Affinage

MICALL2

MICAL-like protein 2 · UniProt Q8IY33

Length
904 aa
Mass
97.5 kDa
Annotated
2026-06-10
26 papers in source corpus 19 papers cited in narrative 19 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

MICALL2 (JRAB) is a multidomain scaffold protein (CH–LIM–coiled-coil) that acts as an effector of GTP-bound Rab13, and also Rab8, to couple vesicle trafficking with actin cytoskeletal reorganization at epithelial junctions (PMID:16525024, PMID:18094055, PMID:18413246). Through its C-terminal coiled-coil it binds active Rab13/Rab8, and through its membrane-targeting and LIM regions it engages the actin cross-linkers actinin-1/4 and filamins and binds F-actin directly, thereby regulating actin cross-linking and stabilization (PMID:18332111, PMID:23100251, PMID:23890175, PMID:31488862). In this capacity it mediates endocytic recycling of tight- and adherens-junction proteins—occludin, claudin-1, and E-cadherin—to the plasma membrane and is required for coordinated TJ/AJ assembly (PMID:16525024, PMID:18094055). MICALL2 operates as a conformational switch: an intramolecular interaction between its N-terminal CH/LIM domains and the C-terminal coiled-coil holds it closed, and Rab13 binding opens the molecule to transfer actinin-4 onto actin structures; this Rab13-dependent open/closed plasticity governs actin remodeling, junctional maturation, and the directionality of collective cell migration (PMID:20008558, PMID:23100251, PMID:27582384, PMID:31488862). Beyond junctions, MICALL2 serves as a Rab13-dependent scaffold linking GLUT4 to a Rab13–MICALL2–ACTN4 ternary complex during insulin-stimulated GLUT4 translocation (PMID:26538022). In cancer contexts MICALL2 acts as a stability factor for multiple oncogenic effectors—stabilizing EGFR by blocking its lysosomal degradation via Cdc42- or Rac1-dependent signaling (PMID:31034158, PMID:38203692), stabilizing c-Myc by preventing Thr58 phosphorylation and polyubiquitination (PMID:33520979), shielding β-catenin from GSK3β to activate Wnt signaling (PMID:41461119), and stabilizing ACTN4 in a Rab13-dependent manner (PMID:39689763). MICALL2's own abundance is set by opposing ubiquitin machinery: TRIM21 ubiquitinates it for proteasomal degradation, while the proteasome-associated deubiquitinase PSMD14 stabilizes it (PMID:36307841, PMID:42174657).

Mechanistic history

Synthesis pass · year-by-year structured walk · 18 steps
  1. 2006 High

    Established MICALL2 as a Rab13 effector that links a small GTPase to junctional vesicle trafficking, answering how Rab13 controls tight junction assembly.

    Evidence Co-IP, recycling and Ca2+-switch assays with a Rab13-binding-deficient mutant in epithelial cells

    PMID:16525024

    Open questions at the time
    • Did not resolve the structural basis of GTP-dependent Rab13 binding
    • Cargo selectivity (occludin vs transferrin receptor) mechanism unexplained
  2. 2007 High

    Showed MICALL2 integrates two Rab GTPases by competitive binding, explaining how it coordinates both tight- and adherens-junction protein delivery.

    Evidence siRNA knockdown, dominant-negative MICAL-L2-C, Ca2+-switch and Co-IP in epithelial cells

    PMID:18094055

    Open questions at the time
    • Did not define how Rab8 vs Rab13 compartment selection is regulated
    • Spatial control of competition not addressed
  3. 2007 Medium

    Linked MICALL2/Rab13 to epithelial scattering, extending its role from static junctions to migratory behavior.

    Evidence siRNA knockdown with re-expression rescue and Rab13 activation assay in TPA-stimulated MDCK cells

    PMID:17891173

    Open questions at the time
    • Did not identify the molecular trigger coupling Rab13 activation to scattering
    • Single-lab observation
  4. 2008 High

    Identified actinin-4 as the link between MICALL2 and F-actin and defined the CH–LIM–coiled-coil domain architecture, providing the structural framework for its scaffold function.

