Protein folding in the ER.
Abstract
The endoplasmic reticulum (ER) is a major protein folding compartment for secreted, plasma membrane and organelle proteins. Each of these newly-synthesized polypeptides folds in a deterministic process, affected by the unique conditions that exist in the ER. An understanding of protein folding in the ER is a fundamental biomolecular challenge at two levels. The first level addresses how the amino acid sequence programs that polypeptide to efficiently arrive at a particular fold out of a multitude of alternatives, and how different sequences obtain similar folds. At the second level are the issues introduced by folding not in the cytosol, but in the ER, including the risk of aggregation in a molecularly crowded environment, accommodation of post-translational modifications and the compatibility with subsequent intracellular trafficking. This review discusses both the physicochemical and cell biological constraints of folding, which are the challenges that the ER molecular chaperones help overcome.
- Authors:
- Publication Date:
- Research Org.:
- Argonne National Lab. (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 942678
- Report Number(s):
- ANL/BIO/JA-33687
Journal ID: ISSN 1084-9521; TRN: US200920%%121
- DOE Contract Number:
- DE-AC02-06CH11357
- Resource Type:
- Journal Article
- Journal Name:
- Semin. Cell Dev. Biol.
- Additional Journal Information:
- Journal Volume: 10; Journal Issue: 5 ; Oct. 1999; Journal ID: ISSN 1084-9521
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; AGGLOMERATION; AMINO ACID SEQUENCE; CELL CONSTITUENTS; ENDOPLASMIC RETICULUM; MEMBRANES; MODIFICATIONS; PLASMA; POLYPEPTIDES; PROTEINS
Citation Formats
Stevens, F J, Argon, Y, Biosciences Division, and Univ. of Chicago. Protein folding in the ER.. United States: N. p., 1999.
Web. doi:10.1006/scdb.1999.0315.
Stevens, F J, Argon, Y, Biosciences Division, & Univ. of Chicago. Protein folding in the ER.. United States. https://doi.org/10.1006/scdb.1999.0315
Stevens, F J, Argon, Y, Biosciences Division, and Univ. of Chicago. 1999.
"Protein folding in the ER.". United States. https://doi.org/10.1006/scdb.1999.0315.
@article{osti_942678,
title = {Protein folding in the ER.},
author = {Stevens, F J and Argon, Y and Biosciences Division and Univ. of Chicago},
abstractNote = {The endoplasmic reticulum (ER) is a major protein folding compartment for secreted, plasma membrane and organelle proteins. Each of these newly-synthesized polypeptides folds in a deterministic process, affected by the unique conditions that exist in the ER. An understanding of protein folding in the ER is a fundamental biomolecular challenge at two levels. The first level addresses how the amino acid sequence programs that polypeptide to efficiently arrive at a particular fold out of a multitude of alternatives, and how different sequences obtain similar folds. At the second level are the issues introduced by folding not in the cytosol, but in the ER, including the risk of aggregation in a molecularly crowded environment, accommodation of post-translational modifications and the compatibility with subsequent intracellular trafficking. This review discusses both the physicochemical and cell biological constraints of folding, which are the challenges that the ER molecular chaperones help overcome.},
doi = {10.1006/scdb.1999.0315},
url = {https://www.osti.gov/biblio/942678},
journal = {Semin. Cell Dev. Biol.},
issn = {1084-9521},
number = 5 ; Oct. 1999,
volume = 10,
place = {United States},
year = {Fri Oct 01 00:00:00 EDT 1999},
month = {Fri Oct 01 00:00:00 EDT 1999}
}