Format

Send to

Choose Destination
See comment in PubMed Commons below
Traffic. 2004 Nov;5(11):815-20.

A cure for traffic jams: small molecule chaperones in the endoplasmic reticulum.

Author information

  • 1University of Cambridge, Cambridge Institute for Medical Research and Department of Clinical Biochemistry, Hills Road, Cambridge CB2 2XY, UK. kbr20@cam.ac.uk

Abstract

Folding in the endoplasmic reticulum is the limiting step for the biogenesis of most secretory pathway cargo proteins; proteins which fail to fold are initially retained in the endoplasmic reticulum and subsequently often degraded. Mutations that affect secretory protein folding have profound phenotypes irrespective of their direct impact on protein function, because they prevent secretory proteins from reaching their final destination. When unicellular organisms are stressed by fluctuation of temperature or ionic strength, they synthesize high concentrations of small molecules such as trehalose or glycerol to prevent protein denaturation. These osmolytes can also stabilize mutant secretory proteins and allow them to pass secretory protein quality control in the endoplasmic reticulum. Specific ligands and cofactors such as ions, sugars, or peptides have similar effects on specific defective proteins and are beginning to be used as therapeutic agents for protein trafficking diseases.

[PubMed - indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Wiley
    Loading ...
    Write to the Help Desk