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The UniProt accession P30305 corresponds to human CDC25B (“M-phase inducer phosphatase 2”; dual-specificity phosphatase; EC 3.1.3.48). Evidence reviewed here consistently refers to CDC25B/Cdc25B as a CDC25-family dual-specificity phosphatase (DSP) that activates cyclin-dependent kinases by removing inhibitory phosphates, with a conserved HCX5R active-site motif and catalytic Cys473 (abdelwahab2022acomprehensiveoverview pages 1-2, abdelwahab2022acomprehensiveoverview pages 2-4, davidson2023investigationofpin1 pages 30-34).
| Topic | Key Details & Evidence |
|---|---|
| Identity & Domains | Name: CDC25B (M-phase inducer phosphatase 2); Family: MPI phosphatase / Dual Specificity Phosphatase (DSP). Structure: Conserved C-terminal catalytic domain with HCX5R motif (HCEFSSER); divergent N-terminal regulatory domain. Active Site: Shallow/flat pocket lacking a defined substrate groove; specificity relies on distal "hotspot" residues (e.g., R488, R492, Y497) 20–30 Å away (davidson2023investigationofpin1a pages 30-34, abdelwahab2022acomprehensiveoverview pages 1-2, davidson2023investigationofpin1 pages 30-34, davidson2023investigationofpin1a pages 34-37). |
| Enzymatic Reaction | Function: Removes inhibitory phosphates from Thr14 and Tyr15 of Cyclin-Dependent Kinases (CDKs). Substrate Specificity: Primary substrate is CDK1/Cyclin B; can also act on CDK2/Cyclin A/E. (davidson2023investigationofpin1a pages 30-34, abdelwahab2022acomprehensiveoverview pages 2-4, liu2020theroleof pages 2-3). |
| Catalytic Mechanism | Two-step Mechanism: 1. Nucleophilic attack by thiolate of Cys473 forms a covalent phospho-cysteine intermediate. 2. Hydrolysis of the intermediate by water, assisted by a catalytic aspartate. Key Residues: Cys473 (catalytic nucleophile), Arg479 (phosphate coordination). (abdelwahab2022acomprehensiveoverview pages 1-2, abdelwahab2022acomprehensiveoverview pages 2-4, davidson2023investigationofpin1 pages 30-34, zhang2018dualspecificityphosphatasecdc25b pages 1-2). |
| Cell Cycle Role | "Starter" Phosphatase: Initiates mitosis by activating CDK1/Cyclin B at the centrosome during the G2/M transition. Timing: Accumulates in late S/early G2; activity peaks at G2/M. (davidson2023investigationofpin1a pages 30-34, abdelwahab2022acomprehensiveoverview pages 1-2, canovas2024survivinmediatesmitotic pages 28-31, contourgalcera2007whatsnewon pages 1-2). |
| Regulation | Positive Feedback: CDK1/Cyclin B phosphorylates CDC25B to enhance activity. 14-3-3 Binding: Phosphorylated CDC25B (e.g., Ser323/Ser151) is bound by 14-3-3, sequestering it in the cytoplasm during interphase; release allows nuclear entry. Redox Switch: Highly sensitive to oxidation; forms a reversible intramolecular disulfide bond between catalytic Cys473 and "backdoor" Cys426, inactivating the enzyme (reversible by thioredoxin). (abdelwahab2022acomprehensiveoverview pages 2-4, davidson2023investigationofpin1a pages 34-37, he2023ser149isanother pages 1-6). |
| Localization | Shuttling: Shuttles between nucleus and cytoplasm. G2/M: Translocates to the cytoplasm/centrosome in late G2 to activate initial CDK1 pools; Survivin may bridge CDC25B-CDK1 interaction at centrosomes. (davidson2023investigationofpin1a pages 30-34, canovas2024survivinmediatesmitotic pages 28-31, contourgalcera2007whatsnewon pages 1-2). |
| Disease Relevance | Overexpression: Found in 78% of gastric cancers, 47% of gliomas, 57% of breast cancers, 43–67% of colorectal cancers. Correlates with poor prognosis. Neurodevelopment: Regulates neurogenic decisions/progenitor cell cycle length. (abdelwahab2022acomprehensiveoverview pages 2-4, contourgalcera2007whatsnewon pages 1-2, bona2020menadionereducescdc25b pages 6-8). |
| Therapeutic Targeting | Menadione (Vitamin K3): Inhibits CDC25B (Ki ~95 µM); reduces tumor growth in gastric cancer (in vivo). HB-21: Natural product; covalently binds Cys473 (IC50 = 24.25 µM). Other Inhibitors: IRC-083864 (low nM activity); NSC-95397 (IC50 ~10-18 µM in colon cancer); Adociaquinone B (IC50 ~0.07 µM). Challenges: Quinones often generate ROS or lack specificity; shallow active site makes rational design difficult. (zhang2018dualspecificityphosphatasecdc25b pages 1-2, abdelwahab2022acomprehensiveoverview pages 2-4, dakilah2024potentialofcdc25 pages 8-9, abdelwahab2022acomprehensiveoverview pages 8-10, bona2020menadionereducescdc25b pages 6-8). |
Table: This table consolidates key findings regarding CDC25B's molecular identity, enzymatic mechanism, regulatory pathways, and role in disease, serving as a structured reference for the report.
