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UID:1199@biology.technion.ac.il

DTSTART;TZID=Asia/Jerusalem:20231122T130000

DTEND;TZID=Asia/Jerusalem:20231122T140000

DTSTAMP:20231120T101413Z

URL:https://biology.technion.ac.il/en/seminars/phd-graduate-seminar-anwar-
 bdarneh/

SUMMARY:PhD Graduate Seminar- Anwar Bdarneh [No Categories]
DESCRIPTION:Location: : hybrid- in the Faculty Auditorium/ZOOM: https://tec
 hnion.zoom.us/j/94240537873   Anwar Bdarneh\n Affiliation: \n Host:Prof. M
 ichael Glickman \n Elucidating the mysterious ubiquitin ligase mechanism o
 f Ubiquitin C-terminal Hydrolase-L1 (UCH-L1)\n\nUbiquitination is a post-t
 ranslational modification that has emerged as a key regulator of most cell
 ular processes\, ranging from subcellular localization to protein function
 \, cell signaling\, and protein degradation by the proteasome or the lysos
 ome.\nLike other PTMs\, ubiquitination is reversible due to the activity o
 f specific protases called deubiquitinating enzymes (DUBs). A unique DUB i
 s ubiquitin C-terminal hydrolase L1 (UCH-L1)\, which is restricted to the 
 cleavage of small adducts from the C-terminus of ubiquitin.\nUCH-L1 is abu
 ndantly expressed in neurons\, yet its biological function in neuronal cel
 ls remains a mystery. Different studies have shown that UCH-L1 plays a rol
 e in neurodegeneration. Moreover\, we showed that UCH-L1 over-expression d
 elays the accumulation of Alzheimer's hallmarks\, which suggests that UCH-
 L1 plays a unique role in prolonging neuronal health.\nIn addition to its 
 extensively studied hydrolase activity as a DUB\, we characterize an addit
 ional enzymatic activity\, in which UCH-L1 acts as a ligase. We succeeded 
 in identifying\, for the first time\, a new active site that is responsibl
 e for this distinct activity. Furthermore\, we demonstrated that the two a
 ctive sites work independently of each other. Additionally\, we provide an
  initial characterization of the enzymatic cascade in which it participate
 s.\nWe are currently delineating which of the two distinct enzymatic activ
 ities is essential for UCH-L1's role in suppressing Alzheimer's hallmarks.
  The investigation into the biochemical mechanisms underlying UCH-L1's dua
 l enzymatic activities aims to unravel the mystery of its unique function 
 in neurons.\n 
LOCATION:: hybrid- in the Faculty Auditorium/ZOOM: https://technion.zoom.us
 /j/94240537873

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