The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
mbk-2 encodes MBK-2, a maternally supplied DYRK-family dual-specificity protein kinase that is activated during the oocyte-to-embryo transition (OET) and phosphorylates key maternal regulators to (i) switch their functions and (ii) mark them for ubiquitin–proteasome-dependent degradation. Its best-supported direct substrates are the oocyte RNA-binding protein OMA-1 (phosphorylation at T239) and the meiotic microtubule-severing enzyme katanin catalytic subunit MEI-1 (phosphorylation at S92; plus additional N-terminal sites affecting enzymatic activity). MBK-2 activation is tightly coupled to meiotic progression via regulated cortical sequestration (EGG-3/EGG-4/EGG-5), CDK-1 phosphorylation, and APC/C-dependent release, enabling phosphorylation of cytoplasmic substrates during meiosis/meiotic exit. Quantitative genetic and biochemical experiments demonstrate MBK-2 is essential for embryonic viability and for coordinated clearance/inactivation of meiotic and maternal factors. (stitzel2006thec.elegans pages 1-2, robertson2013theoocytetoembryotransition. pages 13-15, joly2020phosphorylationofthe pages 4-6)
The retrieved primary literature consistently defines MBK-2 as the C. elegans DYRK-family kinase required for the oocyte-to-embryo transition, matching the UniProt Q9XTF3 description (minibrain/Yak1-related DYRK; EC 2.7.12.1). MBK-2 is distinct from other DYRK-family members in the worm (e.g., MBK-1) and is studied primarily in the context of meiosis and early embryogenesis. (stitzel2006thec.elegans pages 1-2, pellettieri2003coordinateactivationof pages 7-8, robertson2013theoocytetoembryotransition. pages 13-15)
Oocyte-to-embryo transition (OET): a developmental switch spanning meiotic maturation/fertilization through meiotic divisions and entry into the first embryonic mitosis, requiring timed remodeling of maternal proteins and RNAs. MBK-2 is a central kinase in this transition. (robertson2013theoocytetoembryotransition. pages 13-15)
DYRK kinases: an evolutionarily conserved family of “dual-specificity tyrosine phosphorylation-regulated kinases,” with broad roles in cell-cycle control and protein stability. Reviews highlight a recurrent DYRK theme: phosphorylation can act as a priming event enabling subsequent phosphorylation (e.g., by GSK-3) and/or recognition by ubiquitin ligases, linking kinase signaling to regulated proteolysis. (becker2012emergingroleof pages 1-3, becker2012emergingroleof pages 3-4)
MBK-2 is a protein kinase that transfers phosphate from ATP to protein substrates (Ser/Thr targets; “dual specificity” refers to tyrosine-related regulation and/or autophosphorylation within the DYRK family). Functionally critical activity is demonstrated by rescue experiments: a wild-type GFP::MBK-2 transgene restores substantial viability to mbk-2 maternal mutants, whereas a kinase-dead MBK-2 (K196R) does not. (stitzel2006thec.elegans pages 1-2)
Quantitative genetics: In mbk-2(pk1427) maternal mutants, embryo viability was 0% (n=1063); expression of GFP::MBK-2 rescued to 80% viability (n=569); kinase-dead GFP::MBK-2(K196R) rescued 0% (n=198). (stitzel2006thec.elegans pages 1-2)
Primary evidence indicates MBK-2 directly phosphorylates OMA-1 at T239 in vitro and that T239 phosphorylation occurs in vivo shortly after meiosis II (detected with a phospho-specific antibody). T239 phosphorylation also primes subsequent phosphorylation by GSK-3 at T339 (a distant site), and mutations at either site delay OMA-1 degradation in early embryos. (nishi2007studyofoocytetoembryo pages 85-89)
An authoritative OET review synthesizes the functional consequences: OMA-1 T239 phosphorylation acts as a molecular switch (e.g., enabling association with transcriptional machinery component TAF-4 and marking OMA-1 for degradation after the first mitosis), and reduced T239 phosphorylation (e.g., oma-1(zu405) P240L) causes persistence and embryonic lethality. (robertson2013theoocytetoembryotransition. pages 13-15)
MBK-2 directly phosphorylates MEI-1 on S92, a DYRK consensus site overlapping a PEST motif; an S92A substitution reduces phosphorylation and causes persistence of MEI-1 past the first mitosis in vivo. (stitzel2006thec.elegans pages 1-2)
