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

Nie YW,Wang M,Zhang P,Huan L,Liu DJ

doi

10.1016/j.bbrc.2016.03.087

subject

Has Abstract

pub_date

2016-04-22 00:00:00

pages

249-254

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(16)30398-9

journal_volume

473

pub_type

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