Clearance of yeast prions by misfolded multi-transmembrane proteins

Chie Arai, Hiroshi Kurahashi, Masao Ishiwata, Keita Oishi, Yoshikazu Nakamura

研究成果: Article査読

抄録

Accumulation of misfolded proteins in the endoplasmic reticulum (ER) induces the stress response to protect cells against toxicity by the unfolded protein response (UPR), heat shock response (HSR), and ER-associated degradation pathways. Here, we found that over-production of C-terminally truncated multi-transmembrane (MTM) mutant proteins triggers HSR, but not UPR, and clearance of yeast prions [PSI+] and [URE3]. One of the mutant MTM proteins, Dip5ΔC-v82, produces a disabled amino-acid permease. Fluorescence microscopy analysis revealed abnormal accumulation of Dip5ΔC-v82 in the ER. Importantly, the mutant defective in the GET pathway, which functions for ER membrane insertion of tail-anchored proteins, failed to translocate Dip5ΔC-v82 to the ER and disabled Dip5ΔC-v82-mediated prion clearance. These findings suggest that the GET pathway plays a pivotal role in quality assurance of MTM proteins, and entraps misfolded MTM proteins into ER compartments, leading to loss-of-prion through a yet undefined mechanism.

本文言語English
ページ(範囲)1223-1232
ページ数10
ジャーナルBiochimie
95
6
DOI
出版ステータスPublished - 2013 6

ASJC Scopus subject areas

  • 生化学

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