    Evidence Yeast two-hybrid, Co-IP, siRNA, domain-deletion analysis and immunofluorescence

    PMID:18332111 PMID:18413246

    Open questions at the time
    • Precise actinin-4-binding domain boundaries partially defined
    • How Rab13 enhances the actinin-4 interaction left mechanistically open
  5. 2009 High

    Discovered the Rab13-driven intramolecular conformational switch, explaining how Rab13 binding mobilizes actinin-4 to remodel actin.

    Evidence Co-IP, dominant-active Rab13, neurite-outgrowth rescue in PC12 cells

    PMID:20008558

    Open questions at the time
    • Atomic structure of open vs closed states not determined
    • Kinetics of the conformational transition unknown
  6. 2012 High

    Demonstrated MICALL2 binds actinin-1/4 and F-actin through distinct domains to control actin cross-linking and junctional maturation, consolidating its cytoskeletal-regulatory role.

    Evidence Co-IP, domain deletion, live imaging with Rab13 mutants

    PMID:23100251

    Open questions at the time
    • Quantitative effect on actin cross-linking not measured in vitro
    • Hierarchy of multiple actin-binding partners unresolved
  7. 2013 Medium

    Showed the open conformation recruits filamins to drive cell spreading, distinguishing functional outputs of different MICALL2-bound cross-linkers.

    Evidence Co-IP with conformational mutants and ASB2-mediated filamin degradation in NIH3T3 cells

    PMID:23890175

    Open questions at the time
    • Why actinins co-precipitate but do not affect spreading unexplained
    • Single-lab, two-method support
  8. 2015 High

    Extended the scaffold function to metabolic trafficking by placing MICALL2 in an insulin-induced Rab13–MICALL2–ACTN4 complex that delivers GLUT4.

    Evidence Pull-down, Co-IP, siRNA, TIRF/SIM imaging in muscle cells

    PMID:26538022

    Open questions at the time
    • How insulin signaling triggers Rab13–MICALL2 binding not defined
    • Direct GLUT4 contact vs indirect not resolved
  9. 2016 High

    Built a structural model of the conformational switch and tied conformational plasticity directly to collective migration directionality.

    Evidence Structural modeling, biochemical conformation assays, live imaging and computational biomechanics with fixed-conformation mutants

    PMID:27582384

    Open questions at the time
    • Model not validated by experimental high-resolution structure
    • Upstream control of conformational state during migration unclear
  10. 2019 Medium

    Defined a direct F-actin-binding mechanism for the LIM zinc finger and showed overlap with the intramolecular interface, providing a molecular basis for fine-tuning MICALL2 activity.

    Evidence Biochemical actin-binding assays, mutagenesis, intramolecular interaction mapping

    PMID:31488862

    Open questions at the time
    • Functional consequence of minus-end binding on filament dynamics not tested in cells
    • Single-lab biochemistry
  11. 2019 Medium

    Opened a non-junctional oncogenic role by showing MICALL2 stabilizes EGFR via Cdc42-dependent inhibition of lysosomal degradation.

    Evidence Knockdown/overexpression, lysosome inhibitors, Cdc42 activation assays in gastric cancer cells

    PMID:31034158

    Open questions at the time
    • Direct biochemical link between MICALL2 and EGFR trafficking not reconstituted
    • Cdc42-dependence mechanism incomplete
  12. 2021 Medium

    Identified MICALL2 as a c-Myc stabilizer that blocks Thr58 phosphorylation and polyubiquitination, broadening its function to nuclear oncoprotein regulation.

    Evidence Co-IP, polyubiquitylation and protein-stability assays, siRNA in NSCLC cells

    PMID:33520979

    Open questions at the time
    • Whether the interaction is direct or how it blocks Thr58 phosphorylation unresolved
    • Single-lab
  13. 2022 Medium

    Defined upstream control of MICALL2 abundance by identifying TRIM21 as its degradative E3 ligase.