A detailed mechanistic update showed that MBK-2 phosphorylates the katanin complex at multiple N-terminal regulatory sites on MEI-1 (S90, S92, S113, S137) and also phosphorylates MEI-2 (T32, S68, S86; MEI-2 phosphorylation requires MEI-1). LC-MS/MS plus in vitro kinase assays identify S92 as the dominant MBK-2 site: an S92G variant reduced radiolabeled phosphate incorporation by ~80%, supporting “S92 is the main residue phosphorylated by MBK-2.” (joly2020phosphorylationofthe pages 4-6, joly2020phosphorylationofthe pages 2-4)
Critically, MBK-2 phosphorylation alters katanin biochemistry:
- Microtubules normally stimulate katanin ATPase activity by ~2–3-fold, but this stimulation is abolished when katanin is prephosphorylated by MBK-2 (phosphorylation makes katanin “insensitive” to MT stimulation). (joly2020phosphorylationofthe pages 4-6, joly2020phosphorylationofthe pages 2-4)
- S92 phosphorylation is necessary and sufficient to promote MEI-1 binding to the MEL-26 adaptor and to target MEI-1 for degradation; a nonphosphorylatable S92A accumulates at ~3-fold higher levels and shows strong centrosome/chromosome localization with spindle defects, whereas S92D resembles WT for accumulation in this context. (joly2020phosphorylationofthe pages 8-10, joly2020phosphorylationofthe pages 10-12)
Early work established MBK-2 as an essential temporal regulator that enables coordinated degradation of maternal proteins during the egg-to-embryo transition. MBK-2 is required for degradation of OMA-1 and MEI-1/MEI-2, and for regulated degradation of PIE-1 (in specific embryonic regions), and is epistatic to PAR-1 for PIE-1 degradation. (pellettieri2003coordinateactivationof pages 7-8, pellettieri2003coordinateactivationof pages 8-9)
MBK-2-dependent degradation is not a global proteolysis activation; rather, MBK-2 appears to confer “degradation competence” to specific substrates, consistent with phosphorylation-dependent recognition by ubiquitin ligases. (pellettieri2003coordinateactivationof pages 8-9)
Evidence across studies supports a model in which MBK-2 phosphorylation feeds into distinct ubiquitin pathways:
- For MEI-1, MBK-2 phosphorylation (S92) precedes recognition by the MEL-26/CUL-3 (CRL3) machinery to drive proteasomal degradation. (stitzel2006thec.elegans pages 1-2, joly2020phosphorylationofthe pages 8-10)
- For OMA-1, MBK-2 phosphorylation at T239 primes additional phosphorylation (e.g., by GSK-3 at T339) and promotes destruction; an expert review of DYRKs frames this as a paradigm of DYRKs acting as priming kinases that link phosphorylation to E3 ligase recognition, with MBK-2 specifically described as initiating GSK-3 phosphorylation and subsequent recognition by a CUL2-based E3 ligase for OMA proteins. (nishi2007studyofoocytetoembryo pages 85-89, becker2012emergingroleof pages 3-4)
Beyond degradation, MBK-2 is required for proper posterior enrichment/segregation of germ plasm components (PIE-1 and P granules) even in embryos that proceed through meiotic divisions, supporting an integrated role in early embryonic asymmetry. (pellettieri2003coordinateactivationof pages 8-9, pellettieri2003coordinateactivationof pages 9-10)
Live imaging with GFP::MBK-2 demonstrates a tightly stage-coupled relocalization:
- In oocytes and newly fertilized zygotes, MBK-2 is predominantly cortical.
- Around the meiosis I → meiosis II transition it becomes punctate at the cortex; quantitatively, cortical foci are seen in 0/9 embryos at meiosis I metaphase/anaphase, 3/4 at telophase I/prophase II, and 18/18 at meiosis II metaphase/anaphase. (pellettieri2003coordinateactivationof pages 7-8)
- With meiotic progression/exit, MBK-2 redistributes into the cytoplasm, and by mitosis it localizes to centrosomes and chromosomes; it can also associate with P granules in germline blastomeres. (pellettieri2003coordinateactivationof pages 7-8)
A subsequent mechanistic description emphasizes a two-step relocalization: cortex → cortical puncta (anaphase/telophase I) → cytoplasm (during meiosis II and meiotic exit). (stitzel2006thec.elegans pages 3-4)
An authoritative OET review summarizes a regulatory framework:
- MBK-2 is co-translationally autophosphorylated on a tyrosine in a YTY motif, which is required for activity.
