Affinage

CAB39

Calcium-binding protein 39 · UniProt Q9Y376

Length
341 aa
Mass
39.9 kDa
Annotated
2026-04-28
53 papers in source corpus 20 papers cited in narrative 20 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

CAB39 (MO25) is an armadillo-repeat scaffold protein that allosterically activates two major kinase systems: the LKB1–STRADα tumor-suppressor complex and multiple STE20/GCK-family kinases (SPAK, OSR1, MST3, MST4, STK25). In the LKB1 pathway, CAB39 stabilizes the heterotrimeric LKB1–STRADα–MO25 complex by engaging the STRADα C-terminal WEF motif and directly contacting the LKB1 activation loop, thereby activating LKB1 in a phosphorylation-independent manner to drive downstream AMPK signaling, energy sensing, polarity, and autophagy (PMID:14511394, PMID:19892943, PMID:14730349). CAB39 independently binds and potently activates SPAK/OSR1 (~100-fold) and MST3/MST4/STK25 (3–4-fold) by rotating the αC helix of these kinases into an active conformation; through SPAK/OSR1, CAB39 is required for apical membrane targeting of SPAK and consequent phosphorylation of the ion co-transporters NKCC1 and NCC, and loss of CAB39 in mouse distal convoluted tubule abolishes NCC phosphorylation, producing a Gitelman-like salt-wasting phenotype (PMID:21423148, PMID:23434407, PMID:24746913, PMID:38258567). CAB39 expression is post-transcriptionally regulated by miR-451 and miR-195, linking its abundance to AMPK pathway output in cardiac and glioma contexts (PMID:22179124, PMID:22844503).

Mechanistic history

Synthesis pass · year-by-year structured walk · 8 steps
  1. 2003 High

    Identification of CAB39 (MO25) as an obligate component of the LKB1–STRAD complex that constitutes the long-sought AMPK kinase (AMPKK) established that LKB1 kinase activity toward AMPK requires both STRAD and MO25 cofactors.

    Evidence Biochemical purification from rat liver, reconstitution with recombinant proteins, kinase assays, and genetic rescue in LKB1-null cells

    PMID:14511394

    Open questions at the time
    • How MO25 contacts LKB1 and STRAD at the structural level was unknown
    • Whether MO25 has activating roles independent of LKB1 was not addressed
  2. 2004 High

    Structural and mutagenesis studies revealed that MO25α is an armadillo-repeat protein with two distinct binding surfaces: one engages the STRAD C-terminal WEF motif via a hydrophobic pocket and the other faces LKB1, and MO25 binding dramatically increases STRADα–LKB1 affinity without requiring LKB1 T-loop phosphorylation, establishing MO25 as an allosteric activator.

    Evidence X-ray crystallography of MO25α–STRADα peptide complex, site-directed mutagenesis, in vitro kinase and binding assays

    PMID:14730349 PMID:15561763

    Open questions at the time
    • Full heterotrimeric structure was not yet resolved
    • How MO25 engages the LKB1 activation loop remained speculative
  3. 2009 High

    The crystal structure of the complete LKB1–STRADα–MO25α heterotrimer showed that STRADα acts as a pseudosubstrate locked in an active-kinase-like conformation and that MO25α directly contacts the LKB1 activation loop, providing the structural basis for phosphorylation-independent allosteric activation of LKB1.

    Evidence X-ray crystallography of the full heterotrimer with mutagenesis and kinase assays

    PMID:19892943

    Open questions at the time
    • Regulation of the complex by metabolites or post-translational modifications of MO25 itself was not resolved
    • In vivo tissue-specific requirements of MO25 were not tested
  4. 2009 High

    Discovery that MO25 directly binds and relocates the STE20 kinase MST4 from the Golgi to the subapical membrane — where MST4 phosphorylates Ezrin to initiate brush border formation — revealed the first LKB1-independent function of MO25 as an activator of GCK-family kinases in epithelial polarity.

