Proteins that fail to fold properly as well as constitutive or regulated 
short-lived proteins of the endoplasmic reticulum are subjected to proteolysis 
by cytosolic 26S proteasomes. This process is known as endoplasmic 
reticulum-associated protein degradation. In order to become accessible to the 
proteasome of this system substrates must first be retrogradely transported from 
the endoplasmic reticulum into the cytosol, in a process termed dislocation. 
This export step seems to be accompanied by polyubiquitination of such 
molecules. Surprisingly, protein dislocation from the endoplasmic reticulum 
seems to require at least some components that mediate import into this 
compartment. However, protein import and export display differences in the 
mechanism that provides the driving force and ensures directionality. Of special 
interest is the cytoplasmic Cdc48p/Npl4p/Ufd1p complex, which is required for 
the degradation of various endoplasmic reticulum-associated protein degradation 
substrates and seems to function in a step after polyubiquitination but before 
proteasomal digestion. In this review, we will summarize our knowledge on 
protein export during endoplasmic reticulum-associated protein degradation and 
discuss the possible function of certain components involved in this process.