- In oocytes, MBK-2 activity is restrained by binding to pseudo-tyrosine phosphatases EGG-4/EGG-5, which recognize the phosphorylated YTY motif, and by EGG-3, which tethers the complex to the cortex.
- CDK-1 phosphorylates MBK-2 on S68, promoting release from an unknown repressor.
- APC/C activity at the meiosis I metaphase→anaphase transition promotes proteasomal degradation of EGG proteins, releasing MBK-2 into the cytoplasm where it can access substrates.
- Phosphorylated MBK-2 substrates become detectable in 1-cell embryos at anaphase of meiosis I and peak after completion of meiosis II. (robertson2013theoocytetoembryotransition. pages 13-15)
Primary imaging/genetics also support APC/C coupling: arrest in meiosis I via mat-1(RNAi) (an APC subunit) prevents MBK-2 relocalization; 78% of mat-1(RNAi) embryos retained uniform cortical GFP::MBK-2 (n=292). (pellettieri2003coordinateactivationof pages 7-8)
Key quantitative/statistical findings from the mechanistic literature include:
- Essentiality: 0% vs 80% rescue of embryonic viability depending on MBK-2 catalytic competence (n values above). (stitzel2006thec.elegans pages 1-2)
- Localization timing: MBK-2 cortical foci appearing specifically after meiosis I and during meiosis II (0/9, 3/4, 18/18). (pellettieri2003coordinateactivationof pages 7-8)
- Substrate phosphorylation contribution: MEI-1 S92 is dominant (~80% drop in 32P incorporation when mutated) and drives a ~3× accumulation phenotype in vivo when nonphosphorylatable. (joly2020phosphorylationofthe pages 4-6, joly2020phosphorylationofthe pages 8-10)
- Enzyme regulation: MBK-2 phosphorylation removes the typical ~2–3× microtubule stimulation of katanin ATPase activity. (joly2020phosphorylationofthe pages 4-6, joly2020phosphorylationofthe pages 2-4)
MBK-2 is widely used as an experimental entry point to study how meiotic cell-cycle transitions gate biochemical remodeling of maternal proteins. Concrete implementations include:
- Live imaging of GFP::MBK-2 and stage-resolved relocalization phenotyping to read out meiotic progression-dependent kinase control. (pellettieri2003coordinateactivationof pages 7-8, stitzel2006thec.elegans pages 3-4)
- Reporter-based proteostasis assays (OMA-1::GFP, GFP::MEI-1) combined with targeted phosphosite mutants (e.g., OMA-1 T239A/T239D; MEI-1 S92A/S92D) to dissect phosphorylation-to-degradation logic. (nishi2007studyofoocytetoembryo pages 85-89, stitzel2006thec.elegans pages 1-2, joly2020phosphorylationofthe pages 8-10)
- Reconstituted biochemistry of phosphorylation-dependent regulation of a cytoskeletal AAA+ enzyme (katanin), connecting developmental genetics to mechanistic enzymology (ATPase assays; MEL-26 binding). (joly2020phosphorylationofthe pages 4-6, joly2020phosphorylationofthe pages 10-12)
Expert reviews place MBK-2 within a broader DYRK theme: DYRK-family kinases frequently control protein stability and can function as priming kinases that enable downstream phosphorylation and ubiquitin-ligase recognition. In this framing, MBK-2 exemplifies a developmental “timer” that couples meiotic progression to selective proteasomal destruction of oocyte proteins to permit embryonic mitoses. (becker2012emergingroleof pages 1-3, becker2012emergingroleof pages 3-4)
Targeted attempts to retrieve 2023–2024 peer-reviewed, mbk-2-focused mechanistic studies within the available tool-retrieved corpus did not yield extractable MBK-2-specific evidence. As a result, the most recent mechanistic primary study available in this run is Joly et al. 2020 (J Cell Biol) on MBK-2 phosphorylation of katanin. This report therefore reflects the current best-supported mechanistic consensus from foundational (2003–2006) and follow-up mechanistic (2020) literature, complemented by authoritative reviews. (joly2020phosphorylationofthe pages 4-6, robertson2013theoocytetoembryotransition. pages 13-15)
The following table consolidates key roles, mechanisms, substrates, and quantitative findings across sources.