    Evidence Co-IP, mass spectrometry, ubiquitination assays and functional readouts in colorectal cancer cells

    PMID:36307841

    Open questions at the time
    • TRIM21 ubiquitination site(s) on MICALL2 not mapped
    • Single-lab
  14. 2023 Medium

    Showed EGFR stabilization can proceed through Rac1 rather than Cdc42, with MMP9 as a downstream effector, indicating context-dependent GTPase usage.

    Evidence Knockdown/overexpression, Rac1 inhibition, autophagy inhibitors, invasion assays in ovarian cancer cells

    PMID:38203692

    Open questions at the time
    • Basis for tissue-specific Cdc42 vs Rac1 choice unexplained
    • No in vitro reconstitution
  15. 2024 Medium

    Demonstrated Rab13-dependent stabilization of ACTN4 links MICALL2 to vimentin upregulation and therapy resistance, connecting its scaffold role to malignant progression.

    Evidence Co-IP, siRNA/overexpression and functional assays in clear cell renal cell carcinoma cells

    PMID:39689763

    Open questions at the time
    • Mechanism by which MICALL2 protects ACTN4 from degradation undefined
    • Single-lab
  16. 2025 Medium

    Established that MICALL2 shields β-catenin from GSK3β to activate Wnt signaling and identified a small molecule binding its C-terminus that disrupts this function.

    Evidence LiP-SMap, molecular dynamics, Co-IP and in vivo fibrosis model with overexpression rescue

    PMID:41461119

    Open questions at the time
    • Direct vs scaffolded MICALL2–β-catenin contact not fully resolved
    • Single-lab
  17. 2026 Medium

    Completed the regulatory loop on MICALL2 stability by showing the deubiquitinase PSMD14, controlled by DUSP4-mediated dephosphorylation, stabilizes MICALL2.

    Evidence Co-IP, ubiquitination and phosphorylation assays, siRNA, in vivo xenograft in ccRCC

    PMID:42174657

    Open questions at the time
    • Whether TRIM21 and PSMD14 act on the same ubiquitin sites unknown
    • Single-lab
  18. 2025 Low

    Flagged MICALL2 as a candidate LRRK2 kinase substrate, raising the possibility of phosphoregulation of the scaffold.

    Evidence Proximity-labeling MS and quantitative phosphoproteomics with LRRK inhibitors (preprint)

    PMID:bio_10.1101_2025.09.03.674114

    Open questions at the time
    • No direct in vitro kinase assay or site-specific mutagenesis confirming LRRK2-mediated phosphorylation
    • Functional consequence of phosphorylation unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the Rab13-driven conformational switch is mechanistically coupled to MICALL2's diverse protein-stabilization activities (EGFR, c-Myc, β-catenin, ACTN4) remains unresolved.
  • No high-resolution structure of full-length MICALL2 in either conformation
  • Whether stabilization activities are direct or scaffold-dependent unestablished
  • Upstream signals selecting junctional vs oncogenic functions undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0008092 cytoskeletal protein binding 4 GO:0060090 molecular adaptor activity 4 GO:0098772 molecular function regulator activity 4
Localization
GO:0005856 cytoskeleton 3 GO:0005886 plasma membrane 3 GO:0031410 cytoplasmic vesicle 2
Pathway
R-HSA-1500931 Cell-Cell communication 3 R-HSA-5653656 Vesicle-mediated transport 3 R-HSA-162582 Signal Transduction 2
Partners
ACTN1ACTN4CTNNB1MYCPSMD14RAB13RAB8ATRIM21
Complex memberships
Rab13–MICALL2–ACTN4 ternary complex

