Proteins that fail to fold properly as well as constitutive or regulated 
short-lived proteins of the endoplasmatic reticulum (ER) are subjected to 
proteolysis by cytosolic 26 S proteasomes. This process, termed ER-associated 
protein degradation (ERAD), has also been implicated in the generation of some 
important human disorders, for example, cystic fibrosis. To become accessible to 
the proteasome, ERAD substrates must first be retrogradely transported from the 
ER into the cytosol, in a process termed dislocation. Surprisingly, protein 
dislocation from the ER seems to require at least some components that also 
mediate import into this compartment. Moreover, polyubiquitination of ERAD 
substrates at the ER membrane as well as the cytoplasmic Cdc48p/Npl4p/Ufd1p 
complex were shown to contribute to this export reaction. In this article we 
will summarize our current knowledge on ERAD and discuss the possible function 
of certain components involved in this process.