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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
The requested target is the budding-yeast CDC14/OAF3/YFR028C product, not human CDC14A/CDC14B, fission-yeast Clp1/Flp1, or a fungal-pathogen ortholog. The supplied UniProt identity is consistent with the literature: S. cerevisiae Cdc14 is a 551-amino-acid, Cdc14-family dual-specificity protein phosphatase whose conserved N-terminal region contains substrate-recognition and PTP-like catalytic domains, while its less-conserved C-terminal tail contains localization and regulatory elements. Its catalytic core bears the PTP-family HCX₅R signature expected from the listed DSPn/PTP-like domains. Human and fission-yeast proteins are discussed below only as explicitly labeled comparisons because their biological functions are not interchangeable with those of budding-yeast Cdc14. (alonsoramos2024decodingthenucleolar pages 17-19, mocciaro2010cdc14ahighly pages 1-2, manzanolopez2020themultipleroles pages 1-3)
The primary function of Cdc14 is to reverse mitotic Cdc28/Cdk1 phosphorylation during anaphase, causing ordered inactivation of mitotic CDK signaling and exit into G1. Its activity is governed mainly by location: Cdc14 is inhibited through sequestration by Cfi1/Net1 in the nucleolus from G1 through metaphase, then released first into the nucleoplasm by the FEAR network and more broadly into the cytoplasm under MEN control. Direct targets include Cdh1/Hct1, Sic1, Swi5, spindle and kinetochore proteins, MEN regulators, replication factors, DNA-repair enzymes, and meiotic recombination factors. (alonsoramos2024decodingthenucleolar pages 17-19, manzanolopez2020themultipleroles pages 3-5, wang2004kineticandmechanistic pages 1-1)
Identity verification passed. The organism, phenotype, molecular class, size, and domain architecture reported for budding-yeast Cdc14 all match Q00684/YFR028C. The approximately 350-residue conserved N-terminal core comprises an “A” region contributing to substrate specificity and a catalytic “B” region carrying the PTP signature. The variable C terminus includes nuclear localization/export information and additional regulatory sequences. These features align with the supplied InterPro annotations CDC14_C, DSPn, dual-specificity phosphatase catalytic, PTP-like, and PTP. (alonsoramos2024decodingthenucleolar pages 17-19, mocciaro2010cdc14ahighly pages 1-2, mocciaro2010cdc14ahighly pages 2-3)
“Dual-specificity phosphatase” denotes the family’s ability to hydrolyze phosphotyrosine as well as phosphoserine/phosphothreonine substrates. It should not, however, be interpreted as equal physiological activity toward all three residues. Budding-yeast Cdc14’s biologically important substrates are predominantly phosphoserine-containing CDK sites, and phosphothreonine is a relatively poor substrate. (mocciaro2010cdc14ahighly pages 1-2, kataria2018apxlmotif pages 1-2)
Cdc14 catalyzes protein-phosphate monoester hydrolysis:
phosphoprotein + H₂O → dephosphorylated protein + inorganic phosphate.
