| 2010 |
Crystal structure of the C-terminal fragment of Vps53 (at 2.9 Å resolution) revealed two alpha-helical bundles arranged in tandem with a highly conserved surface patch. Mutagenesis of this surface patch caused defects in membrane traffic, identifying this region as functionally critical for vesicle recognition in endosome-to-TGN retrograde transport. |
X-ray crystallography (2.9 Å) combined with site-directed mutagenesis and membrane traffic functional assay |
Proceedings of the National Academy of Sciences of the United States of America |
High |
20660722
|
| 2010 |
The fold of the Vps53 C-terminal domain is structurally reminiscent of subunits from three other tethering complexes (Dsl1, conserved oligomeric Golgi, and the exocyst), indicating that GARP belongs to the same evolutionary family of membrane-tethering complexes. |
Structural comparison via X-ray crystallography |
Proceedings of the National Academy of Sciences of the United States of America |
High |
20660722
|
| 2014 |
Loss-of-function compound heterozygous mutations in VPS53 (c.2084A>G and c.1556+5G>A) affecting its C-terminal domain cause abnormal accumulation of swollen CD63-positive vesicular bodies (likely intermediate recycling/late endosomes) in patient fibroblasts, establishing VPS53 as essential for retrograde endosome-to-Golgi vesicle recycling in human cells. |
Immunofluorescence microscopy of patient fibroblasts with CD63 marker; whole exome sequencing and linkage analysis |
Journal of medical genetics |
Medium |
24577744
|
| 2014 |
VPS53 functions as a subunit of the Golgi-associated retrograde protein (GARP) complex, which mediates retrograde transport of endocytic vesicles to the trans-Golgi network; the C-terminal domain of VPS53 is critical for this function. |
Genetic mapping, whole exome sequencing, and immunofluorescence microscopy in patient-derived fibroblasts |
Journal of medical genetics |
Medium |
24577744
|
| 2019 |
A homozygous VPS53 missense variant (c.2084A>G, p.Gln695Arg) was identified as causative in complicated hereditary spastic paraparesis, placing VPS53/GARP function in intracellular cholesterol transport and sphingolipid homeostasis in lysosomes as relevant to neurodegeneration. |
Whole exome sequencing with family-based genetic analysis |
Neurogenetics |
Low |
31418091
|
| 2020 |
Overexpression of VPS53 in colorectal cancer cells upregulated Beclin 1 and LC3B-II and induced autophagy; pharmacological inhibition of autophagy attenuated the VPS53-mediated suppression of cancer cell proliferation, migration, and invasion, placing VPS53 upstream of the autophagy pathway in CRC cells. |
Overexpression with CCK-8, flow cytometry, transwell assay, electron microscopy, and Western blotting; autophagy inhibitor rescue experiment |
OncoTargets and therapy |
Low |
33116643
|
| 2018 |
Treatment with GZFLW increased VPS53 protein stability (not mRNA level) in endometrial stromal cells, suggesting VPS53 is subject to post-translational regulation of protein stability, and elevated VPS53 promoted apoptosis in these cells. |
iTRAQ proteomics, LC-MS/MS, and Western blotting in human endometrial stromal cells |
Evidence-based complementary and alternative medicine : eCAM |
Low |
30643524
|