title: Identification and characterization of an endoplasmic reticulum localization motif.
abstract: Sorting motifs are involved in the transport of diverse proteins. In the present study, we identified a hydrophobic peptide (WRPWRNFWWSIRVPWRRN) that was able to target enhanced green fluorescent protein- or DsRed2-enriched vesicular-like sub-compartments of the endoplasmic reticulum (ER). Analysis of mutation constructs revealed that the sequence WRPWRNFWW was responsible for the ER-targeting activity, and the arginine residue of the peptide is a critical determinant of ER localization. Results from co-immunoprecipitation, glutathione S-transferase pull-down, liquid chromatography-tandem mass spectrometry, and western blotting analyses demonstrated that this motif could bind with the γ2-COP subcomplex of coat protein complex I (COPI), which is involved in the retrieval and transport of ER-resident proteins from the Golgi apparatus to the ER. Overall, we report a new hydrophobic peptide that possesses an arginine-based ER localization motif, which can help elucidate the mechanisms of ER sorting mediated by COPI.
authors.affiliation: The Key Laboratory of China Education Ministry for Research of Mammal Reproductive Biology and Biotechnology, Inner Mongolia University, Hohhot, PR China.
authors.forename: Yong-Wei
authors.initials: YW
authors.lastname: Nie
authors.affiliation: The Key Laboratory of China Education Ministry for Research of Mammal Reproductive Biology and Biotechnology, Inner Mongolia University, Hohhot, PR China.
authors.forename: Meng
authors.initials: M
authors.lastname: Wang
authors.affiliation: The Key Laboratory of China Education Ministry for Research of Mammal Reproductive Biology and Biotechnology, Inner Mongolia University, Hohhot, PR China.
authors.forename: Ping
authors.initials: P
authors.lastname: Zhang
authors.affiliation: The Key Laboratory of China Education Ministry for Research of Mammal Reproductive Biology and Biotechnology, Inner Mongolia University, Hohhot, PR China.
authors.forename: Lei
authors.initials: L
authors.lastname: Huan
authors.affiliation: The Key Laboratory of China Education Ministry for Research of Mammal Reproductive Biology and Biotechnology, Inner Mongolia University, Hohhot, PR China. Electronic address: nmliudongjun@sina.com.
authors.forename: Dong-Jun
authors.initials: DJ
authors.lastname: Liu
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001120:Arginine / Q000737:chemistry; D002853:Chromatography, Liquid; D020755:Coat Protein Complex I / Q000737:chemistry; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006056:Golgi Apparatus / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D047468:Immunoprecipitation; D008856:Microscopy, Fluorescence; D008969:Molecular Sequence Data; D009154:Mutation; D010455:Peptides / Q000737:chemistry; D010957:Plasmids / Q000378:metabolism; D053719:Tandem Mass Spectrometry
chemical_list: D020755:Coat Protein Complex I; D010455:Peptides; D001120:Arginine
keywords: Arginine-Based ER localization motifs; Coatomer subunit gamma-2 (γ2-COP); Endoplasmic reticulum localization