Cargando…
E2-EPF UCP Possesses E3 Ubiquitin Ligase Activity via Its Cysteine 118 Residue
Here, we show that E2-EPF ubiquitin carrier protein (UCP) elongated E3-independent polyubiquitin chains on the lysine residues of von Hippel-Lindau protein (pVHL) and its own lysine residues both in vitro and in vivo. The initiation of the ubiquitin reaction depended on not only Lys11 linkage but al...
Autores principales: | Lim, Jung Hwa, Shin, Hee Won, Chung, Kyung-Sook, Kim, Nam-Soon, Kim, Ju Hee, Jung, Hong-Ryul, Im, Dong-Soo, Jung, Cho-Rok |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5042379/ https://www.ncbi.nlm.nih.gov/pubmed/27685940 http://dx.doi.org/10.1371/journal.pone.0163710 |
Ejemplares similares
-
E2-EPF UCP regulates stability and functions of missense mutant pVHL via ubiquitin mediated proteolysis
por: Park, Kyeong-Su, et al.
Publicado: (2015) -
Stabilization of E2-EPF UCP protein is implicated in hepatitis B virus-associated hepatocellular carcinoma progression
por: Lim, Jung Hwa, et al.
Publicado: (2019) -
Herpesviruses possess conserved proteins for interaction with Nedd4 family ubiquitin E3 ligases
por: Koshizuka, Tetsuo, et al.
Publicado: (2018) -
Ubiquitin E3 ligases in cancer: somatic mutation and amplification
por: Jo, Eun-Hye, et al.
Publicado: (2023) -
Negative regulation of NEMO signaling by the ubiquitin E3 ligase MARCH2
por: Chathuranga, Kiramage, et al.
Publicado: (2020)