    Evidence Co-immunoprecipitation, live-cell imaging, kinase assays, MST4 loss-of-function in polarizing epithelial cells

    PMID:19386264

    Open questions at the time
    • Whether MO25 activates MST4 catalytically or only controls its localization was ambiguous
    • Generality to other GCK kinases was not established
  5. 2011 High

    MO25 was shown to directly and potently activate SPAK/OSR1 (~100-fold) and MST3/MST4/YSK1 (3–4-fold), with SPAK/OSR1 activation driving phosphorylation of ion co-transporters NKCC1/NKCC2/NCC; siRNA knockdown of MO25 reduced endogenous NKCC1 phosphorylation, establishing MO25 as a master activator of multiple STE20 kinases beyond LKB1.

    Evidence In vitro kinase assays with recombinant proteins, siRNA knockdown and rescue, mass spectrometry phosphosite mapping

    PMID:21423148

    Open questions at the time
    • How MO25 structurally engages SPAK/OSR1 versus STRAD was not resolved
    • In vivo physiological significance for renal ion transport was not tested
  6. 2013 High

    Crystal structures of MO25 in complex with MST4, MST3, and STK25 revealed a unified activation mechanism: MO25 rotates the αC helix of GCK-family kinases into an active conformation, analogous to but distinct from the two-step mechanism used for LKB1 (where MO25 first activates pseudokinase STRAD, which then activates LKB1).

    Evidence X-ray crystallography of MO25α–MST4, MO25β–MST3, and MO25α–STK25 complexes with mutagenesis and kinase assays

    PMID:23296203 PMID:23434407 PMID:24746913

    Open questions at the time
    • Whether αC-helix rotation is sufficient or also requires dimerization-dependent trans-autophosphorylation in vivo was not fully resolved
    • No structural data for MO25–SPAK/OSR1 complexes
  7. 2018 Medium

    WNK-catalyzed phosphorylation of the C-terminal WEWS motif of SPAK/OSR1 was found to enhance their binding to MO25, providing a mechanism by which upstream WNK signaling primes SPAK/OSR1 for MO25-mediated activation; Drosophila studies confirmed that Mo25 is required for stimulated (but not basal) transepithelial ion flux via the WNK–SPAK axis.

    Evidence Phosphomimetic mutagenesis, in vitro kinase assays, co-immunoprecipitation, Drosophila Mo25 knockdown with ion flux measurements

    PMID:29602832 PMID:30060950

    Open questions at the time
    • Relative contributions of WNK phosphorylation versus chloride sensing in regulating MO25–SPAK interaction in vivo were not dissected
    • No mammalian in vivo validation at this stage
  8. 2024 High

    Double knockout of Cab39/Cab39l in mouse distal convoluted tubule abolished NCC phosphorylation and produced a Gitelman-like phenotype, directly demonstrating that MO25 proteins are essential for SPAK apical membrane localization and NCC activation in vivo; without MO25, phosphorylated SPAK accumulates in cytoplasmic condensates that contain WNK4 and L-WNK1 but cannot reach the apical membrane.

    Evidence Conditional and global double-knockout mice, immunofluorescence, immunoblotting, electrolyte measurements, triple-KO genetic epistasis with KS-WNK1

    PMID:38258567 PMID:41903110

    Open questions at the time
    • Identity and biophysical nature of the SPAK-containing cytoplasmic condensates are not fully characterized
    • Whether MO25 loss affects other renal transport pathways beyond NCC/NKCC remains open

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key open questions include: (1) how MO25 selectively partitions between the LKB1–STRAD complex and free GCK kinases in different tissues; (2) whether post-translational modifications of MO25 itself regulate its activity or localization; (3) the structural basis of the MO25–SPAK/OSR1 interaction; and (4) whether therapeutic targeting of the MO25 interface can selectively modulate AMPK versus ion-transport signaling.
  • No structure of MO25–SPAK/OSR1 complex exists
  • No post-translational modification map for MO25 has been reported
  • Tissue-specific stoichiometric competition between LKB1 and GCK kinases for MO25 has not been measured

