Protein folding in the endoplasmic reticulum: Lessons from the human chorionic gonadotropin β subunit

Raymond W. Ruddon, Simon A. Sherman, Elliott Bedows

Research output: Contribution to journalReview articlepeer-review

66 Scopus citations

Abstract

There have been few studies of protein folding in the endoplasmic reticulum of intact mammalian cells. In the one case where the in vivo and in vitro folding pathways of a mammalian secretory protein have been compared, the folding of the human chorionic gonadotropin β subunit (hCG-β), the order of formation of the detected folding intermediates is the same. The rate and efficiency with which multidomain proteins such as hCG-β fold to native structure in intact cells is higher than in vitro, although intracellular rates of folding of the β subunit can be approached in vitro in the presence of an optimal redox potential and protein disulfide isomerase. Understanding how proteins fold in vivo may provide a new way to diagnose and treat human illnesses that occur due to folding defects.

Original languageEnglish (US)
Pages (from-to)1443-1452
Number of pages10
JournalProtein Science
Volume5
Issue number8
DOIs
StatePublished - Aug 1996

Keywords

  • disease states related to protein misfolding
  • hCG-β subunit as a model of secretory protein folding
  • molecular chaperones
  • protein misfolding
  • role of disulfide bonds and N-linked glycosylation in protein folding, assembly, and secretion

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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