Endoplasmic reticulum-associated protein degradation (ERAD) removes 
improperly-folded proteins from the ER membrane into the cytosol where they 
undergo proteasomal degradation. Valosin-containing protein (VCP)/p97 mediates 
in the extraction of ERAD substrates from the ER. BRSK2 (also known as SAD-A), a 
serine/threonine kinase of the AMP-activated protein kinase family affected 
VCP/p97 activity in ERAD. In addition, BRSK2 interacted with VCP/p97 via three 
of the four functional domains of VCP/p97. Immunofluorescence demonstrated that 
BRSK2 and VCP/p97 were co-localized and also that knockdown of endogenous BRSK2 
induced increased levels of CD3δ, a substrate in ERAD for VCP/p97. Thus, BRSK2 
might affect the activity of VCP/p97 in ERAD.