Like other cysteine-based PTPs, it uses the catalytic cysteine of the HCX₅R loop to attack phosphorus and form a covalent cysteinyl-phosphate intermediate. Hydrolysis of that intermediate then releases orthophosphate and regenerates enzyme. Kinetic, pH-dependence, and mutational studies identified Asp253 as the general acid during intermediate formation and the general base during intermediate hydrolysis. Asp50, Asp129, Glu168, Glu171, and Asp177 also support efficient substrate dephosphorylation. (wang2004kineticandmechanistic pages 1-1)
A major 2024 advance revised the simple view of this catalytic cycle. Milholland and colleagues identified a C-terminal substrate-like catalytic enhancer (SLiCE) in the disordered tail. This intramolecular pseudosubstrate preferentially engages the phosphoenzyme state and accelerates the normally rate-limiting hydrolysis step rather than merely blocking the active site. Pro433 and Lys435 are important: P433A/K435A impairs stimulation. The adjacent Cdk-regulated Ser429 behaves as a switch—S429E reduces catalytic performance, whereas S429A does not—supporting inhibition of SLiCE function by phosphorylation when CDK activity is high. The work combines biochemical kinetics, peptide experiments, mutagenesis, and AlphaFold-supported structural modeling; stable direct tail binding was difficult to detect, so the phosphoenzyme-selective interaction remains a mechanistic model rather than a solved phosphoenzyme structure. Published August 2024: https://doi.org/10.1016/j.jbc.2024.107644. (milholland2024cdc14phosphatasesuse pages 1-2, milholland2024cdc14phosphatasesuse pages 8-10, milholland2024cdc14phosphatasesuse pages 12-13)
Cdc14 has at least two separable recognition layers:
Comparative enzyme profiling found the optimal pSPxK preference conserved across diverse Dikarya fungal Cdc14 homologs. In the tested Yen1 peptide context, adding Lys/Arg at +4 improved catalytic efficiency approximately two- to fivefold for several enzymes, whereas adding basic residues at +2 did not. These comparative results reinforce—but do not replace—direct evidence from S. cerevisiae. Published July 2020: https://doi.org/10.1038/s41598-020-68921-3. (demarco2020conservationofcdc14 pages 7-8)
From G1 through metaphase, Cdc14 is concentrated in the nucleolus, where Cfi1/Net1 binds and inhibits it as part of the RENT complex. Thus, cellular activity is controlled chiefly by sequestration and substrate access rather than by large changes in Cdc14 abundance. The protein’s localization elements permit regulated exchange among nucleolus, nucleoplasm, cytoplasm, spindle structures, and the division site. (alonsoramos2024decodingthenucleolar pages 17-19, manzanolopez2020themultipleroles pages 3-5, mocciaro2010cdc14ahighly pages 2-3)
Release occurs in two functionally distinct waves:
The spatial organization is mechanistically important: MEN signals originate at spindle-pole bodies but must reach nucleolar Cdc14. Current models place activated Dbf2–Mob1 in the nucleus/nucleolus after Cdc5-dependent priming, where it phosphorylates Cfi1/Net1 and Cdc14. This connects spindle position and cell-cycle timing to phosphatase activation across compartments. (manzanolopez2020themultipleroles pages 3-5)
A 2024 review further frames the nucleolus as a biomolecular condensate whose sequestration properties enable temporally restricted Cdc14 release. Published November 2024: https://doi.org/10.3390/ijms252312861. (alonsoramos2024decodingthenucleolar pages 17-19)
Cdc14 is essential for late-anaphase-to-G1 progression in budding yeast. Its canonical function is to oppose Cdc28/Cdk1 through a reinforcing network:
Together, cyclin destruction and CDK-inhibitor accumulation create a switch-like fall in mitotic CDK activity. Conditional loss of Cdc14 leaves Cdk1 substrates phosphorylated and cells arrested in late anaphase, establishing this pathway—not its many secondary phenotypes—as the protein’s primary biological role. (alonsoramos2024decodingthenucleolar pages 17-19, wang2004kineticandmechanistic pages 1-1, mocciaro2010cdc14ahighly pages 3-5)