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 8 GO:0060090 molecular adaptor activity 4
Localization
GO:0005829 cytosol 3 GO:0005886 plasma membrane 2
Pathway
R-HSA-162582 Signal Transduction 6 R-HSA-382551 Transport of small molecules 4 R-HSA-9612973 Autophagy 1
Partners
LKB1MST3MST4OSR1SPAKSTK25STRADΑWNK4
Complex memberships
LKB1–STRADα–MO25α heterotrimer

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2003 MO25α/β (CAB39) forms a trimeric complex with LKB1 and STRADα/β that functions as an upstream kinase (AMPKK) phosphorylating AMPK at Thr172; both endogenous and recombinant LKB1-STRADα/β-MO25α/β complexes activate AMPK, and catalytically active LKB1, STRAD, and MO25 are all required for full activity. Biochemical purification from rat liver, immunoprecipitation, in vitro kinase assay, genetic rescue in HeLa cells and LKB1-knockout fibroblasts Journal of biology High 14511394
2004 MO25α has two distinct binding surfaces (on opposite faces of the armadillo-repeat scaffold) required for assembly of the MO25α-STRADα-LKB1 complex; MO25α binding markedly increases STRADα affinity for LKB1 and activates LKB1 kinase activity without requiring phosphorylation of the LKB1 T-loop; STRADα binds ATP with high affinity but this ATP-binding is not required for LKB1 activation. Site-directed mutagenesis of MO25α and LKB1 cancer mutants, co-immunoprecipitation, in vitro kinase assay Journal of cell science High 15561763
2004 Crystal structure of MO25α reveals a helical repeat (Armadillo-like) fold; MO25α binds directly to a conserved Trp-Glu-Phe (WEF) motif at the STRADα C-terminus via a hydrophobic pocket, markedly enhancing STRADα-LKB1 binding and LKB1 catalytic activity. X-ray crystallography (MO25α–STRADα peptide complex), mutagenesis, in vitro binding and kinase assays Nature structural & molecular biology High 14730349
2005 Long-chain acyl-CoA esters (LCACEs, e.g., palmitoyl-CoA) inhibit phosphorylation of AMPK by the recombinant LKB1/STRAD/MO25 complex in a substrate-specific, AMP-dependent manner, without inhibiting LKB1/STRAD/MO25 activity toward a peptide substrate (LKB1tide), revealing that the MO25 complex has substrate-specific regulatory properties. In vitro kinase assay with recombinant LKB1/STRAD/MO25, liver-purified AMPKK, and defined metabolites American journal of physiology. Endocrinology and metabolism Medium 15644453
2009 Crystal structure of the core heterotrimeric LKB1-STRADα-MO25α complex reveals that STRADα adopts a closed, active-kinase-like conformation and binds LKB1 as a pseudosubstrate; MO25α stabilizes the active conformation of LKB1 by interacting with the LKB1 activation loop, providing a phosphorylation-independent allosteric activation mechanism. X-ray crystallography of the heterotrimer, mutagenesis, in vitro kinase assay Science (New York, N.Y.) High 19892943
2009 MO25α (CAB39) directly interacts with the STE20 kinase MST4, and this interaction translocates MST4 from the Golgi to the subapical membrane compartment upon LKB1 activation; MST4 phosphorylates Ezrin at T567 as an essential step in LKB1/STRAD/MO25-induced brush border formation. Co-immunoprecipitation, live-cell imaging, kinase assay, MST4 inhibition/loss-of-function Developmental cell High 19386264