Evidence

Reading pass · 19 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2006 MICAL-L2 (JRAB) was identified as a Rab13 effector protein that specifically binds the GTP-bound form of Rab13 via its C-terminal coiled-coil domain, localizes at tight junctions in epithelial cells, and mediates endocytic recycling of occludin (but not transferrin receptor). A MICAL-L2 mutant lacking the Rab13-binding domain (MICAL-L2-N) specifically inhibited occludin recycling and blocked TJ formation in Ca2+-switch assays. MICAL-L2 was displaced from TJs upon actin depolymerization and redistributed along actin structures, indicating it links Rab13 to the actin cytoskeleton. Immunoprecipitation, immunofluorescence, recycling assay, Ca2+-switch assay, yeast two-hybrid (initial identification), dominant-negative mutant expression Molecular biology of the cell High 16525024
2007 JRAB/MICAL-L2 interacts with both Rab8 and Rab13 via its C-terminal domain, and these two Rab GTPases compete with each other for MICAL-L2 binding. Rab8 and Rab13 functionally associate with MICAL-L2 at perinuclear recycling/storage compartments and at the plasma membrane, respectively. Rab13 knockdown suppressed claudin-1 and occludin but not E-cadherin transport, while Rab8 knockdown inhibited Rab13-independent E-cadherin transport; MICAL-L2 knockdown or dominant-negative MICAL-L2-C expression inhibited transport of all three junctional proteins, coordinating TJ and AJ assembly. siRNA knockdown, dominant-negative mutant expression, Ca2+-switch assay, immunofluorescence, co-immunoprecipitation Molecular biology of the cell High 18094055
2008 Actinin-4 was identified as a binding partner for the plasma membrane-targeting domain of JRAB/MICAL-L2 using yeast two-hybrid and confirmed by co-immunoprecipitation. Actinin-4 colocalizes with JRAB/MICAL-L2 at cell-cell junctions and links JRAB/MICAL-L2 to F-actin. The actinin-4–MICAL-L2 interaction was enhanced by Rab13 activation. siRNA depletion of actinin-4 delayed JRAB/MICAL-L2 recruitment to cell-cell junctions and impaired functional TJ formation during epithelial polarization. Yeast two-hybrid, co-immunoprecipitation, siRNA knockdown, Ca2+-switch assay, immunofluorescence Molecular and cellular biology High 18332111
2008 JRAB/MICAL-L2 domain structure was characterized: it contains a calponin-homology (CH) domain at the N-terminus, a LIM domain in the middle, and a coiled-coil domain at the C-terminus. The C-terminus specifically binds the GTP-bound form of Rab13. In epithelial cells it localizes to tight junctions; in fibroblasts it distributes along stress fibers. Domain deletion analysis, immunoprecipitation, immunofluorescence, yeast two-hybrid (referenced prior work) Methods in enzymology Medium 18413246
2009 JRAB/MICAL-L2 exhibits an intramolecular interaction between its N-terminal CH and LIM domains and the C-terminal coiled-coil domain. Rab13 binding to JRAB/MICAL-L2 stimulates interaction of MICAL-L2 with actinin-4, which localizes to cell body and neurite tips in PC12 cells. Expression of MICAL-L2 alone inhibits neurite outgrowth, but co-expression of dominant-active Rab13 rescues this phenotype, suggesting Rab13-dependent conformational change enables transfer of actinin-4 to neurite tips to reorganize the actin cytoskeleton. Overexpression/dominant-active mutants, co-immunoprecipitation, immunofluorescence, neurite outgrowth assay in PC12 cells Molecular and cellular biology High 20008558
2007 Rab13 and JRAB/MICAL-L2 are involved in epithelial cell scattering in response to TPA. During TPA-induced MDCK cell scattering, Rab13 was transiently activated, and both Rab13 and JRAB/MICAL-L2 co-localized with F-actin at cell-cell contact sites before accumulating at lamellipodia. Knockdown of JRAB/MICAL-L2 inhibited TPA-induced scattering, rescued by re-expression of mouse JRAB/MICAL-L2. siRNA knockdown, rescue by re-expression, immunofluorescence, Rab13 activation assay Oncogene Medium 17891173
