A conserved island of BAG 6/Scythe is related to ubiquitin domains and participates in short hydrophobicity recognition

BAG 6 (also called Scythe) interacts with the exposed hydrophobic regions of newly synthesized proteins and escorts them to the degradation machinery through mechanisms that remain to be elucidated. In this study, we provide evidence that BAG 6 physically interacts with the model defective protein s...

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Bibliographic Details
Published in:The FEBS journal 2016-02, Vol.283 (4), p.662-677
Main Authors: Tanaka, Hirofumi, Takahashi, Toshiki, Xie, Yiming, Minami, Ryosuke, Yanagi, Yuko, Hayashishita, Mizuki, Suzuki, Rigel, Yokota, Naoto, Shimada, Masumi, Mizushima, Tsunehiro, Kuwabara, Naoyuki, Kato, Ryuichi, Kawahara, Hiroyuki
Format: Article
Language:English
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Summary:BAG 6 (also called Scythe) interacts with the exposed hydrophobic regions of newly synthesized proteins and escorts them to the degradation machinery through mechanisms that remain to be elucidated. In this study, we provide evidence that BAG 6 physically interacts with the model defective protein substrate CL 1 in a manner that depends directly on its short hydrophobicity. We found that the N terminus of BAG 6 contains an evolutionarily conserved island tentatively designated the BAG 6 ubiquitin‐linked domain. Partial deletion of this domain in the BAG 6 N‐terminal fragment abolished in cell recognition of polyubiquitinated polypeptides as well as the hydrophobicity‐mediated recognition of the CL 1 degron in cell and in vitro . These observations suggest a mechanism whereby the BAG 6 ubiquitin‐linked domain provides a platform for discriminating substrates with shorter hydrophobicity stretches as a signal for defective proteins.
ISSN:1742-464X
1742-4658
DOI:10.1111/febs.13618