| Process/role | Molecular mechanism | Substrate (protein) and phosphosite(s) | Evidence type | Key quantitative/phenotypic data | Primary source with year, DOI, and URL |
|---|---|---|---|---|---|
| Identity and core biochemical function in the oocyte-to-embryo transition | MBK-2 is a maternally supplied DYRK-family dual-specificity kinase whose kinase activity is essential for marking a subset of maternal proteins for timed post-meiotic turnover; activity depends on catalytic competence and DYRK-like phosphorylation of Ser/Thr substrates in consensus motifs | MEI-1 S92; OMA-1 DYRK consensus site affected by P240L mutation; not POS-1 in vitro (stitzel2006thec.elegans pages 1-2, robertson2013theoocytetoembryotransition. pages 13-15) | In vitro kinase assays; transgenic rescue; genetics | mbk-2(pk1427) maternal embryos: 0% viability (n=1063); GFP::MBK-2 rescue: 80% viability (n=569); kinase-dead GFP::MBK-2(K196R): 0% viability (n=198) (stitzel2006thec.elegans pages 1-2) | Stitzel et al., 2006. DOI: 10.1016/j.cub.2005.11.063. URL: https://doi.org/10.1016/j.cub.2005.11.063 |
| Timed degradation of maternal proteins after meiosis | MBK-2 functions as a temporal activator of maternal protein degradation during the egg-to-embryo transition, likely by phosphorylation that creates degradation competence after meiotic progression | PIE-1, OMA-1, MEI-1/MEI-2; phosphosites not mapped in this study (pellettieri2003coordinateactivationof pages 7-8, pellettieri2003coordinateactivationof pages 8-9) | Live imaging/genetics with GFP reporters; epistasis | GFP::PIE-1ZF1 failed to degrade in mbk-2(RNAi) embryos (n=8); OMA-1::GFP persisted in 34/34 mat-1 zygotes; GFP::MEI-1 persisted in 40/44 mat-1 zygotes (pellettieri2003coordinateactivationof pages 7-8, pellettieri2003coordinateactivationof pages 8-9) | Pellettieri et al., 2003. DOI: 10.1016/S1534-5807(03)00231-4. URL: https://doi.org/10.1016/S1534-5807(03)00231-4 |
| OMA-1 destruction and remodeling of OMA-1 function | MBK-2 directly phosphorylates OMA-1 at T239; this acts as a molecular switch promoting later degradation and enabling OMA-1 functional transition; T239 phosphorylation primes subsequent GSK-3 phosphorylation at T339 | OMA-1 T239; GSK-3-dependent downstream T339; oma-1(zu405) P240L reduces T239 phosphorylation (nishi2007studyofoocytetoembryo pages 85-89, robertson2013theoocytetoembryotransition. pages 13-15) | In vitro kinase assay; phospho-specific antibody in vivo; phosphomimetic/nonphosphorylatable reporter genetics | T239 phosphorylation detected shortly after meiosis II; T239D enhances later T339 phosphorylation; T239A and T339A delay degradation of OMA-1::GFP; reduced T239 phosphorylation in oma-1(zu405) causes persistence past 1-cell stage and embryonic lethality (nishi2007studyofoocytetoembryo pages 85-89, robertson2013theoocytetoembryotransition. pages 13-15) | Nishi, 2007; summarized by Robertson & Lin, 2013. DOI: 10.1007/978-1-4614-4015-4_12. URL: https://doi.org/10.1007/978-1-4614-4015-4_12 |
| OMA-1 destruction in the first embryonic cell cycle | MBK-2 is one of several conserved kinases that promote OMA-1 destruction during the oocyte-to-embryo transition; OMA-1 destruction permits downstream ZIF-1-dependent proteolysis of cell-fate determinants | OMA-1; site not specified in this source (shirayama2006theconservedkinases pages 1-2) | Mutant isolation/genetics | OMA-1 peaks in maturing oocytes and begins to disappear only after the fertilized egg enters the first mitosis; mbk-2 mutation stabilizes OMA-1, and this stabilization is partially suppressed by oma-1 loss-of-function (shirayama2006theconservedkinases pages 1-2) | Shirayama et al., 2006. DOI: 10.1016/j.cub.2005.11.070. URL: https://doi.org/10.1016/j.cub.2005.11.070 |
