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Statements

Subject Item
n2:RIV%2F00216224%3A14110%2F12%3A00057309%21RIV13-GA0-14110___
rdf:type
skos:Concept n17:Vysledek
dcterms:description
Mdm2 can mediate p53 ubiquitylation and degradation either in the form of the Mdm2 homodimer or Mdm2/MdmX heterodimer. The ubiquitin ligase activity of these complexes resides mainly in their respective RING finger domains and also requires adjacent C-terminal tails. So far, structural studies have failed to show significant differences between Mdm2 RING homodimers and Mdm2/MdmX RING heterodimers. Here, we report that not only the primary amino acid sequence, but also the length of the C-terminal tail of Mdm2 is highly conserved through evolution and plays an important role in Mdm2 activity toward p53. Mdm2 mutants with extended C termini do not ubiquitylate p53 despite being capable of forming Mdm2 homodimers through both RING-acidic domain and RING-RING interactions. All extended mutants also retained the ability to interact with MdmX, and this interaction led to reactivation of their E3 ubiquitin ligase activity. Mdm2 can mediate p53 ubiquitylation and degradation either in the form of the Mdm2 homodimer or Mdm2/MdmX heterodimer. The ubiquitin ligase activity of these complexes resides mainly in their respective RING finger domains and also requires adjacent C-terminal tails. So far, structural studies have failed to show significant differences between Mdm2 RING homodimers and Mdm2/MdmX RING heterodimers. Here, we report that not only the primary amino acid sequence, but also the length of the C-terminal tail of Mdm2 is highly conserved through evolution and plays an important role in Mdm2 activity toward p53. Mdm2 mutants with extended C termini do not ubiquitylate p53 despite being capable of forming Mdm2 homodimers through both RING-acidic domain and RING-RING interactions. All extended mutants also retained the ability to interact with MdmX, and this interaction led to reactivation of their E3 ubiquitin ligase activity.
dcterms:title
Mutational analysis of Mdm2 C-terminal tail suggests an evolutionarily conserved role of its length in Mdm2 activity toward p53 and indicates structural differences between Mdm2 homodimers and Mdm2/MdmX heterodimers Mutational analysis of Mdm2 C-terminal tail suggests an evolutionarily conserved role of its length in Mdm2 activity toward p53 and indicates structural differences between Mdm2 homodimers and Mdm2/MdmX heterodimers
skos:prefLabel
Mutational analysis of Mdm2 C-terminal tail suggests an evolutionarily conserved role of its length in Mdm2 activity toward p53 and indicates structural differences between Mdm2 homodimers and Mdm2/MdmX heterodimers Mutational analysis of Mdm2 C-terminal tail suggests an evolutionarily conserved role of its length in Mdm2 activity toward p53 and indicates structural differences between Mdm2 homodimers and Mdm2/MdmX heterodimers
skos:notation
RIV/00216224:14110/12:00057309!RIV13-GA0-14110___
n17:predkladatel
n18:orjk%3A14110
n3:aktivita
n6:P
n3:aktivity
P(GA301/09/1324)
n3:cisloPeriodika
5
n3:dodaniDat
n15:2013
n3:domaciTvurceVysledku
n5:6655394 n5:6824226 n5:2572672
n3:druhVysledku
n19:J
n3:duvernostUdaju
n9:S
n3:entitaPredkladatele
n7:predkladatel
n3:idSjednocenehoVysledku
152543
n3:idVysledku
RIV/00216224:14110/12:00057309
n3:jazykVysledku
n20:eng
n3:klicovaSlova
p53; Mdm2; RING domain; ubiquitylation; ubiquitin ligase; E3
n3:klicoveSlovo
n13:RING%20domain n13:E3 n13:ubiquitylation n13:p53 n13:ubiquitin%20ligase n13:Mdm2
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[47E056FD3099]
n3:nazevZdroje
Cell Cycle
n3:obor
n16:EB
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
4
n3:projekt
n4:GA301%2F09%2F1324
n3:rokUplatneniVysledku
n15:2012
n3:svazekPeriodika
11
n3:tvurceVysledku
Cetkovská, Kateřina Kosztyu, Pavlína Uldrijan, Stjepan Vousden, Karen H.
n3:wos
000300989700024
s:issn
1538-4101
s:numberOfPages
10
n8:doi
10.4161/cc.11.5.19445
n14:organizacniJednotka
14110