[HTML][HTML] Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains

HS Ko, T Uehara, K Tsuruma, Y Nomura - FEBS letters, 2004 - Elsevier
HS Ko, T Uehara, K Tsuruma, Y Nomura
FEBS letters, 2004Elsevier
Mammalian cells acquire tolerance against multiple stressors through the high-level
expression of stress-responsible genes. We have previously demonstrated that protein-
disulfide isomerase (PDI) together with ubiquilin are up-regulated in response to
hypoxia/brain ischemia, and play critical roles in resistance to these damages. We show
here that ubiquilin interacts preferentially with poly-ubiquitin chains and 19S proteasome
subunits. Taken together, these results suggest that ubiquitin could serve as an adaptor …
Mammalian cells acquire tolerance against multiple stressors through the high-level expression of stress-responsible genes. We have previously demonstrated that protein-disulfide isomerase (PDI) together with ubiquilin are up-regulated in response to hypoxia/brain ischemia, and play critical roles in resistance to these damages. We show here that ubiquilin interacts preferentially with poly-ubiquitin chains and 19S proteasome subunits. Taken together, these results suggest that ubiquitin could serve as an adaptor protein that both interacts with PDI and mediates the delivery of poly-ubiquitylated proteins to the proteasome in the cytosol in the vicinity of the endoplasmic reticulum membrane.
Elsevier