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Title 

Amino-terminal arginylation as a degradation signal for selective autophagy

Authors 

Hyunjoo Cha-MolstadY T KwonBo Yeon Kim

Publisher 

Korean Society for Biochemistry and Molecular Biology

Issue Date 

2015

Citation 

BMB Reports, vol. 48, no. 9, pp. 487-488

Keywords 

ATE1Autophagyp62

Abstract 

The ubiquitin-proteasome system and the autophagy lysosome system are the two major protein degradation machineries in eukaryotic cells. These two systems coordinate the removal of unwanted intracellular materials, but the mechanism by which they achieve this synchronization is largely unknown. The ubiquitination of substrates serves as a universal degradation signal for both systems. Our study revealed that the amino-terminal Arg, a canonical N-degron in the ubiquitin-proteasome system, also acts as a degradation signal in autophagy. We showed that many ER residents, such as BiP, contain evolutionally conserved arginylation permissive pro-N-degrons, and that certain inducers like dsDNA or proteasome inhibitors cause their translocation into the cytoplasm where they bind misfolded proteins and undergo amino-terminal arginylation by arginyl transferase 1 (ATE1). The amino-terminal Arg of BiP binds p62, which triggers p62 oligomerization and enhances p62-LC3 interaction, thereby stimulating autophagic delivery and degradation of misfolded proteins, promoting cell survival. This study reveals a novel ubiquitin-independent mechanism for the selective autophagy pathway, and provides an insight into how these two major protein degradation pathways communicate in cells to dispose the unwanted proteins.

ISSN 

1225-8687

Link 

http://dx.doi.org/10.5483/BMBRep.2015.48.9.176

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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