The early Cdc14 pulse dephosphorylates spindle and kinetochore regulators including Ase1, Ask1, Fin1, and Sli15. These reactions stabilize/elongate the anaphase spindle, remodel kinetochores, and move the chromosomal passenger complex from centromeres to the spindle. Cdc14-dependent activation of Fin1–PP1 illustrates a phosphatase relay: Cdc14 can trigger secondary dephosphorylation by PP1 rather than acting directly on every late-mitotic site. (manzanolopez2020themultipleroles pages 3-5, mocciaro2010cdc14ahighly pages 3-5)
Cdc14 also promotes condensin-dependent compaction and segregation of the repetitive rDNA and telomeres. Its transient presence at the bud neck/division site and its control of MEN and cytoskeletal substrates connect it to cytokinesis. The most accurate current interpretation is therefore that Cdc14 is a master trigger embedded in a network with PP1 and PP2A, not the sole enzyme resetting all late-mitotic phosphorylation. (manzanolopez2020themultipleroles pages 3-5, mocciaro2010cdc14ahighly pages 2-3)
Cdc14 helps restore replication competence after mitosis. Reported replication-associated targets include Sld2, Pol12, Dbp2, and Cdc6. Cdc6 regulation is especially illustrative: phosphatases remove distinct Cdk-dependent inhibitory marks so that Cdc6 can be stabilized and replication origins relicensed only after mitotic exit; this works together with Sic1-mediated Cdk inhibition rather than through Cdc14 alone. (mocciaro2010cdc14ahighly pages 3-5)
A 2023 primary study established a more precise repair function. Following an induced double-strand break, Cdk phosphorylation activates Dna2-dependent long-range end resection. Mitotically activated Cdc14 subsequently dephosphorylates Dna2 and excludes it from the lesion, preventing excessive single-stranded-DNA production. Loss of Cdc14 produced over-resection; Dna2 inactivation or mutation of its Cdk sites bypassed the phenotype, placing Dna2 mechanistically downstream. Appropriate Cdc14 action sustained repair synthesis and the normal length, frequency, and distribution of gene-conversion tracts. The study used HO-induced breaks, sequencing-based resection profiles, phosphosite mutants, imaging, and genetic epistasis. Published May 2023: https://doi.org/10.1038/s41467-023-38417-5. (campos2023cdc14phosphatasecounteracts pages 18-19)
Cdc14 is also activated during meiosis, but its activity must be restricted because meiosis I is followed by meiosis II rather than by DNA replication. Cdc14 directly activates the Holliday-junction resolvase Yen1 by removing inhibitory CDK phosphorylation, permitting Yen1 nuclear re-entry and resolution of persistent recombination intermediates. Similar defects caused by loss of Cdc14 or Yen1 in backgrounds lacking Mus81–Mms4/Sgs1 repair routes support their action in the same backup resolution pathway. (alonsoramos2024decodingthenucleolar pages 15-17)
Recent time-resolved phosphoproteomics indicates that the meiosis-I/II transition is not a miniature mitotic exit: most CDK motifs remain phosphorylated, whereas many non-CDK sites are reset. Artificially lowering CDK can produce a more mitosis-like ordered dephosphorylation program. The emerging interpretation is that meiotic Cdc14 causes qualitatively selective rewiring, preserving enough CDK signaling to suppress relicensing while enabling chromosome segregation and recombination-intermediate resolution. This is a central conclusion of 2024 analyses, not evidence that Cdc14’s core enzymatic specificity changes in meiosis. (alonsoramos2024decodingthenucleolar pages 17-19, alonsoramos2024decodingthenucleolar pages 15-17)
The table below separates the core annotation from supporting methods, representative substrates, recent developments, and translational implications.
