Premium
Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin‐associated and ubiquitin‐like domains
Author(s) -
Seok Ko Han,
Uehara Takashi,
Tsuruma Kazuhiro,
Nomura Yasuyuki
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.04.031
Subject(s) - ubiquitin , endoplasmic reticulum , proteasome , microbiology and biotechnology , protein disulfide isomerase , signal transducing adaptor protein , cytosol , deubiquitinating enzyme , chemistry , ubiquitin ligase , biology , biochemistry , signal transduction , gene , enzyme
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.