-
The adaptor, GGA1, and retromer are essential to mediate rapid trafficking of phosphorylated BACE1 to recycling endosomes. Therefore, post-translational phosphorylation of DISLL enhances the exit of BACE1 from early endosomes, a pathway mediated by GGA1 and retromer, which is important in regulating amyloid beta production.
-
full length alpha2B-AR associated with GGA2 but not GGA1, its third intracellular loop was found to directly interact with both GGA1 and GGA2. More interestingly, further mapping of interaction domains showed that the GGA1 hinge region and the GGA2 GAE domain bound to multiple subdomains of the loop.
-
These findings show that the AD-like phenotype of NPC model cells can be partly reverted by promoting a non-amyloidogenic processing of APP through the upregulation of GGA1 supporting its preventive role against AD
-
These data indicate that clathrin is required for the function of AP-1- and GGA-coated carriers at the trans-Golgi network but may be dispensable for outward traffic en route to the plasma membrane.
-
On basis of these results, propose that GGA1 facilitates LR11 endocytic traffic and that LR11 modulates A-beta levels by promoting amyloid-beta precursor protein traffic to the endocytic recycling compartment
-
X-ray structure of the GGA1 VHS domain alone, and in complex with the carboxy-terminal peptide of cation-independent mannose 6-phosphate receptor containing an ACLL sequence
-
endocytosis and intracellular transport of memapsin 2, mediated by its cytosolic domain, may involve the binding of GGA1 and GGA2
-
The 2.4-A crystal structure of the GAT domain of human GGA1 reveals a three-helix bundle, with a long N-terminal helical extension that is not conserved in GAT domains that do not bind ARF.
-
X-ray crystal structures of the human GGA1-GAT domain and the complex between ARF1-GTP and the N-terminal region of the GAT domain
-
Crystal structure of the human GGA1 GAT domain
-
A hydrophobic surface patch on the C-terminal three-helix bundle motif of the GGA1 GAT domain is directly involved in binding with a coiled-coil region of rabaptin-5.
-
GGA1 interacts with the adaptor protein AP-1 through a WNSF sequence in its hinge region
-
Rabaptin-5, ubiquitin, and TSG101 bind to overlapping but distinct binding sites on the trihelical bundle subdomain of GGA-1 protein
-
serine phosphorylation of BACE is a physiologically relevant post-translational modification that regulates trafficking in the juxtanuclear compartment by interaction with GGA1
-
GGA proteins funstion with the phosphorylated ACDL in the memasin 2-recycling pathway from endosomes to trans Golgi on the way back to the cell surface.
-
Our data indicate that GGA proteins are not only involved in the sorting at the TGN but also mediate the retrograde transport of cargo proteins from endosomes to the TGN.
-
the trafficking of adiponectin through its secretory pathway is dependent on GGA-coated vesicles
-
GGA1 prevented APP beta-cleavage products from becoming substrates for gamma-secretase. Direct binding of GGA1 to BACE was not required for these effects, but the integrity of the GAT (GGA1 and TOM) domain of GGA1 was.
-
GGA1 alters the proteolytic processing of beta-amyloid precursor protein (APP) and the secretion of APPs and amyloid-beta, suggesting a role of GGA1 in Alzheimer's disease pathogenesis.
-
These results show that the dual roles of PI4P can promote specific GGA targeting and cargo recognition at the trans-Golgi network.