2011 MO25α/β (CAB39/CAB39L) directly binds and activates SPAK/OSR1 (~100-fold) and MST3/MST4/YSK1 (3–4-fold) STE20 kinases in a manner analogous to STRADα binding; MO25-activated SPAK/OSR1 phosphorylates ion co-transporters NKCC1, NKCC2, and NCC; siRNA knockdown of MO25 in mammalian cells reduces endogenous NKCC1 phosphorylation, rescued by MO25α re-expression. In vitro kinase assay, siRNA knockdown with phosphorylation rescue, mass spectrometry identification of new phosphorylation sites The EMBO journal High 21423148
2011 miR-451 directly targets CAB39 3′-UTR (confirmed by luciferase reporter assay), reducing CAB39 protein levels and suppressing downstream PI3K/AKT pathway activity in glioma cells. Luciferase 3′-UTR reporter assay, Western blot, transfection of miR-451 mimics in glioma cell lines International journal of oncology Medium 22179124
2012 miR-195 and miR-451 functionally target MO25 (CAB39) in cardiac cells; overexpression of miR-195 in C2C12 cells knocks down MO25 expression and suppresses downstream AMPK signaling (reduced ACC phosphorylation and AMPK activity), phenocopying MO25 siRNA knockdown. miRNA overexpression, siRNA knockdown, AMPK activity assay, Western blot for ACC phosphorylation PloS one Medium 22844503
2013 Crystal structure of MST4 kinase domain in complex with MO25 shows that MO25 binding rotates the αC helix of MST4 toward its catalytic core, stabilizing MST4 in an active conformation; MST4 kinase domain forms a homodimer required for trans-autophosphorylation; interface mutations disrupting MST4-MO25 interaction or MST4 homodimerization impair MST4 activation and pro-apoptotic function in HEK293T cells. X-ray crystallography, mutagenesis of interface residues, in vitro kinase assay, cell-based apoptosis assay Structure (London, England : 1993) High 23434407
2013 Crystal structure of MST3 catalytic domain in complex with MO25β reveals that MO25β stabilizes the MST3 kinase domain in a closed, active conformation (active αC helix and A-loop) via an interaction mode similar to MO25α–STRADα; key interface residues Tyr223 of MO25β and Glu58/Ile71 of MST3, when mutated, prevent MO25β-mediated MST3 activation. X-ray crystallography, mutagenesis, in vitro kinase assay Biochemical and biophysical research communications High 23296203
2014 CAB39 (MO25) acts as a binding partner that differentially interacts with WNK4 and SPAK/OSR1, enabling WNK4 to activate NKCC1 in a SPAK/OSR1-independent manner; a PF2-like domain in WNK4 mediates direct interaction with the N-terminal domain of NKCC1, demonstrated by yeast two-hybrid, molecular modeling, and functional cotransporter assays. Yeast two-hybrid, co-immunoprecipitation, functional NKCC1 activation assay in Xenopus oocytes, molecular modeling The Journal of biological chemistry Medium 24811174
2014 Structural analysis of MO25α complexes with STK25 and MST3 reveals a unified mechanism: MO25 directly activates GCK-family kinases (MST3, MST4, STK25, OSR1, SPAK) by stabilizing an active αC helix and A-loop conformation, whereas LKB1 activation requires an additional layer using MO25 to activate the pseudokinase STRAD, which in turn activates LKB1. X-ray crystallography (MO25α–STK25 and MO25α–MST3 structures), comparative structural analysis Journal of structural biology High 24746913
