The Protein Disulfide Isomerase Family: from proteostasis to pathogenesis

Motonori Matsusaki, Shingo Kanemura, Misaki Kinoshita, Young Ho Lee, Kenji Inaba, Masaki Okumura

Research output: Contribution to journalArticlepeer-review

50 Citations (Scopus)


In mammalian cells, nearly one-third of proteins are inserted into the endoplasmic reticulum (ER), where they undergo oxidative folding and chaperoning assisted by approximately 20 members of the protein disulfide isomerase family (PDIs). PDIs consist of multiple thioredoxin-like domains and recognize a wide variety of proteins via highly conserved interdomain flexibility. Although PDIs have been studied intensely for almost 50 years, exactly how they maintain protein homeostasis in the ER remains unknown, and is important not only for fundamental biological understanding but also for protein misfolding- and aggregation-related pathophysiology. Herein, we review recent advances in structural biology and biophysical approaches that explore the underlying mechanism by which PDIs fulfil their distinct functions to promote productive protein folding and scavenge misfolded proteins in the ER, the primary factory for efficient production of the secretome.

Original languageEnglish
Article number129338
JournalBiochimica et Biophysica Acta - General Subjects
Issue number2
Publication statusPublished - 2020 Feb


  • Chaperoning
  • ER-associated degradation
  • Oxidative protein folding
  • Pathogenesis
  • PDI
  • Proteostasis


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