title: Amino-terminal processing of the human cannabinoid receptor 1.
abstract: The human cannabinoid receptor 1 (CB1), a G protein-coupled receptor (GPCR), translocates its long amino-terminal (N-terminal) domain across the endoplasmic reticulum (ER) membrane in a C-to-N terminal direction. Using the Semliki Forest virus (SFV) expression system, CB1 was expressed in baby hamster kidney (BHK) cells. It was found that a large fraction of the CB1 molecules were N-terminally truncated prior to ER translocation. Truncation was fast and independent of the proteasome. It is concluded that the truncation process might be a way to create a novel type of CB1.
authors.affiliation: Department of Biosciences and Nutrition at Novum, Karolinska Institute, Huddinge, Sweden.
authors.forename: Rickard
authors.initials: R
authors.lastname: Nordström
authors.forename: Helena
authors.initials: H
authors.lastname: Andersson
mesh_terms: D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism; D006224:Cricetinae; D003593:Cytoplasm / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism; D006801:Humans; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D043884:Receptor, Cannabinoid, CB1 / Q000737:chemistry* / Q000378:metabolism; D012672:Semliki forest virus / Q000378:metabolism; D014162:Transfection
chemical_list: D043884:Receptor, Cannabinoid, CB1; D046988:Proteasome Endopeptidase Complex