2012 JRAB/MICAL-L2 interacts with both actinin-1 and actinin-4 and with filamentous actin (F-actin) via different domains, and regulates actin cross-linking and stabilization. During epithelial junctional development, JRAB is enriched in the actin bundle at the free border and undergoes a Rab13-dependent conformational change required for maturation of cell-cell adhesion. Co-immunoprecipitation, domain deletion analysis, immunofluorescence, live imaging, Rab13 dominant-active/dominant-negative mutants The Journal of biological chemistry High 23100251
2013 In the 'open' conformation (JRABΔCC mutant), JRAB/MICAL-L2 co-immunoprecipitates with filamin (an actin cross-linking protein). Expression of ASB2, which induces degradation of all three filamin isoforms, inhibited JRABΔCC-induced cell spreading with membrane ruffles, demonstrating that JRAB regulates actin cytoskeletal reorganization and cell spreading through filamins. In contrast, actinin-1/-4 co-precipitated with JRABΔCC but did not affect cell spreading. Co-immunoprecipitation with conformational mutants, ASB2-mediated filamin degradation, morphological analysis in NIH3T3 cells Genes to cells Medium 23890175
2015 Rab13 engages MICAL-L2 as a scaffold upon insulin stimulation in muscle cells. Insulin increased Rab13 binding to MICAL-L2 and binding of MICAL-L2 to α-actinin-4 (ACTN4), forming an insulin-dependent ternary complex (Rab13–MICAL-L2–ACTN4). GLUT4 associated with this complex in response to insulin via the ACTN4-binding domain of MICAL-L2. Knockdown of MICAL-L2 or expression of truncated MICAL-L2-CT impaired insulin-stimulated GLUT4 translocation to the plasma membrane. Co-immunoprecipitation, pull-down with MICAL-L2 fragments, siRNA knockdown, confocal fluorescence, TIRF microscopy, structured illumination microscopy Molecular biology of the cell High 26538022
2016 JRAB/MICAL-L2 undergoes a Rab13-dependent conformational change between closed and open states. A structural model was generated by bioinformatic and biochemical analyses. Impairment of MICAL-L2 conformational plasticity (using fixed conformation mutants) caused excessive rigidity and loss of directionality in collective cell migration. Live imaging and computational analysis showed that closed/open conformations dictate distinct collective migration behaviors. Structural modeling, biochemical conformation assays, live imaging, computational biomechanics, mutant expression Molecular biology of the cell High 27582384
2019 The first LIM zinc finger domain of JRAB/MICAL-L2 binds the first and second actin molecules at the minus end of F-actin, potentially inhibiting actin filament depolymerization. This same zinc finger domain also contributes to the intramolecular interaction with the C-terminal coiled-coil domain, and residues responsible for intramolecular interaction overlap with those involved in F-actin association, providing a mechanism for fine-tuning JRAB function. Biochemical actin-binding assays, mutagenesis, intramolecular interaction mapping, co-immunoprecipitation with mutants Scientific reports Medium 31488862
2019 MICAL-L2 expression upregulated EGFR protein level through a transcription-independent mechanism involving inhibition of EGFR degradation in lysosomes. This effect on EGFR stability was mediated in a Cdc42-dependent manner, activating downstream HSP27/cytoskeleton and HSP27/β-catenin signaling pathways to promote gastric cancer cell migration. siRNA knockdown, overexpression, Western blotting, lysosome inhibitor experiments, Cdc42 activation assays, immunofluorescence Journal of cellular and molecular medicine Medium 31034158