| Aspect | Current functional annotation | Strongest evidence/method | Representative substrates or motifs | Key recent update |
|---|---|---|---|---|
| Identity and domains | Target is Saccharomyces cerevisiae S288c Cdc14 (Q00684; CDC14/OAF3/YFR028C), a 551-aa Cdc14-family dual-specificity phosphatase. Its conserved N-terminal core contains substrate-recognition and PTP catalytic domains; the divergent C-terminal region carries localization and regulatory elements. The catalytic core contains the PTP-family HCX₅R signature. | Sequence/domain comparison, mutagenesis, structural studies, and authoritative reviews (alonsoramos2024decodingthenucleolar pages 17-19, mocciaro2010cdc14ahighly pages 1-2, manzanolopez2020themultipleroles pages 1-3) | Catalytic cysteine in HCX₅R; N-terminal A specificity domain and B catalytic domain; C-terminal nuclear-localization/export elements | A 2024 study identified a regulatory C-terminal substrate-like catalytic enhancer (SLiCE), extending the annotation beyond the canonical catalytic domains. Milholland et al., 2024-08 (milholland2024cdc14phosphatasesuse pages 1-2, milholland2024cdc14phosphatasesuse pages 8-10) |
| Catalytic reaction | Hydrolyzes phosphate monoesters on phosphorylated proteins: phosphoprotein + H₂O → dephosphorylated protein + orthophosphate. Catalysis proceeds through a covalent cysteinyl-phosphate intermediate; Asp253 acts as general acid during intermediate formation and general base during hydrolysis. | Pre-steady-state/steady-state kinetics, pH dependence, and active-site mutagenesis. Wang et al., 2004-07 (wang2004kineticandmechanistic pages 1-1) | Physiological targets are predominantly phosphoserine-containing CDK substrates; acidic active-site residues Asp50, Asp129, Glu168, Glu171, Asp177, and Asp253 support efficient catalysis | SLiCE preferentially associates with the phosphoenzyme state and accelerates normally rate-limiting intermediate hydrolysis; P433A/K435A or phosphomimetic S429E impairs this stimulation. Milholland et al., 2024-08 (milholland2024cdc14phosphatasesuse pages 1-2, milholland2024cdc14phosphatasesuse pages 8-10, milholland2024cdc14phosphatasesuse pages 12-13) |
| Substrate specificity | Although classified as dual-specificity, budding-yeast Cdc14 strongly favors pSer-Pro, especially pSer-Pro-x-Lys/Arg, and phosphothreonine is comparatively poor because of steric constraints. A separate Pro-x-Leu (PxL) docking motif improves binding and determines when substrates are dephosphorylated. | Peptide profiling, phage display, enzyme kinetics, motif transplantation/deletion, and Cdc14–peptide crystal structures. Kataria et al., 2018-11 (manzanolopez2020themultipleroles pages 3-5, kataria2018apxlmotif pages 1-2) | pSPxK/R catalytic motif; PxL docking motif; Cbk1 PxL deletion delays dephosphorylation, whereas PxL addition advances otherwise late substrate dephosphorylation | Fungal ortholog profiling confirmed an invariant optimal pSPxK motif; +4 Lys/Arg improved catalytic efficiency only about 2–5-fold in tested contexts. DeMarco et al., 2020-07 (demarco2020conservationofcdc14 pages 7-8) |
| Localization | Cdc14 is concentrated and inhibited in the nucleolus from G1 through metaphase through association with Cfi1/Net1 in the RENT complex. It is released first into the nucleoplasm and subsequently into the cytoplasm during anaphase; regulated localization, rather than major abundance changes, controls access to substrates. | Live-cell localization, genetics, interaction studies, and cell-cycle synchronization (alonsoramos2024decodingthenucleolar pages 17-19, manzanolopez2020themultipleroles pages 3-5, mocciaro2010cdc14ahighly pages 2-3) | Net1/Cfi1 nucleolar anchor; nuclear localization and export signals; late localization includes spindle-pole bodies and the division site | Current models describe the nucleolus as a regulatory condensate that enables temporally restricted sequestration and release of Cdc14. Alonso-Ramos & Carballo, 2024-11 (alonsoramos2024decodingthenucleolar pages 17-19) |