| MEI-1 degradation at the meiosis-to-mitosis transition | MBK-2 directly phosphorylates MEI-1 on S92, a DYRK consensus site overlapping a PEST sequence; phosphorylation precedes and is required for developmental degradation | MEI-1 S92 (stitzel2006thec.elegans pages 1-2) | In vitro kinase assay; phospho-S92 antibody in vivo; mutant reporter genetics | GFP::MEI-1(R36C) is degraded at meiosis-to-mitosis transition, whereas GFP::MEI-1(R36C,S92A) persists past first mitosis; phosphorylation/degradation occur in unfertilized spe-9 eggs, are blocked by meiotic arrest, and accelerated by wee-1.3(RNAi) (stitzel2006thec.elegans pages 1-2) | Stitzel et al., 2006. DOI: 10.1016/j.cub.2005.11.063. URL: https://doi.org/10.1016/j.cub.2005.11.063 |
| Katanin regulation: stability and enzymatic inhibition | MBK-2 phosphorylates the katanin complex in the N-terminal regulatory region of MEI-1; S92 is the principal site for degradation targeting, while phosphorylation of N-terminal sites suppresses MT-stimulated ATPase activity | MEI-1 S90, S92, S113, S137; MEI-2 T32, S68, S86 (MEI-2 phosphorylation requires MEI-1) (joly2020phosphorylationofthe pages 4-6, joly2020phosphorylationofthe pages 2-4, joly2020phosphorylationofthe pages 10-12) | LC-MS/MS; in vitro kinase assays; ATPase assays; MEL-26 binding assays; in vivo mutant analysis | S92G reduces 32P incorporation by ~80%; MTs normally stimulate katanin ATPase ~2–3-fold, but this stimulation is lost after MBK-2 phosphorylation; S92 phosphorylation is necessary and sufficient for MEL-26 binding/degradation targeting; nonphosphorylatable S92A accumulates to ~3-fold higher levels and causes spindle defects, whereas S92D resembles WT for accumulation (joly2020phosphorylationofthe pages 4-6, joly2020phosphorylationofthe pages 8-10, joly2020phosphorylationofthe pages 10-12) | Joly et al., 2020. DOI: 10.1083/jcb.201912037. URL: https://doi.org/10.1083/jcb.201912037 |
| Cell-cycle-linked activation and localization control | MBK-2 is restrained in oocytes by cortical anchoring with EGG-3/EGG-4/5; it autophosphorylates on a YTY motif during translation, CDK-1 phosphorylates S68, and APC/C-dependent release/degradation of EGG proteins allows active MBK-2 to access cytoplasmic substrates | MBK-2 regulatory sites: YTY autophosphorylation motif; S68 phosphorylation by CDK-1 (robertson2013theoocytetoembryotransition. pages 13-15) | Review synthesis of prior primary studies; localization and regulatory genetics summarized | Phosphorylated substrates first detectable in 1-cell embryos at anaphase of meiosis I and peak after second polar body extrusion; MBK-2 is cortical before sperm signal, then relocalizes to cytoplasmic puncta through meiosis II (robertson2013theoocytetoembryotransition. pages 13-15) | Robertson & Lin, 2013. DOI: 10.1007/978-1-4614-4015-4_12. URL: https://doi.org/10.1007/978-1-4614-4015-4_12 |
| Dynamic relocalization during meiosis | MBK-2 relocalizes in a two-step, cell-cycle-dependent manner from uniform cortex to cortical puncta and then into cytoplasm; progression through meiosis, not fertilization, is the trigger | No substrate phosphosite; localization behavior of MBK-2 itself (pellettieri2003coordinateactivationof pages 7-8, stitzel2006thec.elegans pages 3-4, stitzel2006thec.elegans pages 1-2) | GFP::MBK-2 live imaging; cell-cycle perturbation genetics | Cortical foci in 0/9 meiosis I metaphase/anaphase embryos, 3/4 telophase I/prophase II embryos, and 18/18 meiosis II metaphase/anaphase embryos; 78% of mat-1(RNAi) embryos (n=292) retained uniform cortical MBK-2; kinase-dead K196R showed aberrant spindle localization in 37/66 embryos vs 0/43 WT (pellettieri2003coordinateactivationof pages 7-8, stitzel2006thec.elegans pages 1-2, stitzel2006thec.elegans pages 3-4) | Pellettieri et al., 2003; Stitzel et al., 2006. DOI: 10.1016/S1534-5807(03)00231-4; 10.1016/j.cub.2005.11.063. URLs: https://doi.org/10.1016/S1534-5807(03)00231-4 ; https://doi.org/10.1016/j.cub.2005.11.063 |
