Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Inherited mutations and polymorphisms that alter the sequence of a polypeptide can affect its folding and stability, triggering disease at birth and during aging. A central cellular mechanism for generating and maintaining normal protein folds is the protein homeostasis or proteostasis network (referred to as the PN) (1). These processes sustain functional proteins as well as direct their removal from the cell during protein turnover or in response to misfolding. This "yin-yang" balance is critical for normal cellular, tissue, and organismal physiology. On page 805 in this issue, Okiyoneda et al. (2) show that the PN operates globally, constantly surveying protein folds, from co-translational insertion of proteins into the endoplasmic reticulum (ER) to removal of unstable proteins at the plasma membrane.
1 Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037, USA. 2 Department of Chemical Physiology, Skaggs Institute for Chemical Biology, and Institute for Childhood and Neglected Diseases, Scripps Research Institute, La Jolla, CA 92037, USA.
The editors suggest the following Related Resources on Science sites: