| 1966 |
Aldolase C (fructose-1,6-bisphosphate aldolase, brain isozyme) was identified as one of multiple distinct forms of fructose diphosphate aldolase in mammalian tissues, establishing it as a tissue-specific glycolytic enzyme isozyme. |
Biochemical fractionation and enzymatic characterization of mammalian tissue extracts |
Proceedings of the National Academy of Sciences of the United States of America |
High |
5230152
|
| 2006 |
ALDOC was identified as a lysine-acetylated protein in mammalian cells, including mitochondrial fractions, revealing post-translational acetylation as a regulatory modification on this glycolytic enzyme. |
Proteomic survey using anti-acetyllysine immunoprecipitation followed by mass spectrometry in HeLa cells and mouse liver mitochondria |
Molecular cell |
Medium |
16916647
|
| 2007 |
ALDOC was identified as a high-confidence Huntingtin (Htt)-interacting protein by both yeast two-hybrid screening and affinity pull-down/mass spectrometry, and its Drosophila ortholog was validated as a genetic modifier of polyglutamine-induced neurodegeneration. |
Yeast two-hybrid screening, affinity pull-down with mass spectrometry, co-immunoprecipitation from mouse brain, and Drosophila genetic modifier assay |
PLoS genetics |
High |
17500595
|
| 2008 |
ALDOC protein was detected in normal human urinary exosomes, indicating it is present in membrane vesicles secreted from renal epithelial cells. |
LC-MS/MS proteomic profiling of purified urinary exosomes |
Journal of the American Society of Nephrology : JASN |
Low |
19056867
|
| 2010 |
ALDOC was identified as a substrate of Cullin-RING ubiquitin ligases (CRLs), with its stability regulated by CRL activity, placing it in the ubiquitin-proteasome pathway. |
Quantitative proteomics (GPS and QUAINT assays) upon genetic and pharmacologic Cullin inactivation |
Cell |
Medium |
21145461 21963094
|
| 2010 |
ALDOC was identified as a ubiquitylated protein with specific diglycine-modified lysine residues mapped by mass spectrometry, confirming it as an endogenous ubiquitin substrate. |
Immunoenrichment of diglycine-modified peptides followed by high-resolution mass spectrometry (LTQ Orbitrap Velos) |
Molecular & cellular proteomics : MCP |
Medium |
21139048 21890473
|
| 2010 |
ALDOC was detected as a component of MHC class II-associated protein complexes in B-cell-derived exosomes, suggesting a role in exosome biology. |
Quantitative mass spectrometry of co-immunoprecipitated proteins from purified B-cell exosomes |
Immunology and cell biology |
Low |
20458337
|
| 2011 |
ALDOC was identified as an mRNA-binding protein in HeLa cells by interactome capture, establishing an unexpected RNA-binding function for this glycolytic enzyme. |
UV crosslinking of mRNA-protein complexes followed by oligo(dT) pulldown and mass spectrometry (interactome capture) |
Cell |
Medium |
22658674
|
| 2012 |
ALDOC was identified as a component of stable soluble human protein complexes by chromatographic co-fractionation and quantitative mass spectrometry. |
Biochemical fractionation of human cell extracts into >1,000 fractions combined with quantitative tandem mass spectrometry |
Cell |
Medium |
22939629
|
| 2012 |
ALDOC co-eluted with defined protein complexes in size-exclusion chromatography interactome mapping, providing stoichiometric information about its complex membership. |
Size-exclusion chromatography combined with quantitative SILAC proteomics |
Nature methods |
Low |
22863883
|
| 2014 |
ALDOC (zebrin II) is expressed heterogeneously in Purkinje cell subpopulations arranged in longitudinal stripes in the cerebellar cortex and marks distinct neuronal populations including cartwheel cells, inner ear sensory epithelium, and retinal cells; Aldoc-Venus knock-in mice revealed that ALDOC-positive PC axons project specifically to caudoventral cerebellar nuclei, demonstrating a functional anatomical organization linked to ALDOC expression. |
Aldoc-Venus knock-in mouse generation; fluorescence imaging, serial section alignment, climbing fiber projection analysis, co-staining with HSP25 |
PloS one |
High |
24475166
|
| 2015 |
ALDOC was identified as a protein with binary protein-protein interactions in the human interactome (HuRI/BioPlex), placing it within a network of cellular protein complexes in HEK293T cells. |
High-throughput affinity purification mass spectrometry (AP-MS) of 2,594–10,128 human proteins |
Cell / Nature |
Low |
26186194 28514442 32296183 33961781
|
| 2015 |
Disease-associated missense mutations in ALDOC perturb protein-protein interactions (edgetic effects), demonstrating that specific alleles disrupt a subset of ALDOC's interactions rather than globally destabilizing the protein. |
Systematic interaction assays (Y2H and co-immunoprecipitation) of thousands of disease-associated alleles |
Cell |
Medium |
25910212
|
| 2017 |
Proteome-wide cross-linking mass spectrometry identified structural contacts of ALDOC within macromolecular assemblies in HeLa cell lysates, providing information on its interaction interfaces. |
Chemical cross-linking followed by MS2/MS3 hybrid data acquisition and XlinkX v2.0 analysis |
Nature communications |
Low |
28524877
|
| 2018 |
NME1 (metastasis suppressor) directly binds the ALDOC promoter and activates ALDOC transcription by recruiting RNA polymerase II and promoting activating epigenetic marks (H3K4me3 and H3K27ac) at the ALDOC locus in melanoma cells. |
