The ubiquitin‐like domain of Herp is involved in Herp degradation, but not necessary for its enhancement of amyloid β‐protein generation

FEBS Letters

Komano, Hiroto²  Kawamura, Yuuki²  Shiraishi, Hirohisa²  Yanagisawa, Katsuhiko²  Sai, Xiaorei²  Kokame, Koichi¹  Miyata, Toshiyuki¹ 

[1] National Cardiovascular Center Research Institute, Osaka 565-8565, Japan;Department of Dementia Research, National Institute for Longevity Sciences, Obu, Aichi 474-8522, Japan

关键词: Presenilin;    Herp;    Amyloid β-protein;    Endoplasmic reticulum stress;    Ubiquitin-like domain;    Proteasome;    Aβ;    amyloid β-protein;    PS;    presenilin;    AD;    Alzheimer's disease;    APP;    β-amyloid precursor protein;    ER;    endoplasmic reticulum;    ELISA;    enzyme-linked immunosorbent assay;    ULD;    ubiquitin-like domain;    ULP;    ubiquitin-like protein;    ERAD;    ER-associated degradation;   

DOI  :  10.1016/S0014-5793(03)01009-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown