TY - JOUR AU - Tanji, Kunikazu AU - Miki, Yasuo AU - Ozaki, Taku AU - Maruyama, Atsushi AU - Yoshida, Hidemi AU - Mimura, Junsei AU - Matsumiya, Tomoh AU - Mori, Fumiaki AU - Imaizumi, Tadaatsu AU - Itoh, Ken AU - Kakita, Akiyoshi AU - Takahashi, Hitoshi AU - Wakabayashi, Koichi PY - 2014 DA - 2014/05/03 TI - Phosphorylation of serine 349 of p62 in Alzheimer’s disease brain JO - Acta Neuropathologica Communications SP - 50 VL - 2 IS - 1 AB - Extensive research on p62 has established its role in oxidative stress, protein degradation and in several diseases such as Paget’s disease of the bone, frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Importantly, previous studies showed that p62 binds directly to Keap1, which is a ubiquitin E3 ligase responsible for degrading Nrf2. Indeed, colocalisation of p62 and Keap1 occurs in tumorigenesis and neurodegeneration. A serine (S) residue in the Keap1-interacting region of p62 is phosphorylated in hepatocellular carcinoma, and this phosphorylation contributes to tumour growth through the higher affinity of p62 to Keap1. However, it remains largely unknown whether p62 is phosphorylated in the Keap1-interacting region under neurodegenerative conditions. SN - 2051-5960 UR - https://doi.org/10.1186/2051-5960-2-50 DO - 10.1186/2051-5960-2-50 ID - Tanji2014 ER -