CDC25 phosphatases are “dual-specificity” in that they can dephosphorylate phosphoserine/threonine and phosphotyrosine residues; functionally their defining substrates are CDKs at the inhibitory sites Thr14 and Tyr15 (abdelwahab2022acomprehensiveoverview pages 1-2, liu2020theroleof pages 2-3). CDC25B is widely described as promoting the G2/M transition by activating CDK1–cyclin B through dephosphorylation of these inhibitory phosphosites (davidson2023investigationofpin1a pages 30-34, abdelwahab2022acomprehensiveoverview pages 2-4, liu2020theroleof pages 2-3).
Mechanistic and structural descriptions converge on a cysteine-based phosphatase mechanism analogous to classical protein tyrosine phosphatases (PTPs):
- The conserved HCX5R motif forms the catalytic loop, and the catalytic cysteine exists as a reactive thiolate that performs nucleophilic attack on the substrate phosphate (abdelwahab2022acomprehensiveoverview pages 1-2, davidson2023investigationofpin1 pages 30-34).
- Catalysis proceeds via a covalent phospho-cysteine intermediate, followed by hydrolysis to regenerate the enzyme (abdelwahab2022acomprehensiveoverview pages 1-2, abdelwahab2022acomprehensiveoverview pages 2-4, davidson2023investigationofpin1 pages 30-34).
For human CDC25B specifically, Cys473 is repeatedly identified as the catalytically essential cysteine (abdelwahab2022acomprehensiveoverview pages 1-2, abdelwahab2022acomprehensiveoverview pages 2-4, zhang2018dualspecificityphosphatasecdc25b pages 1-2).
CDC25 catalytic pockets are described as flat/shallow and lacking a strong, peptide-like binding groove; therefore substrate specificity depends on features beyond the immediate catalytic pocket (davidson2023investigationofpin1a pages 30-34, davidson2023investigationofpin1 pages 30-34, liu2020theroleof pages 2-3). For CDC25B, distal hotspot residues (e.g., R488, R492, Y497) located ~20–30 Å from the active site have been described as contributing to recognition (davidson2023investigationofpin1a pages 30-34, davidson2023investigationofpin1 pages 30-34).
A central, conserved functional statement is that CDC25B activates CDKs by removing inhibitory phosphates at Thr14 and Tyr15, thereby promoting mitotic entry via CDK1–cyclin B activation (davidson2023investigationofpin1a pages 30-34, abdelwahab2022acomprehensiveoverview pages 2-4, liu2020theroleof pages 2-3). Structural/docking discussions in the inhibitor literature describe interactions consistent with recognition of phosphorylated CDK activation-loop residues, including contacts of the phosphate with arginine in the CX5R motif (abdelwahab2022acomprehensiveoverview pages 2-4).
CDC25B is frequently described as acting as a “starter” phosphatase that initiates activation of CDK1–cyclin B at the centrosome, helping trigger the G2/M transition (abdelwahab2022acomprehensiveoverview pages 1-2, contourgalcera2007whatsnewon pages 1-2). A recent mechanistic preprint (HeLa cells) further frames CDC25B as the phosphatase “first” activating centrosomal Cdk1, with survivin proposed to enable proper signaling through a CDC25B–Cdk1 axis (canovas2024survivinmediatesmitotic pages 28-31).
CDC25-family phosphatases are extensively regulated by phosphorylation and binding partners, including 14-3-3 proteins that sequester phosphatases and influence localization (davidson2023investigationofpin1a pages 34-37, contourgalcera2007whatsnewon pages 1-2). A 2023 preprint in mouse embryos identifies a phosphorylation site (Ser149 in mouse; corresponding to Ser151 in human) as a potential 14-3-3ε binding site affecting cytoplasmic localization and G2/M control; the work also cites prior human-cell findings where 14-3-3 binding to phosphorylated CDC25B sites drives cytoplasmic localization (he2023ser149isanother pages 1-6). Although this is not a human-only study, it is informative because the residue mapping explicitly links to human numbering and summarizes human-cell literature (he2023ser149isanother pages 1-6).
