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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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