Highlights d P5 dimerizes via a unique leucine-valine adhesive motif in the first Trx-like domain d The adhesive motif is radically different from conventional coiled-coil motifs d The dimeric structure serves to promote P5-mediated inactivation of IRE1a d Ca 2+ -binding regions and Ca 2+ -dependent functional regulation were clarified for P5
Complicated and sophisticated protein homeostasis (proteostasis) networks in the endoplasmic reticulum (ER), comprising disulfide catalysts, molecular chaperones, and their regulators, help to maintain cell viability. Newly synthesized proteins inserted into the ER need to fold and assemble into unique native structures to fulfill their physiological functions, and this is assisted by protein disulfide isomerase (PDI) family. Herein, we focus on recent advances in understanding the detailed mechanisms of PDI family members as guides for client folding and assembly to ensure the efficient production of secretory proteins.
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