Lysosomal integral membrane protein LGP85 (LIMP-2) is ubiquitinated at the N-terminal cytoplasmic domain
Author:
Funder
Japan Society for the Promotion of Science KAKENHI
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference32 articles.
1. Biosynthesis, glycosylation, movement through the Golgi system, and transport to lysosomes by an N-linked carbohydrate-independent mechanism of three lysosomal integral membrane proteins;Barriocanal;J. Biol. Chem.,1986
2. Purification and characterization of an 85 kDa sialoglycoprotein in rat liver lysosomal membranes;Okazaki;J. Biochem.,1992
3. Cloning, sequencing, and expression of a cDNA encoding rat LIMP II, a novel 74-kDa lysosomal membrane protein related to the surface adhesion protein CD36;Vega;J. Biol. Chem.,1991
4. Isolation and sequencing of a cDNA clone encoding 85kDa sialoglycoprotein in rat liver lysosomal membranes;Fujita;Biochem. Biophys. Res. Commun.,1991
5. Array-based gene discovery with three unrelated subjects shows SCARB2/LIMP-2 deficiency causes myoclonus epilepsy and glomerulosclerosis;Berkovic;Am. J. Hum. Genet.,2008
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1. HM1.24/BST-2 is constitutively poly-ubiquitinated at the N-terminal amino acid in the cytoplasmic domain;Biochemistry and Biophysics Reports;2020-09
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