chem 286:15815-20. 2011..Interestingly, the growth speed of yeast cells strongly related to the positive cooperativity rather than the ATPase activity itself, suggesting that the positive cooperativity is critical for the essential functions of p97...- AAA+ chaperone ClpX regulates dynamics of prokaryotic cytoskeletal protein FtsZShinya Sugimoto
Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
J Biol Chem 285:6648-57. 2010..These data together suggest that ClpX modulates FtsZ polymer dynamics in an ATP-independent fashion, which is achieved by interaction between the N-terminal domain of ClpX and FtsZ monomers or oligomers... - ER E3 ubiquitin ligase HRD-1 and its specific partner chaperone BiP play important roles in ERAD and developmental growth in Caenorhabditis elegansYohei Sasagawa
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
Genes Cells 12:1063-73. 2007..We propose that E3 ubiquitin ligases function in concert with a specific partner chaperone... - Caenorhabditis elegans fidgetin homolog FIGL-1, a nuclear-localized AAA ATPase, binds to SUMOAkinobu Onitake
Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto, Japan
J Struct Biol 179:143-51. 2012..elegans. Taken altogether, our results indicate that FIGL-1 is a nuclear protein and that in concert with SMO-1, FIGL-1 plays an important role in the regulation of C. elegans development... - Caenorhabditis elegans p97/CDC-48 is crucial for progression of meiosis IYohei Sasagawa
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
Biochem Biophys Res Commun 358:920-4. 2007..Furthermore, we found that chromosome condensation was significantly reduced in p97-depleted oocytes. Taken these results altogether, we propose that C. elegans p97 plays an important role in the progression of meiosis... - Characterization of mutants of the Escherichia coli AAA protease, FtsH, carrying a mutation in the central pore regionTakashi Okuno
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860 0811, Japan
J Struct Biol 156:109-14. 2006..Proteolytic activities of most mutants are correlated with their ATPase activities. Evidence also indicated that Val229, the 2nd residue of the @XG motif, may have a substrate-specific role... - The C-terminal α-helix of SPAS-1, a Caenorhabditis elegans spastin homologue, is crucial for microtubule severingAkinobu Onitake
Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
J Struct Biol 179:138-42. 2012.... - CDC-48/p97 is required for proper meiotic chromosome segregation via controlling AIR-2/Aurora B kinase localization in Caenorhabditis elegansYohei Sasagawa
Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
J Struct Biol 179:104-11. 2012..However, the amount and localization of PP1 were not changed by the depletion of CDC-48s. These results suggest that CDC-48s control the restricted localization of AIR-2 to the cohesion sites of homologous chromatids in meiosis I... - The C. elegans homologue of the spastic paraplegia protein, spastin, disassembles microtubulesYuka Matsushita-Ishiodori
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
Biochem Biophys Res Commun 359:157-62. 2007..These results indicate that C. elegans SPAS-1 plays an important role in microtubule dynamics. We also found that two kinds of products were generated from spas-1 by alternative splicing in a developmental stage-dependent manner... - Involvement of HMG-12 and CAR-1 in the cdc-48.1 expression of Caenorhabditis elegansSeiji Yamauchi
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
Dev Biol 318:348-59. 2008..Importantly, we found the decreased expression of p97 in embryos prepared from hmg-12(RNAi) or car-1(RNAi) worms. These results indicate that both HMG-12 and CAR-1 play important roles in embryonic expression of cdc-48.1... - Dissecting various ATP-dependent steps involved in proteasomal degradationTeru Ogura
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860-0976, Japan
Mol Cell 11:3-5. 2003..ATP hydrolysis, activated by binding of substrates to PAN, is utilized for substrate unfolding, gate opening of 20S proteasomes, and substrate translocation... - Differential expression pattern of UBX family genes in Caenorhabditis elegansSeiji Yamauchi
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto, Japan
Biochem Biophys Res Commun 358:545-52. 2007..These results altogether demonstrate that the expression of all six ubxn genes of C. elegans is differently regulated... - Conserved aromatic and basic amino acid residues in the pore region of Caenorhabditis elegans spastin play critical roles in microtubule severingYuka Matsushita-Ishiodori
Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
Genes Cells 14:925-40. 2009..We also detected the direct interaction of the extremely acidic C-terminal polypeptide of tubulin with SPAS-1. Consequently, we propose that the central pore residues are important for the recognition of substrates... - The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expressionT Tomoyasu
Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
J Bacteriol 175:1344-51. 1993..g., Sec18p, Pas1p, CDC48p, and TBP-1, which function in protein transport pathways, peroxisome assembly, cell division cycle, and gene expression, respectively. Possible implications of these observations are discussed... - Heat shock regulation in the ftsH null mutant of Escherichia coli: dissection of stability and activity control mechanisms of sigma32 in vivoT Tatsuta
Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Kumamoto 862 0976, Japan
Mol Microbiol 30:583-93. 1998..In addition, CbpA, an analogue of DnaJ, was demonstrated to have overlapping functions with DnaJ in both the activity and the stability control of sigma32... - Defective plasmid partition in ftsH mutants of Escherichia coliT Inagawa
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Japan
Mol Genet Genomics 265:755-62. 2001..It is likely that altered membrane structure affects the localization or activity of a putative plasmid partitioning apparatus located at positions equivalent to 1/4 and 3/4 of the cell length... - Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsHK Karata
Department of Molecular Cell Biology, Institute of Molecular Embryology, Kumamoto University School of Medicine, Kumamoto 862 0976, Japan
J Biol Chem 274:26225-32. 1999.... - Topology and subcellular localization of FtsH protein in Escherichia coliT Tomoyasu
Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
J Bacteriol 175:1352-7. 1993..The average number of FtsH molecules per cell was estimated to be approximately 400... - Analysis of the two p97/VCP/Cdc48p proteins of Caenorhabditis elegans and their suppression of polyglutamine-induced protein aggregationKunitoshi Yamanaka
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 862 0976, Japan
J Struct Biol 146:242-50. 2004..The formation of aggregates was partially suppressed by co-expression of either C41C4.8 or C06A1.1. These results suggest that these p97/VCP/Cdc48p homologues, AAA chaperones, may play a protective role in polyQ aggregation... - Comparative analysis of expression of two p97 homologues in Caenorhabditis elegansSeiji Yamauchi
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2-2-1 Honjo, Kumamoto 860-0811, Japan
Biochem Biophys Res Commun 345:746-53. 2006..2::GFP was expressed mainly in embryos. These results suggest that the expression of two p97 homologues of C. elegans is differently regulated and independent of each other... - Identification of two new genes, mukE and mukF, involved in chromosome partitioning in Escherichia coliK Yamanaka
Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Japan
Mol Gen Genet 250:241-51. 1996..These results indicate that the MukF, MukE, and MukB proteins are involved in the chromosome partitioning steps, but are not required for mini-F plasmid partitioning... - Probing the mechanism of ATP hydrolysis and substrate translocation in the AAA protease FtsH by modelling and mutagenesisK Karata
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 862 0976, Japan
Mol Microbiol 39:890-903. 2001..Furthermore, comparative structural analysis of FtsH and a related ATPase, HslU, reveals interesting similarities and differences in mechanism... - Phosphorylation of Kif26b promotes its polyubiquitination and subsequent proteasomal degradation during kidney developmentTakeshi Terabayashi
Department of Kidney Development, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto, Japan
PLoS ONE 7:e39714. 2012..These results suggest that the function of Kif26b is microtubule-based and that Kif26b degradation in the metanephric mesenchyme via the ubiquitin-proteasome pathway may be important for proper kidney development... - Cdc48p/p97-mediated regulation of mitochondrial morphology is Vms1p-independentMasatoshi Esaki
Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Honjo 2 2 1, Kumamoto 860 0811, Japan
J Struct Biol 179:112-20. 2012..These results suggest that Cdc48p controls mitochondrial morphology by regulating turnover of proteins involved in mitochondrial morphology in a Vms1p-independent manner... - Recent advances in p97/VCP/Cdc48 cellular functionsKunitoshi Yamanaka
Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
Biochim Biophys Acta 1823:130-7. 2012..In this review, we will summarize and discuss recent progress and topics in p97 functions and the relationship to its associated diseases... - ATP-bound form of the D1 AAA domain inhibits an essential function of Cdc48p/p97Masatoshi Esaki
Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
Biochem Cell Biol 88:109-17. 2010..Site-directed and random mutagenesis analyses suggest that the ATP-bound form of D1 changes an inter-domain interaction, thereby perturbing an essential function of Cdc48p/p97... - [Neurodegenerative disease models of AAA proteins in C. elegans]Kunitoshi Yamanaka
Tanpakushitsu Kakusan Koso 49:1124-6. 2004 - Multicopy suppressors, mssA and mssB, of an smbA mutation of Escherichia coliK Yamanaka
Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
Mol Gen Genet 243:9-16. 1994..MssA and MssB might also relate to the expression of some of these genes. Multiple copies mssA and mssB suppressed the various phenotypic features of the smbA2 mutant to various extents, suppressing the cold-sensitive growth completely... - E.coli MukB protein involved in chromosome partition forms a homodimer with a rod-and-hinge structure having DNA binding and ATP/GTP binding activitiesH Niki
Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
EMBO J 11:5101-9. 1992..Photoaffinity cross-linking experiments showed that MukB binds to ATP and GTP in the presence of Zn2+. Throughout the purification steps, acyl carrier protein was co-purified with MukB... - Carboxyl terminal region of the MukB protein in Escherichia coli is essential for DNA binding activityA Z Saleh
Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
