| 2007 |
TMEM192 (encoded by LOC201931/FLJ38482) was identified as an integral lysosomal membrane protein; fusion protein constructs expressed in HeLa cells localized to lysosomal organelles, establishing lysosomal membrane residence. |
Organellar proteomics of placental lysosomal membranes; fluorescent tag fusion protein expression in HeLa cells with colocalization |
Traffic (Copenhagen, Denmark) |
Medium |
17897319
|
| 2010 |
TMEM192 localizes to lysosomal/late endosomal membranes (confirmed for both overexpressed and endogenous protein), lacks N-glycosylation, and forms homodimers linked by interchain disulfide bridges, as demonstrated by co-immunoprecipitation and comparison of reduced vs. non-reduced western blots. |
Anti-TMEM192 antibody generation; Percoll density gradient centrifugation/immunoblotting; co-immunoprecipitation; reduced vs. non-reduced SDS-PAGE; immunofluorescence colocalization with LAMP-2 and cathepsin D |
Biological chemistry |
High |
20370317
|
| 2011 |
Two adjacent N-terminal dileucine motifs (DXXLL-type) are required for TMEM192 targeting to late endosomes/lysosomes; disruption of both motifs misdirects TMEM192 to the plasma membrane, while each single motif is sufficient for correct targeting. Cys266 in the C-terminal cytosolic tail is responsible for intermolecular disulfide bond formation in TMEM192 homodimers; mutation of Cys266 abolishes dimer formation. Immunogold labeling and proteinase protection assays confirmed that both N- and C-termini face the cytosol. |
CD4 chimeric construct mutagenesis; site-directed mutagenesis of dileucine motifs and cysteine residues; immunogold electron microscopy; proteinase protection assay; immunofluorescence |
The Biochemical journal |
High |
21143193
|
| 2016 |
TMEM192 physically interacts with TIG1 (tazarotene-induced gene 1) isoforms A and B, as identified by yeast two-hybrid and confirmed by colocalization in HtTA cervical cancer cells. Silencing of TMEM192 reduced TIG1-mediated upregulation of autophagy (Beclin-1, LC-3B), placing TMEM192 downstream of TIG1 in autophagy induction. |
Yeast two-hybrid; co-immunoprecipitation/colocalization; siRNA knockdown with autophagy marker readout (Beclin-1, LC-3B) |
Molecules and cells |
Medium |
27989102
|
| 2012 |
Knockdown of TMEM192 in HepG2 hepatoma cells induces autophagy (elevated LC3-II) and subsequent apoptosis via the mitochondrial pathway; blocking Atg7 expression in TMEM192-deficient cells inhibits the increased apoptosis, establishing that TMEM192 loss-induced apoptosis is autophagy-dependent. |
siRNA knockdown; immunoblotting for LC3-II; Atg7 siRNA epistasis; apoptosis assays |
Oncology reports |
Medium |
22736246
|
| 2017 |
TMEM192 is ubiquitinated by the SCF(FBXO27) ubiquitin ligase complex upon lysosomal damage; FBXO27 overexpression increases TMEM192 ubiquitination, implicating TMEM192 as a substrate of SCFFBXO27-mediated lysophagy signaling. |
Ubiquitination screen upon lysosomal damage; FBXO27 overexpression with ubiquitination assay; mass spectrometry identification |
Proceedings of the National Academy of Sciences of the United States of America |
Medium |
28743755
|
| 2017 |
In TMEM192-knockout mice, lysosomal morphology, autophagy, and lysosomal exocytosis in MEFs were normal under basal conditions. Murine TMEM192 undergoes proteolytic processing by pH-dependent lysosomal proteases to generate a 17 kDa fragment in a tissue-specific manner (absent in liver). These findings indicate that TMEM192 loss can be compensated in vivo under basal conditions. |
TMEM192 knockout mouse generation; histopathological, ultrastructural (EM), and biochemical analyses; lysosomal exocytosis assay; pH-dependent protease inhibition experiments |
Oncotarget |
Medium |
28504966
|
| 2019 |
3xHA-tagged TMEM192 expressed in cells enables high-efficiency immunoprecipitation-based lysosome enrichment (up to 118-fold enrichment for certain lysosomal proteins vs. whole cell lysate), outperforming centrifugation and sucrose gradient methods; this established TMEM192 as a reliable integral lysosomal membrane anchor for organelle isolation (LysoIP/TMEM-IP methodology). |
Comparative lysosome enrichment by immunoprecipitation of 3xHA-TMEM192 vs. SPIONs, centrifugation, and sucrose gradient; data-independent acquisition proteomics |
Journal of proteome research |
Medium |
31738065
|
| 2024 |
Super-resolution DNA-PAINT imaging of individual late endosomes/lysosomes (LELs) showed that TMEM192 marks a specific LEL subpopulation rather than being uniformly distributed across all LELs, revealing organelle heterogeneity at single-LEL resolution. |
Multiplexed quantitative DNA-PAINT super-resolution imaging of seven LEL membrane proteins on individual organelles |
The Journal of cell biology |
Medium |
39485275
|
| 2024 |
Tagless LysoIP using an antibody against endogenous TMEM192 enables rapid immunoprecipitation of intact lysosomes from primary clinical samples (PBMCs from blood) and iPSC-derived neurons without requiring transgenic tag expression; isolated lysosomes were intact and suitable for multimodal omics analyses. |
Immunoprecipitation of endogenous TMEM192 from clinical blood samples and iPSC neurons; lysosomal integrity assessment; metabolomic and proteomic profiling |
The Journal of clinical investigation |
Medium |
39724071
|
| 2025 |
TBK1-dependent phosphorylation of FBXO3 facilitates FBXO3 interaction with TMEM192, promoting TMEM192 ubiquitination, which is then recognized by the autophagy receptor TAX1BP1 to drive lysophagic flux. Disruption of this TBK1-SCFFBXO3-TMEM192-TAX1BP1 axis significantly reduces lysophagy and causes accumulation of damaged lysosomes. |
Genetic and biochemical perturbation of TBK1, FBXO3, TMEM192, and TAX1BP1; lysophagy flux assays; co-immunoprecipitation; ubiquitination assays |
Autophagy |
Medium |
40083080
|