Quality control of inner nuclear membrane proteins by the Asi complex

Abstract

Trashing misfolded membrane proteins Proteins move to and from the inner nuclear membrane (INM) from the rest of the endoplasmic reticulum through the nuclear pores. This movement is tightly controlled. Consequently, the INM accumulates a specific set of proteins required for a variety of functions, including chromosome organization and transcriptional control. But when INM proteins misfold, how are they eliminated? Foresti et al. addressed this question in yeast and found that a previously elusive branch of the endo–plasmic reticulum–associated degradation system was key (see the Perspective by Shao and Hegde). Science , this issue p. 751 ; see also p. 701