qRT-PCR (pre-mRNA measurement), promoter-luciferase reporter assay, chromatin immunoprecipitation (ChIP) for NME1, H3K4me3, H3K27ac, and RNA Pol II |
Anticancer research |
High |
30396920
|
| 2020 |
MUC16 C-terminal domain (MUC16c) physically interacts with ALDOC, promotes ALDOC protein stability, and disrupts ALDOC's ability to sense glucose deficiency, thereby activating the AMPK pathway and promoting gallbladder carcinoma cell proliferation and glycolysis. |
Mass spectrometry of co-immunoprecipitated proteins, immunoblotting, siRNA knockdown of ALDOC, glucose uptake and glycolysis assays, IHC |
Experimental cell research |
Medium |
32502493
|
| 2020 |
EPB41 forms a complex with ALDOC, sequestering it; loss of EPB41 releases free ALDOC, which disassembles the β-catenin destruction complex (containing GSK3β), leading to β-catenin nuclear translocation and Wnt pathway activation in NSCLC. Thus ALDOC functions as a negative regulator of the β-catenin destruction complex. |
Co-immunoprecipitation, siRNA knockdown, in vitro and in vivo NSCLC models, immunofluorescence for β-catenin localization |
Cancer letters |
Medium |
33242559
|
| 2022 |
ALDOC was identified as a component of the Tau (MAPT) interactome in human iPSC-derived neurons; its interaction with Tau was detected by APEX proximity labeling and AP-MS. |
Engineered APEX proximity labeling combined with quantitative AP-MS and proximity ligation assay (PLA) |
Cell |
Medium |
35063084
|
| 2022 |
OpenCell systematic endogenous tagging revealed ALDOC localization within human cells and its protein interaction partners at endogenous expression levels. |
CRISPR-based endogenous GFP tagging, confocal live-cell imaging, affinity purification mass spectrometry |
Science (New York, N.Y.) |
Low |
35271311
|
| 2023 |
ALDOC glycolytic activity supports anchorage-independent 3D tumor spheroid survival and growth; siRNA-mediated knockdown of ALDOC significantly reduced lactate production, cell viability, and spheroid size in lung and breast cancer cell lines, demonstrating ALDOC drives glucose metabolism toward enhanced lactate production in these contexts. |
siRNA knockdown, 3D spheroid culture, metabolomics (lactate/glucose/fructose measurement), transcriptomics, proteomics |
Journal of experimental & clinical cancer research : CR |
Medium |
36945054
|
| 2023 |
ALDOC promotes NSCLC by enhancing MYC-mediated transcription of UBE2N (ubiquitin-conjugating enzyme E2N), and this ALDOC/UBE2N axis activates the Wnt/β-catenin pathway; knockdown of UBE2N or Wnt inhibition reversed ALDOC-driven NSCLC progression. |
siRNA knockdown, Wnt pathway inhibitor treatment, in vitro and in vivo (xenograft) models, gene expression analysis |
Aging |
Medium |
37724906
|
| 2024 |
ALDOC loss in GBM promotes tumor cell invasion and migration; hypermethylation-driven loss of ALDOC expression is associated with serotonin hypersecretion and inhibition of PPAR-γ signaling. ALDOC regulates serotonin levels and protects PPAR-γ from serotonin-mediated degradation; PPAR-γ agonists restore this axis and enhance temozolomide efficacy in orthotopic GBM models. |
Methylation sequencing, omics datasets, cell and mouse orthotopic GBM models, PPAR-γ agonist treatment, survival analysis |
Cell communication and signaling : CCS |
Medium |
38741139
|
| 2024 |
ALDOC overexpression activates the AKT-mTORC1 signaling axis to promote lipid accumulation in myotubes and intramuscular adipocytes; the mTORC1 inhibitor rapamycin abrogated this proadipogenic effect, placing ALDOC upstream of AKT-mTORC1 in fat deposition. |
Transcriptome sequencing, ALDOC overexpression in vitro and in vivo (pig model), rapamycin inhibition, lipid accumulation assays |
Journal of agricultural and food chemistry |
Medium |
39428631
|
| 2025 |
HIF-1α upregulates BMAL1, which in turn increases ALDOC expression in hypoxic colorectal cancer cells; this HIF-1α/BMAL1/ALDOC cascade promotes glycolytic activity and reduces apoptosis, thereby decreasing sensitivity to oxaliplatin. |
Western blotting, qPCR, CCK-8 cell viability, flow cytometry apoptosis, lactate/ATP measurement in CRC cells under CoCl2-induced hypoxia; clinical sample correlation |
Journal of Cancer |
Medium |
40535800
|
| 2025 |
ALDOC interacts with HIF1A (HIF-1α) and enhances its transcriptional activity on the PGK1 promoter in colorectal cancer cells; dual-luciferase reporter assays and ChIP confirmed ALDOC-mediated transcriptional activation of PGK1, promoting aerobic glycolysis and CRC progression. |
Co-immunoprecipitation, dual-luciferase reporter assay, chromatin immunoprecipitation (ChIP), siRNA knockdown, xenograft in vivo models |
Molecular medicine (Cambridge, Mass.) |
Medium |
40518543
|
| 2025 |
AldoC (ALDOC) is abundantly expressed in astrocytes throughout diverse brain regions; AldoC BAC-GFP transgenic mice confirmed astrocyte identity of GFP-expressing cells, and GFP-positive astrocytes displayed characteristic linear passive conductance of mature astrocytes, validating ALDOC as an astrocyte marker with functional electrophysiological correlate. |
BAC transgenic mouse generation, confocal immunofluorescence co-labeling, whole-cell patch-clamp electrophysiology of brain slices |
Molecular brain |
High |
41339882
|