Abstract:
:Nuclear factor of activated T cells (NFATc4) has been implicated as a critical regulator of the cardiac development and hypertrophy. However, the mechanisms for regulating NFATc4 stability and transactivation remain unclear. We showed that NFATc4 protein was predominantly ubiquitinated through the formation of Lysine 48-linked polyubiquitin chains, and this modification decreased NFATc4 protein levels and its transcriptional activity. Furthermore, activation of GSK3beta markedly enhanced NFATc4 ubiquitination and decreased its transactivation, whereas inhibition of GSK3beta had opposite effects. Importantly, ubiquitination and phosphorylation induced by GSK3beta repressed NFATc4-dependent cardiac-specific gene expression. These results demonstrate that the ubiquitin-proteasome system plays an important role in regulating NFATc4 stability and transactivation.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Fan Y,Xie P,Zhang T,Zhang H,Gu D,She M,Li Hdoi
10.1016/j.febslet.2008.11.009subject
Has Abstractpub_date
2008-12-10 00:00:00pages
4008-14issue
29eissn
0014-5793issn
1873-3468pii
S0014-5793(08)00910-1journal_volume
582pub_type
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