Axel Knebel

TL;DR: These results provide the first evidence that PINK1 is activated following Δψm depolarization and suggest that Pink1 directly phosphorylates and activates Parkin, and indicate that monitoring phosphorylation of Parkin at Ser65 and/or Pinks1 at Thr257 represent the first biomarkers for examining activity of the PINK 1-Parkin signalling pathway in vivo.

TL;DR: It is proposed that phosphorylation of Parkin at Ser65 serves to prime the E3 ligase enzyme for activation by ubiquitinPhospho−Ser65, suggesting that small molecules that mimic ubiquitins could hold promise as novel therapies for Parkinson's disease.

TL;DR: The results of the present study suggest that moesin, ezrin and radixin may be LRRK2 substrates, findings that have been exploited to develop the first robust quantitative assay to measure L RRK2 kinase activity.

TL;DR: This work has developed a sensitive and fast assay to quantify in vitro DUB enzyme activity using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry, and confirms the high specificity of many members of the OTU and JAB/MPN/Mov34 metalloenzyme DUB families.

TL;DR: The anisomycin‐induced phosphorylation of Ser359 was unaffected by SB 203580, U0126 or rapamycin, and was prevented by overexpression of a catalytically inactive SAPK4/p38δ mutant, suggesting that SAPK 4/p 38δ may mediate the inhibition of eEF2K by this stress.