2021 MICAL-L2 physically interacts with c-Myc protein (co-immunoprecipitation), maintains nuclear c-Myc levels, prolongs its half-life, and inhibits c-Myc polyubiquitination. MICAL-L2 knockdown accelerated c-Myc degradation through polyubiquitylation; MICAL-L2 blocked c-Myc phosphorylation at Thr58, which is required for ubiquitin-dependent c-Myc degradation, thereby acting as a deubiquitination/stabilization factor for c-Myc in NSCLC cells. Co-immunoprecipitation, immunofluorescence, polyubiquitylation detection assay, protein stability assay, siRNA knockdown, Western blotting Frontiers in cell and developmental biology Medium 33520979
2022 TRIM21 (ubiquitin E3 ligase) mediates ubiquitination and proteasome-dependent degradation of MICALL2, acting as a negative regulator. Co-immunoprecipitation and mass spectrometry identified TRIM21 as a MICALL2-interacting protein. TRIM21 expression negatively correlates with MICALL2 levels and reversely regulates MICALL2-dependent tumorigenic activity (growth and migration via Wnt/β-catenin) in colorectal cancer cells. Co-immunoprecipitation, mass spectrometry, ubiquitination assays, siRNA/overexpression functional assays, Western blotting Cell communication and signaling Medium 36307841
2023 MICALL2 silencing in ovarian cancer cells promoted EGFR lysosomal degradation in a Rac1-dependent (rather than Cdc42-dependent as in gastric cancer) manner. Rac1 suppression attenuated MICALL2-induced pro-EGFR, pro-MMP9, and pro-invasion effects. MMP9 was identified as the target gene downstream of MICALL2 via EGFR-AKT-mTOR signaling, regulating invadopodium formation and cell invasion. siRNA knockdown, overexpression, Rac1 inhibition, autophagy inhibitors (acadesine, chloroquine), co-immunoprecipitation, invasion assays International journal of molecular sciences Medium 38203692
2024 MICAL-L2 stabilizes ACTN4 protein in a Rab13-dependent manner in clear cell renal cell carcinoma (KIRC) cells, reducing ACTN4 degradation. This MICAL-L2–ACTN4 complex interaction was confirmed by co-immunoprecipitation. ACTN4 stabilization leads to increased Vimentin expression, promoting cancer progression and resistance to sunitinib and everolimus. Co-immunoprecipitation, siRNA knockdown, overexpression, Western blotting, wound-healing, Transwell, CCK-8 assays Biochimica et biophysica acta. Molecular basis of disease Medium 39689763
2025 MICALL2 prevents β-catenin from binding to GSK3β, thereby shielding β-catenin from degradation and promoting Wnt/β-catenin signaling in hepatic stellate cells. A small molecule IMB16-5 binds to the C-terminal domain of MICALL2 (identified by LiP-SMap and molecular dynamics simulation) and disrupts the MICALL2–β-catenin interaction, suppressing β-catenin nuclear translocation and HSC activation. MICALL2 overexpression in vivo abolished the therapeutic efficacy of IMB16-5, confirming target engagement. LiP-SMap (limited proteolysis-small molecule mapping), molecular dynamics simulation, co-immunoprecipitation, in vivo mouse fibrosis model, overexpression rescue experiment International immunopharmacology Medium 41461119
2026 PSMD14 (a proteasome deubiquitinase) physically interacts with MICALL2 (confirmed by co-immunoprecipitation) and suppresses MICALL2 ubiquitination and degradation, thereby increasing MICALL2 protein levels. DUSP4-mediated dephosphorylation of PSMD14 enhances PSMD14–MICALL2 interaction and amplifies PSMD14's stabilizing effect on MICALL2, promoting ccRCC malignant progression. Co-immunoprecipitation, immunoprecipitation for ubiquitination analysis, PSMD14 phosphorylation analysis, siRNA knockdown, Western blotting, in vivo xenograft model Journal of translational medicine Medium 42174657
2025 MICALL2 was identified as a candidate substrate of LRRK2 kinase in proximity-labeling mass spectrometry and quantitative phosphoproteomics experiments. LRRK2 inhibitors altered MICALL2 phosphorylation status at the proteome-wide level. Proximity labeling mass spectrometry (BioID/TurboID), quantitative phosphoproteomics, LRRK1/2 inhibitor treatment bioRxivpreprint Low bio_10.1101_2025.09.03.674114

