IndraLab

Statements


USP9X deubiquitinates SNCA. 7 / 7
2 | 5

reach
"We recently found that USP9X deubiquitinates alpha-synuclein, and that this process determines the partition of alpha-synuclein between the proteasomal and autophagy pathways."

reach
"Moreover, USP9X can increase MAPT phosphorylation via a second mechanism, by deubiquitinating the protein alpha-synuclein (SNCA) [XREF_BIBR], which functions as a connecting mediator between the glycogen synthase kinase 3beta (GSK3B) and MAPT and has been shown to stimulate MAPT phosphorylation via GSK3B in vitro [XREF_BIBR]."

reach
"In the brain tissues of PD patients, USP9X colocalises with alpha-synuclein inclusions, and in vitro studies show a functional interaction; whilst monoubiquitylated alpha-synuclein is degraded by the proteasome, USP9X deubiquitylation of alpha-synuclein directs its degradation by the less efficient autophagy pathway [XREF_BIBR]."

"Deubiquitination of α-synuclein by USP9X impairs SIAH-dependent α-synuclein proteasomal degradation and promotes degradation by autophagy"

"We recently found that USP9X deubiquitinates α-synuclein, and that this process determines the partition of α-synuclein between the proteasomal and autophagy pathways."

reach
"Usp9x also deubiquitylates mono-ubiquitylated alpha-synuclein raising the possibility it may play a role in the progression of neurodegenerative diseases such as Parkinson 's disease XREF_BIBR."

reach
"We now report that the deubiquitinase USP9X interacts in vivo with and deubiquitinates alpha-synuclein."