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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Nie YW,Wang M,Zhang P,Huan L,Liu DJdoi
10.1016/j.bbrc.2016.03.087subject
Has Abstractpub_date
2016-04-22 00:00:00pages
249-254issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(16)30398-9journal_volume
473pub_type
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