A 2024 Research Square preprint reports that survivin depletion reduces centrosomal Cdk1 level and activity and leads to accumulation of inactive (pT14/pY15) Cdk1; survivin is proposed to facilitate signaling via the Cdc25B–Cdk1 axis at centrosomes (canovas2024survivinmediatesmitotic pages 28-31). Quantitatively, survivin loss reduced the fraction of cells showing a split centrosomal Cdk1 signal by >2-fold (38% vs 15%) (canovas2024survivinmediatesmitotic pages 28-31).
CDC25B is unusually sensitive to oxidation at its catalytic cysteine, and multiple biochemical/structural sources support a reversible redox-control mechanism:
- Oxidation of the active-site cysteine by H2O2 is described with a measured second-order rate constant (164 ± 14 M−1 s−1, 20°C, pH 7.0) for Cdc25B (rudolph2005redoxregulationof pages 1-2).
- Structural studies show formation of an intramolecular disulfide between Cys473 (active site) and a “backdoor” cysteine Cys426, accompanied by a P-loop rearrangement that occludes the active site and prevents substrate binding (buhrman2005structuralmechanismof pages 7-8, buhrman2005structuralmechanismof pages 6-7, buhrman2005structuralmechanismof pages 4-6).
- The disulfide form is reported to be rapidly reduced by thioredoxin but not by glutathione, consistent with structural sequestration of the bond and selective cellular reactivation (buhrman2005structuralmechanismof pages 7-8, rudolph2005redoxregulationof pages 1-2).
A 2024 review in Frontiers in Pharmacology positions CDC25 phosphatases (including CDC25B) as proto-oncogenic cell-cycle drivers and discusses inhibitor strategies and precision-medicine framing, emphasizing that rational active-site inhibitor design is challenged by CDC25’s shallow active site and that alternative strategies (interface hotspots, allostery, etc.) may be needed (published Jan 2024; https://doi.org/10.3389/fphar.2024.1324001) (dakilah2024potentialofcdc25 pages 8-9, dakilah2024potentialofcdc25 pages 9-10, dakilah2024potentialofcdc25 pages 10-11).
The 2024 HeLa-cell preprint expands on a centrosomal model in which survivin influences the CDC25B–Cdk1 activation axis, providing quantitative imaging readouts and biochemical evidence of altered Cdk1 activation status upon survivin depletion (published Feb 2024; https://doi.org/10.21203/rs.3.rs-3949429/v1) (canovas2024survivinmediatesmitotic pages 28-31).
A 2023 bioRxiv preprint identifies an additional potential 14-3-3ε binding site affecting CDC25B localization and MPF activation dynamics, mapping mouse residues to human (Ser149 mouse ↔ Ser151 human) and citing human-cell literature for 14-3-3-driven cytoplasmic localization (published Aug 2023; https://doi.org/10.1101/2023.08.15.553381) (he2023ser149isanother pages 1-6).
A comprehensive inhibitor review reports high frequencies of CDC25B overexpression across tumor types, including gastric cancer (78%), breast cancer (57%), gliomas (47%), and colorectal cancer (43–67%), among others (abdelwahab2022acomprehensiveoverview pages 2-4). Such prevalence underpins clinical/translational interest in CDC25B as a biomarker and target in oncology (abdelwahab2022acomprehensiveoverview pages 2-4, dakilah2024potentialofcdc25 pages 9-10).
Covalent active-site targeting:
- The natural product HB-21 irreversibly inhibits recombinant human CDC25B with IC50 = 24.25 μM by covalently binding the catalytic Cys473 (Frontiers in Chemistry, Nov 2018; https://doi.org/10.3389/fchem.2018.00531) (zhang2018dualspecificityphosphatasecdc25b pages 1-2). Structural docking figures show HB-21 positioned in the binding cavity with CYS-473 labeled, supporting the proposed mechanism (zhang2018dualspecificityphosphatasecdc25b media 792a4956, zhang2018dualspecificityphosphatasecdc25b media f30089ca).
Quinones and related scaffolds / broader inhibitor landscape:
- A 2022 review compiles many CDC25 inhibitors with potencies spanning submicromolar to micromolar ranges, including adociaquinone B (IC50 ~0.07 μM against CDC25B catalytic domain) and multiple NSC-series compounds with submicromolar activity (Molecules, Apr 2022; https://doi.org/10.3390/molecules27082389) (abdelwahab2022acomprehensiveoverview pages 8-10).
- Menadione (vitamin K3) is discussed as a CDC25-family inhibitor with Ki ~95 ± 3 μM against CDC25B in compiled biochemical data (abdelwahab2022acomprehensiveoverview pages 2-4).
