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The ubiquitin‐like domain of Herp is involved in Herp degradation, but not necessary for its enhancement of amyloid β‐protein generation
Author(s) -
Sai Xiaorei,
Kokame Koichi,
Shiraishi Hirohisa,
Kawamura Yuuki,
Miyata Toshiyuki,
Yanagisawa Katsuhiko,
Komano Hiroto
Publication year - 2003
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/s0014-5793(03)01009-3
Subject(s) - endoplasmic reticulum , ubiquitin , intracellular , microbiology and biotechnology , chemistry , protein degradation , unfolded protein response , proteasome , presenilin , calcium in biology , biochemistry , biology , alzheimer's disease , medicine , disease , gene
Herp is an endoplasmic reticulum (ER)‐stress‐inducible membrane protein, which has a ubiquitin‐like domain (ULD). However, its biological function is as yet unknown. Previously, we reported that a high expression level of Herp in cells increases the generation of amyloid β‐protein (Aβ) and that Herp interacts with presenilin (PS). Here, we addressed the role of the ULD of Herp in Aβ generation and intracellular Herp stability. We found that the ULD is not essential for the enhancement of Aβ generation by Herp expression and the interaction of Herp with PS, but is involved in the rapid degradation of Herp, most likely via the ubiquitin/proteasome pathway. Thus, the ULD of Herp most likely plays a role in the regulation of the intracellular level of Herp under ER stress.