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- W2002149580 abstract "Hydrophobic amino acids are normally shielded from the cytosol and their exposure is often used as an indicator of protein misfolding to enable the chaperone mediated recognition and quality control of aberrant polypeptides. Mislocalised membrane proteins, or MLPs, represent a particular challenge to cellular quality control, and in this study membrane protein fragments have been exploited to study a specialised pathway that underlies the efficient detection and proteasomal degradation of MLPs. Our data show that the BAG6 complex and SGTA compete for cytosolic MLPs via recognition of their exposed hydrophobicity, and suggest that SGTA acts to maintain these substrates in a non-ubiquitinated state. Hence, SGTA may counter the actions of BAG6 to delay the ubiquitination of specific precursors and thereby increase their opportunity for successful post-translational delivery to the endoplasmic reticulum. However, when SGTA is overexpressed the normally efficient removal of aberrant MLPs is delayed, increasing their steady state level and promoting aggregation. Our data suggest that SGTA regulates the cellular fate of a range of hydrophobic polypeptides should they become exposed to the cytosol." @default.
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- W2002149580 date "2014-01-01" @default.
- W2002149580 modified "2023-10-17" @default.
- W2002149580 title "SGTA regulates the cytosolic quality control of hydrophobic substrates" @default.
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- W2002149580 doi "https://doi.org/10.1242/jcs.155648" @default.
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