Derlin-1 also known as degradation in endoplasmic reticulum protein 1 is a protein that in humans is encoded by the DERL1gene.[1][2][3] It is a member of the rhomboid-like clan of polytopic membrane proteins.
Derlin-1 is part of a complex (that includes VIMP, SEL1, HRD1, and HERP) that mediates endoplasmic-reticulum-associated degradation (ERAD) that detects misfolded proteins in the endoplasmic reticulum and targets them for destruction.[4]
Clinical significance
Derlin 1 (DERL1) is up-regulated in metastatic canine mammary tumors as part of the unfolded protein response.[5][6][7]
↑Lilley BN, Ploegh HL (Jun 2004). "A membrane protein required for dislocation of misfolded proteins from the ER". Nature. 429 (6994): 834–40. doi:10.1038/nature02592. PMID15215855.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
Ye Y, Shibata Y, Yun C, et al. (2004). "A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol". Nature. 429 (6994): 841–7. doi:10.1038/nature02656. PMID15215856.
Schulze A, Standera S, Buerger E, et al. (2006). "The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway". J. Mol. Biol. 354 (5): 1021–7. doi:10.1016/j.jmb.2005.10.020. PMID16289116.
Sun F, Zhang R, Gong X, et al. (2007). "Derlin-1 promotes the efficient degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and CFTR folding mutants". J. Biol. Chem. 281 (48): 36856–63. doi:10.1074/jbc.M607085200. PMID16954204.
Crawshaw SG, Cross BC, Wilson CM, High S (2007). "The oligomeric state of Derlin-1 is modulated by endoplasmic reticulum stress". Mol. Membr. Biol. 24 (2): 113–20. doi:10.1080/09687860600988727. PMID17453418.