| FEAR and MEN regulation | The FEAR network triggers transient nucleoplasmic release in early anaphase; the mitotic-exit network (MEN) drives sustained, broader release in late anaphase. Polo/Cdc5 and CDK-dependent Net1 regulation, PP2A-Cdc55 inhibition, and MEN kinase signaling coordinate these waves; declining CDK and Cdc5 activity permit resequestration. | Epistasis, phosphoregulation assays, synchronized-cell imaging, and localization studies (manzanolopez2020themultipleroles pages 3-5, manzanolopez2020themultipleroles pages 1-3) | Net1/Cfi1, Esp1/separase, Cdc5, PP2A-Cdc55, Tem1–Cdc15–Dbf2/Mob1 MEN cascade | The regulatory model now includes phosphorylation of Net1 and Cdc14 by nucleolar Dbf2–Mob1 after Cdc5-dependent priming, linking a spindle-pole-generated MEN signal to nucleolar Cdc14 activation. (manzanolopez2020themultipleroles pages 3-5) |
| Primary mitotic-exit function | Cdc14 is essential for transition from late anaphase into G1 because it reverses Cdc28/Cdk1 phosphorylation. It activates APC/C–Cdh1, stabilizes and promotes expression of the CDK inhibitor Sic1 through Sic1 and Swi5 dephosphorylation, and thereby creates positive feedback that destroys mitotic cyclins and suppresses CDK activity. Loss of function causes late-anaphase arrest. | Conditional mutants, biochemical dephosphorylation, genetics, and cell-cycle phenotyping (alonsoramos2024decodingthenucleolar pages 17-19, wang2004kineticandmechanistic pages 1-1, manzanolopez2020themultipleroles pages 1-3) | Cdh1/Hct1, Sic1, Swi5, Cdc15, Bfa1, Mob1, Swe1, Acm1 and Pds1 | Recent expert synthesis retains mitotic exit as the defining essential function in budding yeast while emphasizing that this role is not conserved wholesale in human CDC14A/B. Partscht & Schiebel, 2023-07 (mocciaro2010cdc14ahighly pages 1-2) |
| Chromosomes, spindle and cytokinesis | Released Cdc14 promotes anaphase-spindle stabilization and elongation, chromosomal-passenger-complex redistribution, kinetochore remodeling, accurate rDNA/telomere condensation and segregation, MEN activation, and cytokinesis. Its cytokinetic effects involve both direct substrate reversal and activation of downstream phosphatases. | Mutant phenotyping, substrate dephosphorylation, microscopy, condensin-localization studies, and genetic interaction analysis (manzanolopez2020themultipleroles pages 3-5, mocciaro2010cdc14ahighly pages 2-3, mocciaro2010cdc14ahighly pages 3-5) | Ase1, Ask1, Fin1, Sli15, Cdc15 and Bfa1; Cdc14-dependent Fin1–PP1 activation contributes to kinetochore/CPC remodeling | Current work places Cdc14 within a broader phosphatase relay rather than as the sole late-mitotic phosphatase; ordered dephosphorylation reflects cooperation with PP1 and PP2A plus motif-dependent substrate timing. (manzanolopez2020themultipleroles pages 3-5, kataria2018apxlmotif pages 1-2) |
| DNA replication and repair | Cdc14 helps reset replication competence and limits homologous-recombination DNA-end resection. During mitotic repair it dephosphorylates Dna2, excluding this nuclease from the lesion and preventing excessive single-stranded-DNA formation, thereby supporting correctly distributed gene-conversion tracts and repair synthesis. | HO-induced double-strand-break systems, resection sequencing, phosphosite mutants, microscopy, and genetic epistasis. Campos et al., 2023-05 (campos2023cdc14phosphatasecounteracts pages 18-19) | Dna2; replication-associated substrates include Cdc6, Sld2, Pol12 and Dbp2 (mocciaro2010cdc14ahighly pages 3-5) | The 2023 Dna2 study established a direct mechanism: loss of Cdc14 yields over-resection, while Dna2 inactivation or mutation of its CDK sites bypasses that defect. Campos et al., 2023-05 (campos2023cdc14phosphatasecounteracts pages 18-19) |