2018 In Drosophila Malpighian tubules, Mo25 (CAB39 ortholog) enhances the kinase activity of Fray (SPAK homolog) in vitro and is required for stimulated (but not basal) transepithelial ion flux; Mo25 cooperates with intracellular chloride to regulate WNK signaling and cotransporter-mediated ion transport. In vitro kinase assay (Drosophila Mo25 + Fray), transgenic Drosophila knockdown, ion flux measurements, chloride sensor imaging Journal of the American Society of Nephrology : JASN Medium 29602832
2018 C-terminal serine phosphorylation within the WEWS motif of SPAK and OSR1 (catalyzed by WNK kinases in vitro and in cells) enhances their binding to MO25 (CAB39); mutagenesis of key MO25 residues abrogates MO25-mediated activation of SPAK/OSR1. In vitro kinase assay, phosphomimetic mutagenesis, cell-based co-immunoprecipitation, MO25 interface mutagenesis Biochemical and biophysical research communications Medium 30060950
2022 Intracellular Midkine (MDK) interacts with LKB1 and STRAD to disrupt the LKB1-STRAD-MO25 (CAB39) complex, reducing LKB1 kinase activity and dampening basal and stress-induced AMPK activation. Co-immunoprecipitation, in vitro kinase assay, 2-DG/glucose starvation stress assays, cancer cell proliferation assays Cell death & disease Medium 35487917
2024 Global/inducible double knockout of Cab39 and Cab39l in mouse distal convoluted tubule abolishes NCC phosphorylation (Gitelman-like phenotype); Cab39 proteins are required to localize SPAK at the apical membrane with NCC — in their absence, phosphorylated SPAK is confined to intracellular puncta, preventing NCC activation. Conditional and global mouse knockout, Western blot, immunofluorescence, urine/blood electrolyte measurements Hypertension (Dallas, Tex. : 1979) High 38258567
2023 CAB39 promotes cisplatin resistance in bladder cancer through the CAB39-LKB1-AMPK-LC3 autophagy pathway; CAB39 knockdown sensitizes cisplatin-resistant cells to cisplatin and disrupts mitophagy-mediated ROS reduction; LKB1 knockdown downstream of CAB39 phenocopies CAB39 knockdown in resistance. Proteomic analysis of resistant vs. parental cells, gene knockdown (siRNA/shRNA), overexpression, autophagy flux assays, in vivo xenograft Free radical biology & medicine Medium 37726090
2026 In Cab39/Cab39l double-knockout mouse distal convoluted tubule, phosphorylated SPAK accumulates in cytoplasmic puncta (distinct from canonical WNK bodies) independently of KS-WNK1; these condensates require active upstream phosphorylation and contain WNK4 and L-WNK1 but are absent under high-K+ conditions; Cab39 is thus required for SPAK translocation from condensates to the apical membrane to phosphorylate NCC. Triple knockout mice (Cab39-DKO × KS-WNK1 KO), immunofluorescence, immunoblotting, dietary K+ manipulation American journal of physiology. Renal physiology Medium 41903110
2024 STRAD-binding small molecules can activate LKB1 kinase activity in a target-dependent manner in cancer cell lines, demonstrating that pharmacological engagement of the STRAD subunit of the LKB1-STRAD-MO25 complex is sufficient to stimulate the complex. Small-molecule screen, LKB1 kinase activity assay, cancer cell line target-dependent proliferation assay bioRxivpreprint Low bio_10.1101_2024.12.17.628051

