Proteasome inhibition promotes Parkin-Ubc13 interaction and lysine 63-linked ubiquitination.
Disruption of the ubiquitin-proteasome system, which normally identifies and degrades unwanted intracellular proteins, is thought to underlie neurodegeneration. Supporting this, mutations of Parkin, a ubiquitin ligase, are associated with autosomal recessive parkinsonism. Remarkably, Parkin can prot...
Main Authors: | Grace G Y Lim, Katherine C M Chew, Xiao-Hui Ng, Adeline Henry-Basil, Roy W X Sim, Jeanne M M Tan, Chou Chai, Kah-Leong Lim |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2013-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC3759450?pdf=render |
Similar Items
-
K63-linked ubiquitination and neurodegeneration
by: Kah-Leong Lim, et al.
Published: (2011-07-01) -
Characterization of the Ubc13-Mms2 Lysine-63-linked ubiquitin conjugating complex
by: Pastushok, Landon Keith
Published: (2006) -
UBC13 is an RNF213‐associated E2 ubiquitin‐conjugating enzyme, and Lysine 63‐linked ubiquitination by the RNF213‐UBC13 axis is responsible for angiogenic activity
by: Toshiyuki Habu, et al.
Published: (2021-04-01) -
Dynamic regulation of histone lysine methylation via the ubiquitin-proteasome system.
by: Lim, Hui Jun
Published: (2013) -
Parkin interacts with the 26S proteasome via Rpn13, a novel ubiquitin receptor
by: Aguileta, Miguel
Published: (2011)