Cargando…
Structure of the human ATG12~ATG5 conjugate required for LC3 lipidation in autophagy
The autophagy factor ATG12~ATG5 conjugate exhibits E3 ligase-like activity by which the lipidation of members of the LC3 family is facilitated. The crystal structure of the human ATG12~ATG5 conjugate bound to the amino-terminal region of ATG16L1, the factor that recruits the conjugate to autophagoso...
Autores principales: | Otomo, Chinatsu, Metlagel, Zoltan, Takaesu, Giichi, Otomo, Takanori |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3540207/ https://www.ncbi.nlm.nih.gov/pubmed/23202584 http://dx.doi.org/10.1038/nsmb.2431 |
Ejemplares similares
-
The autophagic membrane tether ATG2A transfers lipids between membranes
por: Maeda, Shintaro, et al.
Publicado: (2019) -
Structure, lipid scrambling activity and role in autophagosome formation of ATG9A
por: Maeda, Shintaro, et al.
Publicado: (2020) -
Crystallization of the Atg12–Atg5 conjugate bound to Atg16 by the free-interface diffusion method
por: Noda, Nobuo N., et al.
Publicado: (2008) -
ATG5 cancer mutations and alternative mRNA splicing reveal a conjugation switch that regulates ATG12–ATG5-ATG16L1 complex assembly and autophagy
por: Wible, Daric J., et al.
Publicado: (2019) -
An ATG12‐ATG5‐TECPR1 E3‐like complex regulates unconventional LC3 lipidation at damaged lysosomes
por: Corkery, Dale P, et al.
Publicado: (2023)