Source papers

Stage 0 corpus · 53 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2003 Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade. Journal of biology 1335 14511394
2009 Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation. Science (New York, N.Y.) 284 19892943
2009 Mst4 and Ezrin induce brush borders downstream of the Lkb1/Strad/Mo25 polarization complex. Developmental cell 131 19386264
2004 Analysis of the LKB1-STRAD-MO25 complex. Journal of cell science 129 15561763
2011 MicroRNA miR-451 downregulates the PI3K/AKT pathway through CAB39 in human glioma. International journal of oncology 127 22179124
2011 MO25 is a master regulator of SPAK/OSR1 and MST3/MST4/YSK1 protein kinases. The EMBO journal 121 21423148
2004 Crystal structure of MO25 alpha in complex with the C terminus of the pseudo kinase STE20-related adaptor. Nature structural & molecular biology 63 14730349
2005 Fission yeast MO25 protein is localized at SPB and septum and is essential for cell morphogenesis. The EMBO journal 61 16096637
2012 Micro-RNA-195 and -451 regulate the LKB1/AMPK signaling axis by targeting MO25. PloS one 60 22844503
2018 MiRNA-451 Inhibits Glioma Cell Proliferation and Invasion Through the mTOR/HIF-1α/VEGF Signaling Pathway by Targeting CAB39. Human gene therapy. Clinical development 53 30180756
2005 Long-chain acyl-CoA esters inhibit phosphorylation of AMP-activated protein kinase at threonine-172 by LKB1/STRAD/MO25. American journal of physiology. Endocrinology and metabolism 52 15644453
2012 The NDR kinase scaffold HYM1/MO25 is essential for MAK2 map kinase signaling in Neurospora crassa. PLoS genetics 49 23028357
2021 Metformin-Induced MicroRNA-34a-3p Downregulation Alleviates Senescence in Human Dental Pulp Stem Cells by Targeting CAB39 through the AMPK/mTOR Signaling Pathway. Stem cells international 45 33505470
2008 Thyroid hormone effects on LKB1, MO25, phospho-AMPK, phospho-CREB, and PGC-1alpha in rat muscle. Journal of applied physiology (Bethesda, Md. : 1985) 42 18669938
2018 Intracellular Chloride and Scaffold Protein Mo25 Cooperatively Regulate Transepithelial Ion Transport through WNK Signaling in the Malpighian Tubule. Journal of the American Society of Nephrology : JASN 40 29602832
2017 MiR-451 Promotes Cell Proliferation and Metastasis in Pancreatic Cancer through Targeting CAB39. BioMed research international 39 28197410
2013 Structure of the MST4 in complex with MO25 provides insights into its activation mechanism. Structure (London, England : 1993) 39 23434407
2020 MicroRNA-31-5p Exacerbates Lipopolysaccharide-Induced Acute Lung Injury via Inactivating Cab39/AMPKα Pathway. Oxidative medicine and cellular longevity 35 33101593
2014 A novel Ste20-related proline/alanine-rich kinase (SPAK)-independent pathway involving calcium-binding protein 39 (Cab39) and serine threonine kinase with no lysine member 4 (WNK4) in the activation of Na-K-Cl cotransporters. The Journal of biological chemistry 35 24811174
2005 The fission yeast MO25 protein functions in polar growth and cell separation. European journal of cell biology 35 16325501
2022 Eucalyptol relieves imidacloprid-induced autophagy through the miR-451/Cab39/AMPK axis in Ctenopharyngodon idellus kidney cells†. Aquatic toxicology (Amsterdam, Netherlands) 34 35661494
2016 WNK-Cab39-NKCC1 signaling increases the susceptibility to ischemic brain damage in hypertensive rats. Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism 26 27798271
1996 Molecular characterization of the Drosophila Mo25 gene, which is conserved among Drosophila, mouse, and yeast. DNA and cell biology 26 8672247
2020 miR-107 inhibition upregulates CAB39 and activates AMPK-Nrf2 signaling to protect osteoblasts from dexamethasone-induced oxidative injury and cytotoxicity. Aging 25 32527986
2004 Endurance training increases LKB1 and MO25 protein but not AMP-activated protein kinase kinase activity in skeletal muscle. American journal of physiology. Endocrinology and metabolism 25 15292028
2022 Midkine noncanonically suppresses AMPK activation through disrupting the LKB1-STRAD-Mo25 complex. Cell death & disease 23 35487917
2013 Structural insights into the activation of MST3 by MO25. Biochemical and biophysical research communications 22 23296203
