Arabidopsis BAG1 Functions as a Cofactor in Hsc70-Mediated Proteasomal…

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  • 저널명Mol Plant. 2016 Oct 10;9(10):1428-1431. doi: 10.1016/j.molp.2016.06.005.
    • 담당교수[2016년 10월] 황인환 교수연구실
    • 조회74
    • 작성자최고관리자
    • 2017-10-17


    Eliminating misfolded or mistargeted proteins is crucial for cell
    viability because these proteins accumulate as non-specific
    aggregates, which can be toxic to the cell (Lee et al., 2009;
    Sroka et al., 2009). Previously, we have shown that in ppi2
    (plastid protein import 2) mutant plants, the transcript levels of
    Hsc70-4 (one isoform of the Hsc70 family) and CHIP (an E3
    ligase) were highly upregulated, which ultimately plays crucial
    roles in proteasomal degradation of unimported plastid proteins
    (Lee et al., 2009). We also found that, along with those of
    Hsc70-4 and CHIP, the transcript level of AtBAG1 (Arabidopsis
    thaliana Bcl2-associated athanogene 1) in the ppi2 mutant was
    2.38-fold higher than that in the wild-type (Lee et al., 2009). In
    mammalian cells, BAG proteins play multiple roles in protein
    homeostasis, especially as nucleotide exchange factors of
    Hsc70, thereby contributing to protein quality control (Alberti
    et al., 2003; Doukhanina et al., 2006). Therefore, in this study,
    we examined the role of AtBAG in Hsc70-4-mediated protein
    quality control in the cytosol