| Early embryonic polarity and germ-plasm asymmetry | MBK-2 is required not only for degradation but also for proper posterior enrichment/segregation of PIE-1 and P granules, acting downstream of meiotic progression and independently of general microtubule failure | PIE-1 and germ-plasm regulators; phosphosite(s) not mapped here (pellettieri2003coordinateactivationof pages 8-9, pellettieri2003coordinateactivationof pages 9-10) | Genetics; live imaging/phenotypic analysis | mbk-2 mutants proceed through meiosis into mitosis but fail to localize P granules and POS-1 properly and fail to degrade maternal proteins; PIE-1::GFP asymmetry averaged 2.0 embryos per gonad in mat-1(ax227) (n=28) and mat-1(ax227); mbk-2(RNAi) (n=29) backgrounds (pellettieri2003coordinateactivationof pages 8-9, pellettieri2003coordinateactivationof pages 9-10) | Pellettieri et al., 2003. DOI: 10.1016/S1534-5807(03)00231-4. URL: https://doi.org/10.1016/S1534-5807(03)00231-4 |
| Developmental necessity and phenotype spectrum | Maternal MBK-2 is essential for meiosis-to-mitosis transition and early embryogenesis; defective turnover of meiotic and cell-fate regulators explains pleiotropic 1-cell defects | MEI-1, OMA-1, PIE-1, MEX-5, POS-1; specific sites variably defined in later work (nishi2007studyofoocytetoembryo pages 38-42, nishi2007studyofoocytetoembryo pages 85-89) | Maternal-effect genetics; suppression by mei-1 depletion; reporter analysis | mbk-2 loss causes penetrant maternal-effect embryonic lethality; embryos complete meiosis and extrude two polar bodies but fail mitotic spindle formation because MEI-1 persists ectopically on the mitotic spindle; spindle defect is suppressed by mei-1 depletion (nishi2007studyofoocytetoembryo pages 38-42) | Nishi, 2007. URL not available in gathered snippet; dissertation-like source summarized in evidence (nishi2007studyofoocytetoembryo pages 38-42) |
Table: This table compiles experimentally supported functional annotation for C. elegans MBK-2 (UniProt Q9XTF3), including substrates, phosphosites, regulatory mechanisms, localization dynamics, and key quantitative phenotypes. It is useful as a source-by-source evidence map for writing a rigorous gene function report.
References
(stitzel2006thec.elegans pages 1-2): Michael L. Stitzel, Jason Pellettieri, and Geraldine Seydoux. The c. elegans dyrk kinase mbk-2 marks oocyte proteins for degradation in response to meiotic maturation. Current Biology, 16:56-62, Jan 2006. URL: https://doi.org/10.1016/j.cub.2005.11.063, doi:10.1016/j.cub.2005.11.063. This article has 129 citations and is from a highest quality peer-reviewed journal.
(robertson2013theoocytetoembryotransition. pages 13-15): Scott Robertson and Rueyling Lin. The oocyte-to-embryo transition. Advances in experimental medicine and biology, 757:351-72, Jun 2013. URL: https://doi.org/10.1007/978-1-4614-4015-4_12, doi:10.1007/978-1-4614-4015-4_12. This article has 55 citations and is from a peer-reviewed journal.
(joly2020phosphorylationofthe pages 4-6): Nicolas Joly, Eva Beaumale, Lucie Van Hove, Lisa Martino, and Lionel Pintard. Phosphorylation of the microtubule-severing aaa+ enzyme katanin regulates c. elegans embryo development. The Journal of Cell Biology, May 2020. URL: https://doi.org/10.1083/jcb.201912037, doi:10.1083/jcb.201912037. This article has 17 citations.
(pellettieri2003coordinateactivationof pages 7-8): Jason Pellettieri, Valerie Reinke, Stuart K. Kim, and Geraldine Seydoux. Coordinate activation of maternal protein degradation during the egg-to-embryo transition in c. elegans. Developmental cell, 5 3:451-62, Sep 2003. URL: https://doi.org/10.1016/s1534-5807(03)00231-4, doi:10.1016/s1534-5807(03)00231-4. This article has 171 citations and is from a highest quality peer-reviewed journal.