2005 Evidence against regulation of AMP-activated protein kinase and LKB1/STRAD/MO25 activity by creatine phosphate. American journal of physiology. Endocrinology and metabolism 21 16278246
2020 HPV16 E6/E7 promote the translocation and glucose uptake of GLUT1 by PI3K/AKT pathway via relieving miR-451 inhibitory effect on CAB39 in lung cancer cells. Therapeutic advances in chronic disease 19 32994913
2019 Antagonism of miR-429 ameliorates anoxia/reoxygenation injury in cardiomyocytes by enhancing MO25/LKB1/AMPK mediated autophagy. Life sciences 18 31494170
2022 MicroRNA-22 promoted osteogenic differentiation of valvular interstitial cells by inhibiting CAB39 expression during aortic valve calcification. Cellular and molecular life sciences : CMLS 17 35190902
2014 Structural insights into regulatory mechanisms of MO25-mediated kinase activation. Journal of structural biology 17 24746913
2023 CAB39 promotes cisplatin resistance in bladder cancer via the LKB1-AMPK-LC3 pathway. Free radical biology & medicine 16 37726090
2007 The GC kinase Fray and Mo25 regulate Drosophila asymmetric divisions. Biochemical and biophysical research communications 16 18054329
2006 Effects of 3-phosphoglycerate and other metabolites on the activation of AMP-activated protein kinase by LKB1-STRAD-MO25. American journal of physiology. Endocrinology and metabolism 16 16985256
2020 Circular RNA circGSK3B Promotes Cell Proliferation, Migration, and Invasion by Sponging miR-1265 and Regulating CAB39 Expression in Hepatocellular Carcinoma. Frontiers in oncology 15 33262952
2013 Cell cycle regulated interaction of a yeast Hippo kinase and its activator MO25/Hym1. PloS one 15 24205201
2015 LKB1/Mo25/STRAD uniquely impacts sarcomeric contractile function and posttranslational modification. Biophysical journal 13 25809261
2024 Kinase Scaffold Cab39 Is Necessary for Phospho-Activation of the Thiazide-Sensitive NCC. Hypertension (Dallas, Tex. : 1979) 11 38258567
2018 C-terminal phosphorylation of SPAK and OSR1 kinases promotes their binding and activation by the scaffolding protein MO25. Biochemical and biophysical research communications 9 30060950
2017 Towards the Development of Small-Molecule MO25 Binders as Potential Indirect SPAK/OSR1 Kinase Inhibitors. Chembiochem : a European journal of chemical biology 9 28004876
2018 Evolutionary history of Mo25 gene in plants, a component of RAM/MOR signaling network. Mechanisms of development 7 30208334
2023 MAPKAPK5-AS1/miR-515-5p/CAB39 Axis Contributes to Non-small Cell Lung Cancer Cell Proliferation and Migration. Molecular biotechnology 5 36867352
2023 MicroRNA-32-3p facilitates cerebral ischemia/reperfusion injury through inhibiting Cab39/AMPK. International immunopharmacology 5 37379707
2022 Long noncoding RNA TRG-AS1 protects against glucocorticoid-induced osteoporosis in a rat model by regulating miR-802-mediated CAB39/AMPK/SIRT-1/NF-κB axis. Human cell 5 35794445
2024 miR-451a was selectively sorted into exosomes and promoted the progression of esophageal squamous cell carcinoma through CAB39. Cancer gene therapy 4 38649419
2020 CAB39 Promotes the Proliferation of Nasopharyngeal Carcinoma CNE-1 Cells via Up-Regulating p-JNK. Cancer management and research 4 33177871
2013 Structure of zebrafish MO25. Acta crystallographica. Section F, Structural biology and crystallization communications 4 23989145
2025 Roles of the MO25 protein Pmo25 in contractile-ring stability and localization of the NDR kinase Sid2 during cytokinesis. bioRxiv : the preprint server for biology 2 40463288
2024 CAB39 modulates epithelial-mesenchymal transition through NF-κB signaling activation, enhancing invasion, and metastasis in bladder cancer. Environmental toxicology 2 39171884
2021 Retracted: MiR-451 Promotes Cell Proliferation and Metastasis in Pancreatic Cancer through Targeting CAB39. BioMed research international 1 33855067
2026 Deletion of Cab39 adaptors results in KS-WNK1 independent accumulation of SPAK in biomolecular condensates. American journal of physiology. Renal physiology 0 41903110
2025 The MO25 protein Pmo25 functions in contractile ring stability and Sid2 localization during cytokinesis. iScience 0 41550769