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@article{750765,
author = {Uldrijan, Stjepan and Pannekoek, WillemandJan and Vousden, Karen H.},
article_number = {1},
keywords = {E3; MDM2; MDMX; p53; ubiquitin},
language = {eng},
issn = {0261-4189},
journal = {EMBO Journal},
title = {An essential function of the extreme C-terminus of MDM2 can be provided by MDMX},
volume = {26},
year = {2007}
}
TY - JOUR
ID - 750765
AU - Uldrijan, Stjepan - Pannekoek, Willem-Jan - Vousden, Karen H.
PY - 2007
TI - An essential function of the extreme C-terminus of MDM2 can be provided by MDMX
JF - EMBO Journal
VL - 26
IS - 1
SP - 102-120
EP - 102-120
SN - 02614189
KW - E3
KW - MDM2
KW - MDMX
KW - p53
KW - ubiquitin
N2 - MDM2 (HDM2) is a ubiquitin ligase that can target the p53 tumor suppressor protein for degradation. The RING domain is essential for the E3 activity of MDM2, and we show here that the extreme C-terminal tail of MDM2 is also critical for efficient E3 activity. Loss of E3 function in MDM2 mutants deleted of the C-terminal tail correlated with a failure of these mutants to oligomerize with MDM2, or with the related protein MDMX (HDMX). However, MDM2 containing point mutations within the C-terminus that inactivated E3 function retained the ability to oligomerize with the wild-type MDM2 RING domain and MDMX, and our results indicate that oligomers containing both wild-type MDM2 and a C-terminal mutant protein retain E3 function both in auto-degradation and degradation of p53. Interestingly, the E3 activity of C-terminal point mutants of MDM2 can also be supported by interaction with wild-type MDMX, suggesting that MDMX can directly contribute to E3 function.
ER -
ULDRIJAN, Stjepan, Willem-Jan PANNEKOEK a Karen H. VOUSDEN. An essential function of the extreme C-terminus of MDM2 can be provided by MDMX. \textit{EMBO Journal}. 2007, roč.~26, č.~1, s.~102-120. ISSN~0261-4189.
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