(becker2012emergingroleof pages 1-3): Walter Becker. Emerging role of dyrk family protein kinases as regulators of protein stability in cell cycle control. Cell Cycle, 11:3389-3394, Sep 2012. URL: https://doi.org/10.4161/cc.21404, doi:10.4161/cc.21404. This article has 131 citations and is from a peer-reviewed journal.
(becker2012emergingroleof pages 3-4): Walter Becker. Emerging role of dyrk family protein kinases as regulators of protein stability in cell cycle control. Cell Cycle, 11:3389-3394, Sep 2012. URL: https://doi.org/10.4161/cc.21404, doi:10.4161/cc.21404. This article has 131 citations and is from a peer-reviewed journal.
(nishi2007studyofoocytetoembryo pages 85-89): Y Nishi. Study of oocyte-to-embryo transition regulators, oma-1 and oma-2 in c. elegans. Unknown journal, 2007.
(joly2020phosphorylationofthe pages 2-4): Nicolas Joly, Eva Beaumale, Lucie Van Hove, Lisa Martino, and Lionel Pintard. Phosphorylation of the microtubule-severing aaa+ enzyme katanin regulates c. elegans embryo development. The Journal of Cell Biology, May 2020. URL: https://doi.org/10.1083/jcb.201912037, doi:10.1083/jcb.201912037. This article has 17 citations.
(joly2020phosphorylationofthe pages 8-10): Nicolas Joly, Eva Beaumale, Lucie Van Hove, Lisa Martino, and Lionel Pintard. Phosphorylation of the microtubule-severing aaa+ enzyme katanin regulates c. elegans embryo development. The Journal of Cell Biology, May 2020. URL: https://doi.org/10.1083/jcb.201912037, doi:10.1083/jcb.201912037. This article has 17 citations.
(joly2020phosphorylationofthe pages 10-12): Nicolas Joly, Eva Beaumale, Lucie Van Hove, Lisa Martino, and Lionel Pintard. Phosphorylation of the microtubule-severing aaa+ enzyme katanin regulates c. elegans embryo development. The Journal of Cell Biology, May 2020. URL: https://doi.org/10.1083/jcb.201912037, doi:10.1083/jcb.201912037. This article has 17 citations.
(pellettieri2003coordinateactivationof pages 8-9): Jason Pellettieri, Valerie Reinke, Stuart K. Kim, and Geraldine Seydoux. Coordinate activation of maternal protein degradation during the egg-to-embryo transition in c. elegans. Developmental cell, 5 3:451-62, Sep 2003. URL: https://doi.org/10.1016/s1534-5807(03)00231-4, doi:10.1016/s1534-5807(03)00231-4. This article has 171 citations and is from a highest quality peer-reviewed journal.
(pellettieri2003coordinateactivationof pages 9-10): Jason Pellettieri, Valerie Reinke, Stuart K. Kim, and Geraldine Seydoux. Coordinate activation of maternal protein degradation during the egg-to-embryo transition in c. elegans. Developmental cell, 5 3:451-62, Sep 2003. URL: https://doi.org/10.1016/s1534-5807(03)00231-4, doi:10.1016/s1534-5807(03)00231-4. This article has 171 citations and is from a highest quality peer-reviewed journal.
(stitzel2006thec.elegans pages 3-4): Michael L. Stitzel, Jason Pellettieri, and Geraldine Seydoux. The c. elegans dyrk kinase mbk-2 marks oocyte proteins for degradation in response to meiotic maturation. Current Biology, 16:56-62, Jan 2006. URL: https://doi.org/10.1016/j.cub.2005.11.063, doi:10.1016/j.cub.2005.11.063. This article has 129 citations and is from a highest quality peer-reviewed journal.
(shirayama2006theconservedkinases pages 1-2): Masaki Shirayama, Martha C. Soto, Takao Ishidate, Soyoung Kim, Kuniaki Nakamura, Yanxia Bei, Sander van den Heuvel, and Craig C. Mello. The conserved kinases cdk-1, gsk-3, kin-19, and mbk-2 promote oma-1 destruction to regulate the oocyte-to-embryo transition in c. elegans. Current Biology, 16:118, Jan 2006. URL: https://doi.org/10.1016/j.cub.2005.11.070, doi:10.1016/j.cub.2005.11.070. This article has 124 citations and is from a highest quality peer-reviewed journal.
(nishi2007studyofoocytetoembryo pages 38-42): Y Nishi. Study of oocyte-to-embryo transition regulators, oma-1 and oma-2 in c. elegans. Unknown journal, 2007.