| 2023 |
TMEM25 physically associates with monomeric EGFR and suppresses ligand-independent EGFR monomer-mediated phosphorylation of STAT3 at basal state; loss of TMEM25 allows monomeric EGFR to phosphorylate STAT3 independently of ligand binding, enhancing basal STAT3 activation and promoting TNBC progression. AAV-mediated TMEM25 restoration suppressed STAT3 activation in vivo. |
Co-immunoprecipitation, loss-of-function (TMEM25-KO cells and mice), AAV overexpression rescue, phospho-STAT3 immunoblotting, electrophysiology |
Nature Communications |
High |
37095176
|
| 2019 |
TMEM25 localizes to late endosomes in neurons, physically interacts with the NMDA receptor NR2B subunit (co-localized to late endosome compartments), induces acidification changes in lysosome compartments, and accelerates lysosomal degradation of NR2B, thereby modulating neuronal excitability. TMEM25 overexpression attenuated epileptic seizure phenotypes while knockdown exacerbated them. |
Subcellular fractionation/immunofluorescence co-localization to late endosomes, Co-immunoprecipitation (TMEM25–NR2B interaction), lysosomal pH assays, Western blot for NR2B protein levels, electrophysiology, in vivo KD/OE in epilepsy mouse models |
The Journal of Clinical Investigation |
High |
31424425
|
| 2023 |
TMEM25 localizes to tight junctions in epithelial cells and binds Par3 via a PDZ-mediated interaction with its C-terminal cytoplasmic tail. Via its N-terminal extracellular domain, TMEM25 associates with claudin-1 and claudin-2 and suppresses their cis- and trans-oligomerizations, thereby attenuating tight junction strand formation. Par3 binding to TMEM25 attenuates TMEM25–claudin association, modulating claudin oligomerization. Depletion of TMEM25 accelerates TJ development, while overexpression (but not C-terminally deleted mutant) delays it. |
Immunofluorescence localization to tight junctions, Co-immunoprecipitation (TMEM25–Par3 and TMEM25–claudin-1/2), domain deletion mutagenesis (C-terminal and N-terminal truncations), siRNA knockdown and overexpression with TJ assembly kinetics assay, claudin oligomerization assays |
EMBO Reports |
High |
38177906
|
| 2023 |
TMEM25 overexpression in mouse ventricular cortical progenitors promoted proliferation of basal radial glia (bRG) and increased upper-layer neuron numbers in vivo. Knockdown of TMEM25 in human neural progenitor cells inhibited cell cycle progression via repression of Akt signaling, suggesting TMEM25 receives extracellular signals to promote NPC expansion through an Akt-dependent pathway. |
In vitro NPC proliferation assays (overexpression), in vivo mouse cortical electroporation (bRG expansion, upper-layer neuron counting), TMEM25 knockdown in human NPCs with RNA-seq and pharmacological Akt pathway assays |
FEBS Letters |
Medium |
37846797
|
| 2013 |
CpG island hypermethylation of TMEM25 is inversely correlated with reduced TMEM25 expression in colorectal cancer tissue, demonstrating that epigenetic silencing via DNA methylation is a mechanism of TMEM25 downregulation in cancer. |
Whole-genome methylation scan, methylation-specific high-resolution melting analysis (133 CRC samples), expression quantification by RT-PCR, correlation analysis of methylation vs. expression |
Disease Markers |
Medium |
23324576
|
| 2004 |
TMEM25 was identified as a member of the immunoglobulin superfamily containing a C-2 type immunoglobulin domain (codons 42–112). The gene encodes two isoforms by alternative exon skipping: isoform 1 (366 aa, transmembrane) and isoform 2 (322 aa, secreted). Human TMEM25 shares 91% amino acid identity with mouse Tmem25. |
In silico bioinformatics analysis of cDNA sequences (BC042896, AY358919, AK002841), domain homology prediction |
Oncology Reports |
Low |
15254712
|