| Meiosis and recombination | Meiotic Cdc14 activity is more restricted than the full mitotic-exit pulse, allowing two chromosome divisions without intervening DNA replication. It activates the Yen1 Holliday-junction resolvase by dephosphorylation, promoting nuclear re-entry and resolution of persistent recombination intermediates; it also contributes to chromosome segregation and meiotic exit. | Meiotic genetics, phosphomutants, localization, synthetic interactions with Mus81–Mms4/Sgs1 pathways, and time-resolved phosphoproteomics (alonsoramos2024decodingthenucleolar pages 15-17) | Yen1; meiotic regulatory targets also include Rim4 | A 2024 synthesis and phosphoproteomic studies show that most CDK motifs remain phosphorylated after meiosis I while many non-CDK sites are reset, indicating qualitatively selective—not globally mitosis-like—dephosphorylation. Alonso-Ramos & Carballo, 2024-11 (alonsoramos2024decodingthenucleolar pages 17-19, alonsoramos2024decodingthenucleolar pages 15-17) |
| Translational and application relevance | Cdc14 is principally a mechanistic research target and potential antifungal-enzyme target, not an established clinical or industrial intervention. Its unusually conserved fungal substrate pocket may permit selective inhibitor design, but essentiality and biological roles vary among fungal species and differ markedly from human CDC14 paralogs. | Phylogenetics, comparative enzymology, substrate profiling, and inhibitor assays across fungal orthologs. DeMarco et al., 2020-07 (demarco2020conservationofcdc14 pages 7-8) | Nonhydrolysable pCF₂Ser peptide mimetic derived from a Pds1-site sequence; fungal Cdc14 inhibition Kᵢ 3–19 µM, versus no effective PTP1B/VHR inhibition at ≤200 µM and estimated VHR Kᵢ >350 µM | Conserved fungal specificity supports exploratory broad-spectrum crop-antifungal development, while the 2024 SLiCE mechanism offers a second regulatory surface for inhibitor discovery; neither concept yet constitutes a real-world approved application. (demarco2020conservationofcdc14 pages 7-8, milholland2024cdc14phosphatasesuse pages 1-2) |
Table: Compact evidence map for budding-yeast Cdc14, integrating catalytic function, localization, cell-cycle pathways, recent mechanistic advances, and translational relevance. Human and non-budding-yeast homologs are used only for clearly identified comparative evidence.
Cdc14 currently has three practical uses:
The 2024 SLiCE discovery offers another potential regulatory surface for chemical intervention, although it remains preclinical biochemical biology rather than a validated drug-discovery program. (milholland2024cdc14phosphatasesuse pages 1-2, milholland2024cdc14phosphatasesuse pages 8-10)
Authoritative reviews agree that Cdc14 is the defining mitotic-exit phosphatase in budding yeast, but emphasize that Cdc14-family functions have diverged. Fission-yeast Clp1/Flp1 is more important for cytokinesis and mitotic timing than for the essential mitotic-exit switch. Human CDC14A and CDC14B have different localization and developmental/cellular roles, and genetic studies do not support simply assigning them the essential budding-yeast function. Consequently, results on human CDC14B, Schizosaccharomyces pombe Clp1, or pathogen homologs cannot be used as direct functional annotations for Q00684. (mocciaro2010cdc14ahighly pages 1-2, manzanolopez2020themultipleroles pages 1-3, mocciaro2010cdc14ahighly pages 3-5)
