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The C‐degron pathway eliminates mislocalized proteins and products of deubiquitinating enzymes
Author(s) -
Yeh ChiWei,
Huang WeiChieh,
Hsu PangHung,
Yeh KunHai,
Wang LiChin,
Hsu Paul WeiChe,
Lin HsiuChuan,
Chen YiNing,
Chen ShuChuan,
Yeang ChenHsiang,
Yen HsuehChi S
Publication year - 2021
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.15252/embj.2020105846
Subject(s) - degron , deubiquitinating enzyme , biology , proteome , ubiquitin , proteolysis , microbiology and biotechnology , protein degradation , biochemistry , enzyme , ubiquitin ligase , gene
Protein termini are determinants of protein stability. Proteins bearing degradation signals, or degrons, at their amino‐ or carboxyl‐termini are eliminated by the N‐ or C‐degron pathways, respectively. We aimed to elucidate the function of C‐degron pathways and to unveil how normal proteomes are exempt from C‐degron pathway‐mediated destruction. Our data reveal that C‐degron pathways remove mislocalized cellular proteins and cleavage products of deubiquitinating enzymes. Furthermore, the C‐degron and N‐degron pathways cooperate in protein removal. Proteome analysis revealed a shortfall in normal proteins targeted by C‐degron pathways, but not of defective proteins, suggesting proteolysis‐based immunity as a constraint for protein evolution/selection. Our work highlights the importance of protein termini for protein quality surveillance, and the relationship between the functional proteome and protein degradation pathways.