A 2020 study in Therapeutic Advances in Gastroenterology reports that menadione reduces CDC25B mRNA/protein in gastric cancer cell lines and induces a G2/M arrest signature with increased p-CDK1 and cyclin B1 consistent with an inactive cyclin B–CDK1 complex; in a primate carcinogenesis model, CDC25B mRNA/protein were reported to be ~40% lower in menadione-treated animals by day 960, and in certain prevention groups no tumors developed (published Jan 2020; https://doi.org/10.1177/1756284819895435) (bona2020menadionereducescdc25b pages 6-8).
References
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(buhrman2005structuralmechanismof pages 6-7): Greg Buhrman, Benjamin Parker, Jungsan Sohn, Johannes Rudolph, and Carla Mattos. Structural mechanism of oxidative regulation of the phosphatase cdc25b via an intramolecular disulfide bond. Biochemistry, 44 14:5307-16, Mar 2005. URL: https://doi.org/10.1021/bi047449f, doi:10.1021/bi047449f. This article has 131 citations and is from a peer-reviewed journal.
(buhrman2005structuralmechanismof pages 4-6): Greg Buhrman, Benjamin Parker, Jungsan Sohn, Johannes Rudolph, and Carla Mattos. Structural mechanism of oxidative regulation of the phosphatase cdc25b via an intramolecular disulfide bond. Biochemistry, 44 14:5307-16, Mar 2005. URL: https://doi.org/10.1021/bi047449f, doi:10.1021/bi047449f. This article has 131 citations and is from a peer-reviewed journal.
(dakilah2024potentialofcdc25 pages 9-10): Ibraheem Dakilah, Amani Harb, Eman Abu-Gharbieh, Waseem El-Huneidi, Jalal Taneera, Rifat Hamoudi, Mohammed H. Semreen, and Yasser Bustanji. Potential of cdc25 phosphatases in cancer research and treatment: key to precision medicine. Frontiers in Pharmacology, Jan 2024. URL: https://doi.org/10.3389/fphar.2024.1324001, doi:10.3389/fphar.2024.1324001. This article has 22 citations.
(dakilah2024potentialofcdc25 pages 10-11): Ibraheem Dakilah, Amani Harb, Eman Abu-Gharbieh, Waseem El-Huneidi, Jalal Taneera, Rifat Hamoudi, Mohammed H. Semreen, and Yasser Bustanji. Potential of cdc25 phosphatases in cancer research and treatment: key to precision medicine. Frontiers in Pharmacology, Jan 2024. URL: https://doi.org/10.3389/fphar.2024.1324001, doi:10.3389/fphar.2024.1324001. This article has 22 citations.
(zhang2018dualspecificityphosphatasecdc25b media 792a4956): Shoude Zhang, Qiangqiang Jia, Qiang Gao, Xueru Fan, Yuxin Weng, and Zhanhai Su. Dual-specificity phosphatase cdc25b was inhibited by natural product hb-21 through covalently binding to the active site. Frontiers in Chemistry, Nov 2018. URL: https://doi.org/10.3389/fchem.2018.00531, doi:10.3389/fchem.2018.00531. This article has 12 citations.
(zhang2018dualspecificityphosphatasecdc25b media f30089ca): Shoude Zhang, Qiangqiang Jia, Qiang Gao, Xueru Fan, Yuxin Weng, and Zhanhai Su. Dual-specificity phosphatase cdc25b was inhibited by natural product hb-21 through covalently binding to the active site. Frontiers in Chemistry, Nov 2018. URL: https://doi.org/10.3389/fchem.2018.00531, doi:10.3389/fchem.2018.00531. This article has 12 citations.
(abdelwahab2022acomprehensiveoverview pages 18-20): Ahmed Bakr Abdelwahab, Eslam Reda El-Sawy, Atef G. Hanna, Denyse Bagrel, and Gilbert Kirsch. A comprehensive overview of the developments of cdc25 phosphatase inhibitors. Molecules, 27:2389, Apr 2022. URL: https://doi.org/10.3390/molecules27082389, doi:10.3390/molecules27082389. This article has 13 citations.
(buhrman2005structuralmechanismof pages 1-2): Greg Buhrman, Benjamin Parker, Jungsan Sohn, Johannes Rudolph, and Carla Mattos. Structural mechanism of oxidative regulation of the phosphatase cdc25b via an intramolecular disulfide bond. Biochemistry, 44 14:5307-16, Mar 2005. URL: https://doi.org/10.1021/bi047449f, doi:10.1021/bi047449f. This article has 131 citations and is from a peer-reviewed journal.
(rudolph2005redoxregulationof pages 2-3): Johannes Rudolph. Redox regulation of the cdc25 phosphatases. Antioxidants & redox signaling, 7 5-6:761-7, May 2005. URL: https://doi.org/10.1089/ars.2005.7.761, doi:10.1089/ars.2005.7.761. This article has 77 citations and is from a domain leading peer-reviewed journal.