The strongest annotation confidence applies to the catalytic phosphatase function, pSPxK/R preference, nucleolar sequestration, FEAR/MEN-controlled release, and essential mitotic-exit role. Individual substrate lists require more caution: some are supported by direct biochemical dephosphorylation and motif perturbation, whereas others derive from genetics, trapping mutants, interaction studies, or phosphoproteomics. Likewise, Cdc14’s broad effects on autophagy, morphogenesis, transcription, and stress adaptation are biologically credible but are secondary to—and often downstream of—its precisely established role in reversing proline-directed phosphorylation during anaphase. (alonsoramos2024decodingthenucleolar pages 17-19, manzanolopez2020themultipleroles pages 3-5)
The most defensible concise annotation is: CDC14/YFR028C encodes an essential, nucleolus-regulated dual-specificity phosphatase that preferentially dephosphorylates pSer-Pro-X-Lys/Arg Cdk1 sites, aided by PxL substrate docking. FEAR- and MEN-dependent release during anaphase allows Cdc14 to activate APC/C–Cdh1 and Sic1/Swi5 pathways, reverse phosphorylation on spindle, chromosome, replication, and repair proteins, and thereby coordinate chromosome segregation, mitotic exit, cytokinesis, and return to G1. Recent work adds direct control of Dna2-mediated DNA-end resection in 2023 and an intramolecular, phosphoregulated SLiCE catalytic-enhancer mechanism in 2024. (alonsoramos2024decodingthenucleolar pages 17-19, kataria2018apxlmotif pages 1-2, milholland2024cdc14phosphatasesuse pages 1-2, campos2023cdc14phosphatasecounteracts pages 18-19)
References
(alonsoramos2024decodingthenucleolar pages 17-19): Paula Alonso-Ramos and Jesús A. Carballo. Decoding the nucleolar role in meiotic recombination and cell cycle control: insights into cdc14 function. International Journal of Molecular Sciences, 25:12861, Nov 2024. URL: https://doi.org/10.3390/ijms252312861, doi:10.3390/ijms252312861. This article has 2 citations.
(mocciaro2010cdc14ahighly pages 1-2): Annamaria Mocciaro and Elmar Schiebel. Cdc14: a highly conserved family of phosphatases with non-conserved functions? Journal of Cell Science, 123:2867-2876, Sep 2010. URL: https://doi.org/10.1242/jcs.074815, doi:10.1242/jcs.074815. This article has 214 citations and is from a domain leading peer-reviewed journal.
(manzanolopez2020themultipleroles pages 1-3): Javier Manzano-López and Fernando Monje-Casas. The multiple roles of the cdc14 phosphatase in cell cycle control. International Journal of Molecular Sciences, 21:709, Jan 2020. URL: https://doi.org/10.3390/ijms21030709, doi:10.3390/ijms21030709. This article has 47 citations.
(manzanolopez2020themultipleroles pages 3-5): Javier Manzano-López and Fernando Monje-Casas. The multiple roles of the cdc14 phosphatase in cell cycle control. International Journal of Molecular Sciences, 21:709, Jan 2020. URL: https://doi.org/10.3390/ijms21030709, doi:10.3390/ijms21030709. This article has 47 citations.
(wang2004kineticandmechanistic pages 1-1): Wei-Qing Wang, Joshua Bembenek, Kyle R. Gee, Hongtao Yu, Harry Charbonneau, and Zhong-Yin Zhang. Kinetic and mechanistic studies of a cell cycle protein phosphatase cdc14*. Journal of Biological Chemistry, 279:30459-30468, Jul 2004. URL: https://doi.org/10.1074/jbc.m402217200, doi:10.1074/jbc.m402217200. This article has 45 citations and is from a domain leading peer-reviewed journal.
(mocciaro2010cdc14ahighly pages 2-3): Annamaria Mocciaro and Elmar Schiebel. Cdc14: a highly conserved family of phosphatases with non-conserved functions? Journal of Cell Science, 123:2867-2876, Sep 2010. URL: https://doi.org/10.1242/jcs.074815, doi:10.1242/jcs.074815. This article has 214 citations and is from a domain leading peer-reviewed journal.
(kataria2018apxlmotif pages 1-2): Meghna Kataria, Stephane Mouilleron, Moon-Hyeong Seo, Carles Corbi-Verge, Philip M. Kim, and Frank Uhlmann. A pxl motif promotes timely cell cycle substrate dephosphorylation by the cdc14 phosphatase. Nov 2018. URL: https://doi.org/10.1038/s41594-018-0152-3, doi:10.1038/s41594-018-0152-3. This article has 41 citations and is from a highest quality peer-reviewed journal.
