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UID:1162@biology.technion.ac.il

DTSTART;TZID=Asia/Jerusalem:20230214T130000

DTEND;TZID=Asia/Jerusalem:20230214T133000

DTSTAMP:20230129T091648Z

URL:https://biology.technion.ac.il/en/seminars/msc-graduate-seminar-2/

SUMMARY:Msc Graduate Seminar- Shany Greenstein [No Categories]
DESCRIPTION:Location:  hybrid- in the Faculty Auditorium/ZOOM:   https://te
 chnion.zoom.us/j/93416730395  Shany Greenstein\n Affiliation: \n Host:Prof
 . Glickman Michael\n Understanding the turnover of the truncated form of m
 utant ubiquitin UBB+1\, UBBG76Y\n\nUbiquitin is a 76 amino acid molecule t
 hat labels proteins for degradation. Its C-terminus at 76 glycine is conju
 gated to the side chain of a substrate lysine. The only known ubiquitin mu
 tant is ubiquitin B+1 (UBB+1)\, caused by a non-heredity missense mutation
  during transcription of the UBB gene. The resulting protein is a ubiquiti
 n domain with a G76Y mutation and an additional 19 amino acids (AA) tail. 
 This UBB+1 protein is found in sporadic and familial AD brains. It was rec
 ently shown in our lab that the expression of UBB+1 accelerates AD patholo
 gy. UBB+1 has been claimed to be cleaved by a carboxyl-terminal hydrolase 
 isozyme L3 (UCHL3)\, resulting in a truncated form of UBB+1: ubiquitin wit
 h a G76Y mutation (UBG76Y). Lacking a C-terminal glycine at position 76\, 
 UBG76Y is unable to conjugate to substrates. To date\, little is known abo
 ut UBG76Y. We wanted to study the fate of UBG76Y and understand whether it
  alleviates or exacerbates the stress imposed by UBB+1. We generated a UCH
 L3 KO cell line in HEK293 using CRISPR/Case9 and showed that UCHL3 is the 
 main enzyme that cleaves UBB+1 in mammalian cells. We also expressed UBG76
 Y in HEK293 cells and observed that UBG76Y does not accumulate  to the sa
 me extent as UBB+1. In addition\, by inhibiting degradation pathways we pr
 ovide evidence that UBG76Y is degraded by autophagy. To summarize\, conver
 ting UBB+1 to UBG76Y may be a strategy of cells to alleviate the stress as
 sociated with UBB+1 . 
LOCATION: hybrid- in the Faculty Auditorium/ZOOM:   https://technion.zoom.u
 s/j/93416730395

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