Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway

Article Abstract:

A study illustrates that protein translocation into the endoplasmic reticulum (ER) lumen is not a constitutive or deterministic process but instead could be regulated in response to changes in cellular conditions. It is found that during acute ER stress, translocation of secretory and membrane proteins is rapidly and transiently attenuated in a signal sequence-selective manner and their cotranslational rerouting to the cytosol for degradation reduces the burden of misfolded substrates entering the ER and represents a pathway for pre-emptive quality control (pQC).

Eukaryotes, Cellular signal transduction, Structure, Report

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Cotranslocational degradation protects the stressed endoplasmic reticulum from protein overload

Article Abstract:

A study was presented to report that P58[super IPK]/DNAJC3, an unfolded protein response-responsive gene previously implicated in translational control, encodes a cytosolic cochaperone that associates with the ER protein translocation channel Sec61. It is found that P58[super IPK] plays a mediator of cotranslocational ER protein degradation, and this process likely contributes to ER homeostasis in stressed cells.

United States, Membrane proteins, Homeostasis, Molecular chaperones

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CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum

Article Abstract:

The transcription factor C/EBP homologous protein (CHOP) is activated by endoplasmic reticulum (ER) stress, and CHOP deletion protects against its lethal consequences. It is observed that CHOP directly activates GADD34, which promotes ER client protein biosynthesis by dephosphorylating phospho-Ser 51 of the alpha-subunit of translation initiation factor 2 (elF2(alpha)) in stressed cells.

Protein synthesis, Protein biosynthesis, Genetic research

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