Cell Reports, 2022 Summary: The accumulation of misfolded proteins in the endoplasmic reticulum (ER) induces the unfolded protein response (UPR), which acts through various mechanisms to reduce ER stress.
Yi-Hsun Wang +9 more
doaj +4 more sources
Mesenchymal stem cells inhibit T cell activation by releasing TGF-β1 from TGF-β1/GARP complex. [PDF]
Oncotarget, 2017 Intervention with mesenchymal stem cells (MSCs) reveals a promising therapeutic tool to treat transplantation and autoimmune disease due to their immunoregulation capability. But the mechanisms of action are not fully investigated yet.
Niu J, Yue W, Le-Le Z, Bin L, Hu X.
europepmc +5 more sources
The GARP Complex Is Involved in Intracellular Cholesterol Transport via Targeting NPC2 to Lysosomes [PDF]
Cell Reports, 2017 Proper intracellular cholesterol trafficking is critical for cellular function. Two lysosome-resident proteins, NPC1 and NPC2, mediate the egress of low-density lipoprotein-derived cholesterol from lysosomes.
Jian Wei +10 more
doaj +4 more sources
Hepatic Stellate Cells Inhibit T Cells through Active TGF-β1 from a Cell Surface-Bound Latent TGF-β1/GARP Complex. [PDF]
J Immunol, 2015 Abstract Hepatic stellate cells (HSCs) inhibit T cells, a process that could help the liver to maintain its immunoprivileged status. HSCs secrete latent TGF-β1, but the detailed mechanisms by which latent TGF-β1 is activated and whether it plays any role in HSC-mediated T cell suppression remain unclear.
Li Y +6 more
europepmc +5 more sources
A systematic approach to identify recycling endocytic cargo depending on the GARP complex [PDF]
eLife, 2019 Proteins and lipids of the plasma membrane underlie constant remodeling via a combination of the secretory- and the endocytic pathway. In the yeast endocytic pathway, cargo is sorted for recycling to the plasma membrane or degradation in vacuoles ...
Sebastian Eising +2 more
doaj +2 more sources
Release of active TGF-β1 from the latent TGF-β1/GARP complex on T regulatory cells is mediated by integrin β8. [PDF]
J Immunol, 2014 Abstract Activated T regulatory cells (Tregs) express latent TGF-β1 on their cell surface bound to GARP. Although integrins have been implicated in mediating the release of active TGF-β1 from the complex of latent TGF-β1 and latent TGF-β1 binding protein, their role in processing latent TGF-β1 from the latent TGF-β1/GARP complex is ...
Edwards JP, Thornton AM, Shevach EM.
europepmc +5 more sources
Role of GARP Vesicle Tethering Complex in Golgi Physiology
International Journal of Molecular Sciences, 2023 The Golgi associated retrograde protein complex (GARP) is an evolutionarily conserved component of Golgi membrane trafficking machinery that belongs to the Complexes Associated with Tethering Containing Helical Rods (CATCHR) family.
Amrita Khakurel, Vladimir V. Lupashin
semanticscholar +3 more sources
GARP complex controls Golgi physiology by stabilizing COPI machinery and Golgi v-SNAREs
bioRxiv, 2022 GARP is an evolutionary conserved heterotetrameric protein complex that is thought to tether endosome-derived vesicles and promotes their fusion in the trans-Golgi network.
Amrita Khakurel +4 more
semanticscholar +2 more sources
A systematic approach to identify recycling endocytic cargo depending on the GARP complex
eLife, 2018 Proteins and lipids of the plasma membrane underlie constant remodeling via a combination of the secretory- and the endocytic pathway. In the yeast endocytic pathway, cargo is sorted for recycling to the plasma membrane or degradation in vacuoles.
Sebastian Eising +2 more
semanticscholar +4 more sources
Loss of the GARP but not EARP protein complex drives Golgi sterol overload during dendrite remodeling [PDF]
Human Molecular Genetics, 2021 Membrane trafficking is essential for sculpting neuronal morphology. The GARP and EARP complexes are conserved tethers that regulate vesicle trafficking in the secretory and endolysosomal pathways, respectively.
C. O’BRIEN +3 more
semanticscholar +7 more sources