Source papers

Stage 0 corpus · 26 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2007 The interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the assembly of tight junctions and adherens junctions. Molecular biology of the cell 102 18094055
2006 JRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the endocytic recycling of occludin. Molecular biology of the cell 84 16525024
2009 Rab13 regulates neurite outgrowth in PC12 cells through its effector protein, JRAB/MICAL-L2. Molecular and cellular biology 68 20008558
2015 A complex of Rab13 with MICAL-L2 and α-actinin-4 is essential for insulin-dependent GLUT4 exocytosis. Molecular biology of the cell 52 26538022
2008 Involvement of actinin-4 in the recruitment of JRAB/MICAL-L2 to cell-cell junctions and the formation of functional tight junctions. Molecular and cellular biology 48 18332111
2015 Silencing of MICAL-L2 suppresses malignancy of ovarian cancer by inducing mesenchymal-epithelial transition. Cancer letters 42 25864591
2012 Rab13 small G protein and junctional Rab13-binding protein (JRAB) orchestrate actin cytoskeletal organization during epithelial junctional development. The Journal of biological chemistry 37 23100251
2019 MICAL-L2 potentiates Cdc42-dependent EGFR stability and promotes gastric cancer cell migration. Journal of cellular and molecular medicine 33 31034158
2007 Involvement of Rab13 and JRAB/MICAL-L2 in epithelial cell scattering. Oncogene 31 17891173
2017 A new locus regulating MICALL2 expression was identified for association with executive inhibition in children with attention deficit hyperactivity disorder. Molecular psychiatry 22 28416812
2023 Comprehensive Analysis of MICALL2 Reveals Its Potential Roles in EGFR Stabilization and Ovarian Cancer Cell Invasion. International journal of molecular sciences 20 38203692
2016 Conformational plasticity of JRAB/MICAL-L2 provides "law and order" in collective cell migration. Molecular biology of the cell 18 27582384
2013 Junctional Rab13-binding protein (JRAB) regulates cell spreading via filamins. Genes to cells : devoted to molecular & cellular mechanisms 15 23890175
2022 MICALL2 as a substrate of ubiquitinase TRIM21 regulates tumorigenesis of colorectal cancer. Cell communication and signaling : CCS 14 36307841
2019 Actin Cytoskeletal Reorganization Function of JRAB/MICAL-L2 Is Fine-tuned by Intramolecular Interaction between First LIM Zinc Finger and C-terminal Coiled-coil Domains. Scientific reports 13 31488862
2021 MICAL-L2 Is Essential for c-Myc Deubiquitination and Stability in Non-small Cell Lung Cancer Cells. Frontiers in cell and developmental biology 11 33520979
2008 Identification and characterization of JRAB/MICAL-L2, a junctional Rab13-binding protein. Methods in enzymology 8 18413246
2023 MICALL2 participates in the regulation of epithelial-mesenchymal transition in alveolar epithelial cells - Potential roles in pulmonary fibrosis. Archives of biochemistry and biophysics 6 37690696
2024 MICAL-L2, as an estrogen-responsive gene, is involved in ER-positive breast cancer cell progression and tamoxifen sensitivity via the AKT/mTOR pathway. Biochemical pharmacology 5 38729448
2018 Dancing Styles of Collective Cell Migration: Image-Based Computational Analysis of JRAB/MICAL-L2. Frontiers in cell and developmental biology 5 29468157
2022 Copy Number Variations in the MICALL2 and MOGAT2 Genes Are Associated with Ashidan Yak Growth Traits. Animals : an open access journal from MDPI 4 36290165
2023 Micall2 Is Responsible for the Malignancy of Clear Cell Renal Cell Carcinoma. Yonago acta medica 3 36811029
2024 High MICAL-L2 promotes cancer progression and drug resistance in renal clear cell carcinoma cells through stabilization of ACTN4 following vimentin expression. Biochimica et biophysica acta. Molecular basis of disease 2 39689763
2026 MICALL2 promotes angiogenesis of colorectal cancer by regulating the EGFR/PI3K/AKT/KLF5/VEGFA axis. Biochemical pharmacology 0 41617093
2026 DUSP4-mediated dephosphorylation of PSMD14 enhances PSMD14-dependent deubiquitination of MICALL2 and promotes malignant progression in clear cell renal cell carcinoma. Journal of translational medicine 0 42174657
2025 IMB16-5 alleviates liver fibrosis by targeting MICALL2/β-catenin signaling. International immunopharmacology 0 41461119

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