FEMS Microbiol Lett 143:211-6. 1996..This mutant MukB protein was defective for DNA binding, while the ATP binding activity remained unaffected. A truncated MukB protein that is short of 109 amino acids from the C-terminus failed to bind DNA... - Characterization of translucent segments observed in an smbA mutant of Escherichia coliK Yamanaka
Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Japan
FEMS Microbiol Lett 116:61-6. 1994..Electron microscopic observation revealed that the translucent segments resulted from the enlargement of a periplasmic space by separation of the inner membrane from the peptidoglycan layer and the outer membrane... - Identification of a cysteine residue important for the ATPase activity of C. elegans fidgetin homologueYasufumi Yakushiji
Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 862 0976, Japan
FEBS Lett 578:191-7. 2004..These results suggest that the unique position of cysteine 368, located immediately downstream of the Walker A motif, plays an important role in the ATP hydrolysis process of C. elegans F32D1.1 protein... - Identification and characterization of the smbA gene, a suppressor of the mukB null mutant of Escherichia coliK Yamanaka
Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
J Bacteriol 174:7517-26. 1992..The smbA mutants are sensitive to a detergent, sodium dodecyl sulfate, and they show a novel morphological phenotype under nonpermissive conditions, suggesting a defect in specific membrane sites... - RNase E polypeptides lacking a carboxyl-terminal half suppress a mukB mutation in Escherichia coliM Kido
Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Kumamoto, Japan
J Bacteriol 178:3917-25. 1996..RNase E and PNPase of the multiprotein complex presumably cooperate for effective processing and turnover of specific substrates, such as mRNAs and other RNAs in vivo... - New killing system controlled by two genes located immediately upstream of the mukB gene in Escherichia coliJ Feng
Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
Mol Gen Genet 243:136-47. 1994..It was also demonstrated that KicA and KicB can function as a post-segregational killing system, when the genes are transferred from the E. coli chromosome onto a plasmid... - Cloning, sequencing, and characterization of multicopy suppressors of a mukB mutation in Escherichia coliK Yamanaka
Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
Mol Microbiol 13:301-12. 1994..Hence, the msmB and msmC genes were renamed cspC and cspE, respectively. Possible mechanisms for suppression of the mukB106 mutation are discussed... - Two mutant alleles of mukB, a gene essential for chromosome partition in Escherichia coliK Yamanaka
Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
FEMS Microbiol Lett 123:27-31. 1994.... - Identification of the cpdA gene encoding cyclic 3',5'-adenosine monophosphate phosphodiesterase in Escherichia coliR Imamura
Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Kumamoto, Kumamoto 862, Japan
J Biol Chem 271:25423-9. 1996..Our results suggested that regulation of intracellular concentration of cAMP is dependent not only on synthesis of cAMP but also on hydrolysis of cAMP by cAMP phosphodiesterase... - Characterization of the smtA gene encoding an S-adenosylmethionine-dependent methyltransferase of Escherichia coliK Yamanaka
Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
FEMS Microbiol Lett 133:59-63. 1995..The smtA gene is not essential for cell growth and its expression is positively regulated by H-NS, an Escherichia coli histone-like protein... - Allelic characterization of the leaf-variegated mutation var2 identifies the conserved amino acid residues of FtsH that are important for ATP hydrolysis and proteolysisWataru Sakamoto
Research Institute for Bioresources, Okayama University, 2 20 1 Chuo, Kurashiki, Okayama 710 0046, Japan
Plant Mol Biol 56:705-16. 2004..Based on these results, we propose that the conserved Gly-Ala-Asp motif plays an important role in FtsH activity. Thus, characterization of the var2 alleles could help to identify the physiologically important domain of FtsH... - Crystallization of the AAA domain of the ATP-dependent protease FtsH of Escherichia coliSzymon Krzywda
Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, England
Acta Crystallogr D Biol Crystallogr 58:1066-7. 2002..The ATPase domain of FtsH from Escherichia coli has been crystallized from ammonium sulfate solutions and crystals diffracting to 1.5 A resolution have been obtained... - The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 A resolutionSzymon Krzywda
Structural Biology Laboratory, Department of Chemistry, University of York, United Kingdom
Structure 10:1073-83. 2002..A sulfate anion in the ATP binding pocket mimics the beta-phosphate group of an adenine nucleotide. A hexamer form of FtsH has been modeled, providing insights into possible modes of nucleotide binding and intersubunit catalysis... - C. elegans RBX-2-CUL-5- and RBX-1-CUL-2-based complexes are redundant for oogenesis and activation of the MAP kinase MPK-1Yohei Sasagawa
Graduate School of Life Sciences, Tohoku University, 2 1 1 Katahira, Aoba, Sendai, Miyagi, Japan
FEBS Lett 581:145-50. 2007..Yeast two-hybrid analysis and RNAi-knockdown experiments suggest that oocyte maturation from pachytene exit and MPK-1 activation are redundantly controlled by the RBX-2-CUL-5- and RBX-1-CUL-2-based complexes...