Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
Automatic Gene Ontology annotation based on Rhea mapping
Combined Automated Annotation using Multiple IEA Methods
Coordinate activation of maternal protein degradation during the egg-to-embryo transition in C. elegans.
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MBK-2 coordinates degradation of maternal proteins including MEI-1 and germ plasm components
"the C. elegans DYRK family kinase MBK-2 coordinates the degradation of several maternal proteins"
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MBK-2 is required for spindle positioning and cytokinesis in early embryos
"is essential for zygotes to complete cytokinesis and pattern the first embryonic axis"
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MBK-2 localizes to cytoplasm, cortex, centrosomes, chromosomes, and P granules
"MBK-2 distribution changes dramatically after fertilization during the meiotic divisions"
DYRK2 and GSK-3 phosphorylate and promote the timely degradation of OMA-1, a key regulator of the oocyte-to-embryo transition in C. elegans.
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MBK-2 phosphorylates OMA-1 at T239 to promote its degradation
"OMA-1 protein is directly phosphorylated at T239 by the DYRK kinase MBK-2"
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Phosphorylation at T239 is required for OMA-1 function and degradation timing
"phosphorylation at T239 is required both for OMA-1 function in the 1-cell embryo and its degradation after the first mitosis"
The C. elegans DYRK Kinase MBK-2 Marks Oocyte Proteins for Degradation in Response to Meiotic Maturation.
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MBK-2 directly phosphorylates MEI-1 and OMA-1 in vitro
"we demonstrate that MBK-2 directly phosphorylates MEI-1 and OMA-1 in vitro and that this activity is essential for degradation in vivo"
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MBK-2 relocalization from cortex to cytoplasm during meiotic divisions
"A GFP:MBK-2 fusion relocalizes from the cortex to the cytoplasm during the meiotic divisions"
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Phosphorylation of MEI-1 by MBK-2 is essential for degradation in vivo
"this activity is essential for degradation in vivo"
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.
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MBK-2 (with CDK-1, GSK-3, KIN-19) promotes OMA-1 destruction
"Mutations in four conserved protein kinase genes-mbk-2/Dyrk, kin-19/CK1alpha, gsk-3, and cdk-1/CDC2-cause stabilization of OMA-1 protein"
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MBK-2 regulates the oocyte-to-embryo transition via protein degradation
"destruction of OMA-1 is needed during the first cell division for the initiation of ZIF-1-dependent proteolysis of cell-fate determinants"
Regulation of MBK-2/Dyrk kinase by dynamic cortical anchoring during the oocyte-to-zygote transition.
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MBK-2 is tethered at cortex by EGG-3 before meiotic divisions
"Prior to the meiotic divisions, MBK-2 is tethered at the cortex by EGG-3, an oocyte protein required for egg activation"
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EGG-3 internalization releases MBK-2 for substrate phosphorylation
"EGG-3 internalization and degradation correlate with MBK-2 release from the cortex and MEI-1 phosphorylation in the cytoplasm"
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Cell cycle-regulated release of MBK-2 ensures proper timing of MEI-1 phosphorylation
"precise timing of MEI-1 phosphorylation depends on the cell cycle-regulated release of MBK-2 from the cortex"
Polo kinases regulate C. elegans embryonic polarity via binding to DYRK2-primed MEX-5 and MEX-6.
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MBK-2 primes MEX-5 at T186 for polo kinase-dependent phosphorylation
"We also show that MBK-2, a developmentally regulated DYRK2 kinase activated at meiosis II, primes T(186) for subsequent polo kinase-dependent phosphorylation"
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MBK-2 regulates asymmetric PLK-1 localization at 2-cell stage
"These polo kinases are asymmetrically localized along the anteroposterior axis of newly fertilized C. elegans embryos"
EGG-4 and EGG-5 Link Events of the Oocyte-to-Embryo Transition with Meiotic Progression in C. elegans.
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MBK-2 interacts with EGG-4 and EGG-5 pseudophosphatases
"EGG-4 and EGG-5 assemble at the oocyte cortex with the previously identified regulators or effectors of the oocyte-to-embryo transition EGG-3, CHS-1, and MBK-2"
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MBK-2 is part of cortical complex with EGG-3, CHS-1, EGG-4, EGG-5
"All of these molecules share a complex interdependence with regards to their dynamics and subcellular localization"
Regulation of MBK-2/DYRK by CDK-1 and the pseudophosphatases EGG-4 and EGG-5 during the oocyte-to-embryo transition.
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MBK-2 is activated by CDK-1 phosphorylation at S68
"MBK-2 is activated during oocyte maturation by CDK-1-dependent phosphorylation of serine 68"
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EGG-4 and EGG-5 sequester MBK-2 by binding to its YTY motif
"The pseudotyrosine phosphatases EGG-4 and EGG-5 sequester activated MBK-2 until the meiotic divisions by binding to the YTY motif"
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MBK-2 autophosphorylates at Y621
"DYRKs are kinases that self-activate in vitro by autophosphorylation of a YTY motif in the kinase domain"
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MBK-2 is part of complex with EGG-3, EGG-4, EGG-5
"EGG-4 and EGG-5 sequester activated MBK-2 until the meiotic divisions"
Eggshell chitin and chitin-interacting proteins prevent polyspermy in C. elegans.
