GGA2 Antibody

1. Study shows that reduced expression of GGA3 resultes in accumulation of endocytosed EGFR within enlarged endosomes. GGA2 interacts with EGFR cytoplasmic domain to stabilize the receptor expression and promote cell growth. Finally, GGA2 was upregulated in 30.8% of human hepatocellular carcinomas and 23.3% of colorectal cancers. PMID:29358589
2. PI4KIIIbeta interaction with the VHS domain of GGA2 affected PI4KIIIbeta localization. PMID:28289207
3. 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. PMID:27901063
4. 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. PMID:24407285
5. GGA2 mediates a vital function that cannot be compensated for by GGA1and/or GGA3. PMID:22291915
6. endocytosis and intracellular transport of memapsin 2, mediated by its cytosolic domain, may involve the binding of GGA1 and GGA2 PMID:12135764
7. GGA proteins function with the phosphorylated ACDL in the memasin 2-recycling pathway from endosomes to trans Golgi on the way back to the cell surface. PMID:15615712
8. Results demonstrate that cargo proteins contribute to the recruitment of GGA2 onto membranes and to the formation of GGA-positive clathrin-coated vesicles. PMID:17451558
9. These results show that the dual roles of PI4P can promote specific GGA targeting and cargo recognition at the trans-Golgi network. PMID:17494868
10. p56 tightly cooperates with the GGAs in the sorting of cathepsin D to lysosomes, probably by enabling the movement of GGA-containing transport carriers. PMID:17596511
11. GGA2 is recruited to the trans-Golgi network independently of the other Golgi-localized, gamma-ear-containing, ARF-binding proteins and is required for the efficient sorting of lysosomal enzymes PMID:18431031
12. GGA overexpression causes various sorting defects as measured by recycling of CD-MPR, internalization of transferrin receptor, and the subcellular localization of proteins like Tsg101, ubiquitin, and Hrs. PMID:19788741

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HGNC: 16064

UNIGENE: Hs.460336

KEGG: hsa:23062

STRING: 9606.ENSP00000311962

OMIM: 606005