Structural basis for the folding of PINK1 by the HSP90–CDC37 chaperone complex
Kei Okatsu(Kyoto University), Shuya Fukai(Tokyo Institute of Technology), Yukihiko Sugita(Okinawa Institute of Science and Technology Graduate University), S. Goto(Kyoto University), Hayato Yamamoto(Kyoto University), Akinori Okamoto(Kyoto University), Takeshi Noda(Kyoto University)
Cited by 0
Related Papers
PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
|The Journal of Cell Biology|2010|1.9k
Ubiquitin is phosphorylated by PINK1 to activate parkin
|Nature|2014|1.5k
PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria
|Nature Communications|2012|599
p62/SQSTM1 cooperates with Parkin for perinuclear clustering of depolarized mitochondria
|Genes to Cells|2010|390
Phosphorylated ubiquitin chain is the genuine Parkin receptor
|The Journal of Cell Biology|2015|261