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MBK-2 cortical distribution is affected by loss of CBD-1 or EGG-1/2
"Loss of CBD-1 or EGG-1/2 disrupts oocyte cortical distribution of CHS-1, as well as MBK-2 and EGG-3"
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MBK-2 is part of CHS-1/MBK-2/EGG-3 cortical complex
"aberrantly clustered CHS-1/MBK-2/EGG-3 may fail to support construction of a continuous eggshell"
Regulation of RNA granule dynamics by phosphorylation of serine-rich, intrinsically disordered proteins in C. elegans.
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MEG-1 and MEG-3 are substrates of MBK-2/DYRK kinase
"We demonstrate that MEG-1 and MEG-3 are substrates of the kinase MBK-2/DYRK and the phosphatase PP2A"
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MBK-2 phosphorylation of MEGs promotes P granule disassembly
"Phosphorylation of the MEGs promotes granule disassembly and dephosphorylation promotes granule assembly"
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mbk-2 RNAi causes P granules to persist in anterior cytoplasm
"P granules in C. elegans embryos"
Phosphorylation of the microtubule-severing AAA+ enzyme Katanin regulates C. elegans embryo development.
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MBK-2 phosphorylates MEI-1 at S92, S90, S113, S137
"This analysis showed that MBK-2 phosphorylates MEI-1 at S92, consistent with a previous report (Stitzel et al., 2006), but also at S90, S113, and S137"
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S92 phosphorylation is necessary and sufficient for MEI-1 degradation
"phosphorylation of MEI-1 by MBK-2 at a single serine (S92) is both necessary and sufficient to target MEI-1 for degradation after meiosis"
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MBK-2-mediated phosphorylation inhibits katanin MT-stimulated ATPase activity
"MBK-2, by phosphorylating the catalytic MEI-1 Katanin subunit, inhibits Katanin ATPase activity stimulated by MTs"
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MBK-2 localizes to centrosomes and chromosomes during mitosis
"Katanin is readily expressed during embryogenesis, where it is actively recruited to the centrosomes and chromosomes during mitosis"
The oocyte-to-embryo transition.
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The oocyte-to-embryo transition is coordinated primarily through the MBK-2 kinase, whose activation is tied to completion of meiosis.
"which are coordinated primarily through the MBK-2 kinase, whose activation is intimately tied to completion of meiosis"
Emerging role of DYRK family protein kinases as regulators of protein stability in cell cycle control.
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MBK-2, the C. elegans DYRK2 ortholog, triggers proteasomal destruction of oocyte proteins after meiosis to permit embryonic mitotic divisions, exemplifying the DYRK family role in regulating protein stability.
"The DYRK2 ortholog of C. elegans, MBK-2, triggers the proteasomal destruction of oocyte proteins after meiosis to allow the mitotic divisions in embryo development."
Falcon deep research report on mbk-2 (C. elegans)
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MBK-2 is a maternally supplied DYRK-family dual-specificity kinase activated during the oocyte-to-embryo transition; it phosphorylates maternal regulators to switch their function and mark them for ubiquitin-proteasome-dependent degradation, with best-supported direct substrates OMA-1 (T239) and katanin MEI-1 (S92).
"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)."
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MBK-2 kinase activity is essential for embryonic viability: kinase-dead MBK-2 fails to rescue mbk-2 maternal mutants.
"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)"
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MBK-2 phosphorylates OMA-1 at T239, priming subsequent GSK-3 phosphorylation at T339 and promoting timely OMA-1 degradation after the first mitosis.
"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"
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MBK-2 phosphorylates the katanin complex on multiple N-terminal regulatory sites of MEI-1 and MEI-2; S92 is the dominant site for MEL-26/CUL-3-dependent degradation targeting, while N-terminal phosphorylation abolishes microtubule-stimulated katanin ATPase activity.
"S92 is the principal site for degradation targeting, while phosphorylation of N-terminal sites suppresses MT-stimulated ATPase activity"
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MBK-2 acts as a temporal activator that confers degradation competence to specific maternal substrates after meiotic progression, rather than triggering global proteolysis.
"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"
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MBK-2 activation is gated by meiotic cell-cycle events: co-translational YTY autophosphorylation, restraint by EGG-4/EGG-5 pseudophosphatases and cortical EGG-3, CDK-1 phosphorylation of S68, and APC/C-dependent degradation of EGG proteins that releases active MBK-2 into the cytoplasm.
"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"
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MBK-2 relocalizes in a two-step, meiosis-driven manner from the uniform cortex to cortical puncta and then into the cytoplasm; progression through meiosis rather than fertilization is the trigger.
"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"