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Statements

Subject Item
n2:RIV%2F00216224%3A14110%2F12%3A00065570%21RIV14-MZ0-14110___
rdf:type
n5:Vysledek skos:Concept
dcterms:description
The exact role of the central acidic domain of Mdm2 in p53 degradation remains unclear. We therefore performed a systematic and comprehensive analysis of the acidic domain using a series of short deletions and found that only a minor part of the domain was indispensable for Mdm2-mediated p53 ubiquitylation. Moreover, we identified a short stretch of acidic amino acids required for p53 degradation but not ubiquitylation, indicating that, in addition to p53 ubiquitylation, the acidic domain might be involved in a critical post-ubiquitylation step in p53 degradation. Rather than representing a single functional domain, different parts of the acidic region perform separate functions in p53 degradation, suggesting that it might be possible to therapeutically target them independently. The exact role of the central acidic domain of Mdm2 in p53 degradation remains unclear. We therefore performed a systematic and comprehensive analysis of the acidic domain using a series of short deletions and found that only a minor part of the domain was indispensable for Mdm2-mediated p53 ubiquitylation. Moreover, we identified a short stretch of acidic amino acids required for p53 degradation but not ubiquitylation, indicating that, in addition to p53 ubiquitylation, the acidic domain might be involved in a critical post-ubiquitylation step in p53 degradation. Rather than representing a single functional domain, different parts of the acidic region perform separate functions in p53 degradation, suggesting that it might be possible to therapeutically target them independently.
dcterms:title
Mutational analysis reveals a dual role of Mdm2 acidic domain in the regulation of p53 stability Mutational analysis reveals a dual role of Mdm2 acidic domain in the regulation of p53 stability
skos:prefLabel
Mutational analysis reveals a dual role of Mdm2 acidic domain in the regulation of p53 stability Mutational analysis reveals a dual role of Mdm2 acidic domain in the regulation of p53 stability
skos:notation
RIV/00216224:14110/12:00065570!RIV14-MZ0-14110___
n5:predkladatel
n6:orjk%3A14110
n3:aktivita
n16:P
n3:aktivity
P(ED1.100/02/0123), P(GA301/09/1324), P(NS10236)
n3:cisloPeriodika
16
n3:dodaniDat
n18:2014
n3:domaciTvurceVysledku
n8:2572672 n8:6655394 n8:6824226
n3:druhVysledku
n14:J
n3:duvernostUdaju
n20:S
n3:entitaPredkladatele
n17:predkladatel
n3:idSjednocenehoVysledku
152546
n3:idVysledku
RIV/00216224:14110/12:00065570
n3:jazykVysledku
n10:eng
n3:klicovaSlova
p53 degradation; Mdm2; Acidic domain; Mutagenesis; Ubiquitin ligase activity; Binding partner
n3:klicoveSlovo
n4:Mutagenesis n4:Ubiquitin%20ligase%20activity n4:Mdm2 n4:Binding%20partner n4:Acidic%20domain n4:p53%20degradation
n3:kodStatuVydavatele
GB - Spojené království Velké Británie a Severního Irska
n3:kontrolniKodProRIV
[4A481F7D9AA4]
n3:nazevZdroje
FEBS Letters
n3:obor
n7:FD
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
4
n3:projekt
n11:NS10236 n11:GA301%2F09%2F1324 n11:ED1.100%2F02%2F0123
n3:rokUplatneniVysledku
n18:2012
n3:svazekPeriodika
586
n3:tvurceVysledku
Kosztyu, Pavlína Vousden, Karen H. Uldrijan, Stjepan Cetkovská, Kateřina
n3:wos
000306694800004
s:issn
0014-5793
s:numberOfPages
7
n9:doi
10.1016/j.febslet.2012.05.034
n19:organizacniJednotka
14110