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gp78 plays a critical role in protecting against ER stress in liver
Gp78, an E3 ubiquitin ligase (show MUL1 Proteins) acts as a gatekeeper suppressing nonalcoholic steatohepatitis (NASH (show SAMSN1 Proteins)) and liver cancer.
The ubiquitin ligase (show RNF123 Proteins) gp78, known for its role in protein quality control, is critical for unglycosylated PrP ubiquitylation and degradation.
we consistently observe involvement of gp78 in Insig-1 degradation, we find no substantive evidence to support roles for either gp78 or TRC8 (show RNF139 Proteins) in the robust sterol-accelerated degradation of HMG-CoA reductase (show HMGCR Proteins)
Ablation of gp78 in liver improves hyperlipidemia and insulin (show INS Proteins) resistance by inhibiting SREBP to decrease lipid biosynthesis.
Palmitoylation of RING finger (show PCGF1 Proteins) cysteines therefore regulates gp78 distribution to the peripheral ER
AMFR is involved in the process of learning and memory in the central nervous system.
KAI1 has a role in promotion of cell proliferation and mammary gland hyperplasia by the gp78 ubiquitin ligase
Gp78 promotes SOD1 (show SOD1 Proteins) and ataxin-3 (show ATXN3 Proteins) degradation in endoplasmic reticulum.
cytoplasmic protein (show BLZF1 Proteins) mouse p97 (show EIF4G2 Proteins)(mp97) participates in the formation of a ternary complex containing mouse autocrine motility factor receptor (mAMFR), mp97, and peptide N-glycanase
the receptor molecule for AMF/NLK/MF in leukemic differentiation is not gp78
overexpression of gp78 or SVIP (show SVIP Proteins) suppression may eliminate the toxic gain of function associated with polymerization of ZAAT, thus providing a potential new therapeutic approach to the treatment of alpha-1 antitrypsin (show SERPINA1 Proteins) deficiency
Despite its interaction with gp78, Lnp does not seem to have a broad function in degradation of misfolded ER proteins.
Further study discovered that the gp78 CUE domain works as a proofreading machine during the growth of K48-linked polyubiquitin (show UBB Proteins) chains to ensure the linkage specificity. Together, our studies uncover a novel mechanism underlying the linkage specificity determination of longer polyubiquitin (show UBB Proteins) chains.
AMFR expression is significantly reduced in plasma from osteoporosis patients.
Catalytic inactivation of MGRN1 (show MGRN1 Proteins) results in elevated levels of GP78 and a consequential increase in the initiation of mitophagy.
Authors conclude that the Hrd1 (show SYVN1 Proteins) complex forms an essential retrotranslocation module that is evolutionarily conserved, but the mammalian ERAD system uses additional ubiquitin ligases to assist Hrd1 (show SYVN1 Proteins) during retrotranslocation.
Downregulation of AMFR induced cell cycle arrest at the G0/G1 phase, and increased apoptosis of the THP1 cells.
The authors identify USP13 (show USP13 Proteins) as a gp78-associated deubiquitinase that eliminates ubiquitin conjugates from Ubl4A (show UBL4A Proteins) to maintain the functionality of Bag6 (show BAT3 Proteins).
Data show that autocrine motility factor receptor (AMFR) and NOTCH1 (show NOTCH1 Proteins) protein are the direct target genes of microRNA miR (show MLXIP Proteins)-139-5p in colorectal cancer (CRC (show CALR Proteins)).
gp78 elongates polyubiquitin chains from the distal end through the cooperation of its G2BR and CUE domains.
This locus encodes a glycosylated transmembrane receptor. Its ligand, autocrine motility factor, is a tumor motility-stimulating protein secreted by tumor cells. The encoded receptor is also a member of the E3 ubiquitin ligase family of proteins. It catalyzes ubiquitination and endoplasmic reticulum-associated degradation of specific proteins.
autocrine motility factor receptor
, autocrine motility factor receptor, amfr
, autocrine motility factor receptor amfr
, autocrine motility factor receptor, isoform 2-like
, AMF receptor
, E3 ubiquitin-protein ligase AMFR
, RING finger protein 45