(milholland2024cdc14phosphatasesuse pages 1-2): Kedric L. Milholland, Benjamin T. Waddey, Kevin G. Velázquez-Marrero, Michelle V. Lihon, Emily L. Danzeisen, Noelle H. Naughton, Timothy J. Adams, Jack L. Schwartz, Xing Liu, and Mark C. Hall. Cdc14 phosphatases use an intramolecular pseudosubstrate motif to stimulate and regulate catalysis. The Journal of Biological Chemistry, Aug 2024. URL: https://doi.org/10.1016/j.jbc.2024.107644, doi:10.1016/j.jbc.2024.107644. This article has 1 citations.
(milholland2024cdc14phosphatasesuse pages 8-10): Kedric L. Milholland, Benjamin T. Waddey, Kevin G. Velázquez-Marrero, Michelle V. Lihon, Emily L. Danzeisen, Noelle H. Naughton, Timothy J. Adams, Jack L. Schwartz, Xing Liu, and Mark C. Hall. Cdc14 phosphatases use an intramolecular pseudosubstrate motif to stimulate and regulate catalysis. The Journal of Biological Chemistry, Aug 2024. URL: https://doi.org/10.1016/j.jbc.2024.107644, doi:10.1016/j.jbc.2024.107644. This article has 1 citations.
(milholland2024cdc14phosphatasesuse pages 12-13): Kedric L. Milholland, Benjamin T. Waddey, Kevin G. Velázquez-Marrero, Michelle V. Lihon, Emily L. Danzeisen, Noelle H. Naughton, Timothy J. Adams, Jack L. Schwartz, Xing Liu, and Mark C. Hall. Cdc14 phosphatases use an intramolecular pseudosubstrate motif to stimulate and regulate catalysis. The Journal of Biological Chemistry, Aug 2024. URL: https://doi.org/10.1016/j.jbc.2024.107644, doi:10.1016/j.jbc.2024.107644. This article has 1 citations.
(demarco2020conservationofcdc14 pages 7-8): Andrew G. DeMarco, Kedric L. Milholland, Amanda L. Pendleton, John J. Whitney, Peipei Zhu, Daniel T. Wesenberg, Monessha Nambiar, Antonella Pepe, Stefan Paula, Jean Chmielewski, Jennifer H. Wisecaver, W. Andy Tao, and Mark C. Hall. Conservation of cdc14 phosphatase specificity in plant fungal pathogens: implications for antifungal development. Scientific Reports, Jul 2020. URL: https://doi.org/10.1038/s41598-020-68921-3, doi:10.1038/s41598-020-68921-3. This article has 14 citations and is from a peer-reviewed journal.
(mocciaro2010cdc14ahighly pages 3-5): Annamaria Mocciaro and Elmar Schiebel. Cdc14: a highly conserved family of phosphatases with non-conserved functions? Journal of Cell Science, 123:2867-2876, Sep 2010. URL: https://doi.org/10.1242/jcs.074815, doi:10.1242/jcs.074815. This article has 214 citations and is from a domain leading peer-reviewed journal.
(campos2023cdc14phosphatasecounteracts pages 18-19): Adrián Campos, Facundo Ramos, Lydia Iglesias, Celia Delgado, Eva Merino, Antonio Esperilla-Muñoz, Jaime Correa-Bordes, and Andrés Clemente-Blanco. Cdc14 phosphatase counteracts cdk-dependent dna2 phosphorylation to inhibit resection during recombinational dna repair. Nature Communications, May 2023. URL: https://doi.org/10.1038/s41467-023-38417-5, doi:10.1038/s41467-023-38417-5. This article has 8 citations and is from a highest quality peer-reviewed journal.
(alonsoramos2024decodingthenucleolar pages 15-17): Paula Alonso-Ramos and Jesús A. Carballo. Decoding the nucleolar role in meiotic recombination and cell cycle control: insights into cdc14 function. International Journal of Molecular Sciences, 25:12861, Nov 2024. URL: https://doi.org/10.3390/ijms252312861, doi:10.3390/ijms252312861. This article has 2 citations.