UBQLN4 recognizes mislocalized transmembrane domain proteins and targets these to proteasomal degradation
作者： Rigel Suzuki , Hiroyuki Kawahara
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摘要: The majority of transmembrane proteins are integrated into the endoplasmic reticulum (ER) by virtue a signal sequence-mediated co-translational process. However, substantial portion fails to reach ER, leading mislocalized cytosolic polypeptides. Their appropriate recognition and removal utmost importance avoid proteotoxic stress. Here, we identified UBQLN4 as BAG6-binding factor that eliminates newly synthesized defective Using truncated domain protein whose degradation occurs during pre-ER incorporation process model, show recognizes misassembled in cytoplasm targets these proteasome. We suggest exposed segment polypeptides is essential for UBQLN4-mediated substrate discrimination. Importantly, not only model but also pool endogenous were induced depletion SRP54 subunit particle. This study identifies novel quality control mechanism fail their correct destination at ER membrane.
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