| 2007 |
NCU-G1 (GLMP) binds specifically to the footprint 1 element of the human cellular retinol-binding protein 1 gene promoter (shown by EMSA) and activates transcription from this promoter; it also functions as a co-activator for ligand-activated PPARα in transiently transfected Drosophila S2 cells, increasing expression of a CAT reporter under the acyl-CoA oxidase promoter. |
Electrophoretic mobility shift assay (EMSA), transient transfection reporter assays in Drosophila S2 cells |
BMC molecular biology |
Medium |
18021396
|
| 2009 |
NCU-G1 (GLMP/C1orf85) is a highly glycosylated integral lysosomal membrane protein; its lysosomal localization depends on a tyrosine-based sorting motif at position 400 in its C-terminal tail (Y→A mutation impairs lysosomal targeting), and its apparent molecular mass (~70–80 kDa) greatly exceeds calculated mass (~39 kDa) due to extensive N-glycosylation (shown by N-glycosidase F digestion). |
Immunofluorescence co-localization with LAMP-1, subcellular fractionation with density-shift assay, site-directed mutagenesis of sorting motif, N-glycosidase F digestion |
The Biochemical journal |
High |
19489740
|
| 2014 |
Disruption of Ncu-g1 (Glmp) in mice causes spontaneous liver fibrosis with increased hepatocyte death, oxidative stress, active fibrogenesis, and accumulation of lipofuscin and iron in Kupffer cells, demonstrating GLMP is required for lysosomal homeostasis in liver. |
Gene-trap knockout mouse model, histological/immunohistochemical analysis, biochemical assays for oxidative stress and fibrogenesis markers |
Disease models & mechanisms |
High |
24487409
|
| 2015 |
Loss of GLMP in mice (Glmp gt/gt) leads to metabolic dysregulation in liver: increased hepatic glucose flux, elevated de novo lipogenesis, lipid accumulation, and upregulation of genes for fatty acid uptake and lipogenesis, while blood glucose, triacylglycerol, and non-esterified fatty acids are reduced. |
Glmp knockout mouse model, primary hepatocyte metabolic flux assays, gene expression analysis |
PloS one |
Medium |
26047317
|
| 2016 |
GLMP ablation in mouse skeletal muscle myotubes shifts metabolism toward glycolysis: Glmp gt/gt myotubes show faster glucose metabolism, larger glycogen pools, and reduced oleic acid uptake, storage, and oxidation, with decreased expression of PPARα, PPARβ/δ, PPARγ, PGC1α, and lipid metabolism genes. |
Primary myotubes from Glmp knockout mice, radiotracer-based metabolic assays, gene expression analysis |
Archives of physiology and biochemistry |
Medium |
26707125
|
| 2019 |
GLMP is a critical accessory subunit of the lysosomal transporter MFSD1: MFSD1 and GLMP physically interact (co-immunoprecipitation), and each protein is required for maintenance of normal lysosomal levels of the other. Glmp knockout mice phenocopy Mfsd1 knockout mice (splenomegaly, severe liver disease), identifying a tightly linked MFSD1/GLMP lysosomal membrane protein transporter complex. |
Proteomics of isolated lysosomes from Mfsd1 knockout mice, co-immunoprecipitation, Glmp and Mfsd1 knockout mouse phenotyping |
eLife |
High |
31661432
|
| 2021 |
BRG1 transcriptionally represses GLMP expression by binding to the GLMP promoter region (shown by chromatin immunoprecipitation); BRG1 knockdown increases GLMP expression, which in turn alters the PIK3AP1/PI3K/AKT pathway and reduces lipid droplet accumulation in HCC cells, and GLMP knockdown partially restores lipid droplets and pathway changes caused by BRG1 loss. |
Chromatin immunoprecipitation (ChIP), siRNA knockdown, lipid staining (BODIPY, Oil Red O), western blot for pathway markers |
Digestive and liver disease |
Medium |
34158256
|
| 2023 |
NAT10 induces ac4C modification of GLMP mRNA, stabilizing it and increasing GLMP protein levels, which triggers activation of the MAPK/ERK signaling pathway to promote HNSCC cell metastasis. |
Gain- and loss-of-function experiments, ac4C-seq (RNA modification mapping), mRNA stability assays, in vivo mouse metastasis models |
Cell death & disease |
Medium |
37914704
|
| 2023 |
MFSD1 and GLMP each associate with GIMAP5 (identified by proteomics); GLMP and MFSD1 interactions with GIMAP5 are essential for maintaining normal GIMAP5 expression, which is required for lymphocyte survival and liver homeostasis. Germline knockout of Glmp causes lymphopenia, liver pathology, extramedullary hematopoiesis, and lipid deposition. |
ENU mutagenesis screen, proteomic analysis, germline knockout mouse models for Mfsd1, Glmp, and Gimap5, flow cytometry, histology |
Proceedings of the National Academy of Sciences of the United States of America |
High |
38055739
|
| 2024 |
MFSD1 forms a tight complex with GLMP in the lysosomal membrane and together they function as a general dipeptide uniporter: purified MFSD1 selectively binds diverse dipeptides; MFSD1-GLMP transports cationic, neutral, and anionic dipeptides as a uniporter (shown by electrophysiology, isotope tracer, and fluorescence assays in Xenopus oocytes and proteoliposomes). Cryo-EM structure of the dipeptide-bound MFSD1-GLMP complex in outward-open conformation defined the heterodimer interface and structural basis for dipeptide selectivity. |
Cryo-EM structure determination, untargeted metabolomics of MFSD1-deficient mouse lysosomes, electrophysiology in Xenopus oocytes, isotope tracer transport assays, fluorescence transport assays in proteoliposomes, molecular dynamics simulations |
Nature cell biology |
High |
38839979
|
| 2025 |
GLMP overexpression in non-small cell lung cancer cells promotes EGFR-TKI (osimertinib) resistance by regulating RhoA ubiquitination, activating the RhoA pathway to drive EMT, and activating the late stage of autophagy via lysosomal hyperactivity. |
In vitro and in vivo overexpression/knockdown models, ubiquitination assays, RhoA pathway inhibition, autophagy flux assays |
NPJ precision oncology |
Medium |
41298761
|