Abstract:
:CHFR ubiquitin ligase acts as a checkpoint upon DNA damage and its functional inactivation is one of key characteristics of tumor development and metastasis. Despite the crucial role in maintaining genome integrity and cell cycle progression, little is known how CHFR stability is regulated. Here, we showed that CHFR is covalently modified by SUMO-1 at lysine 663 and subsequently destabilized by ubiquitin-proteasome system. While CHFR(K663R) substitution mutation does not alter its subcellular localization, SUMOylation-defective CHFR(K663R)-stable cells exhibit substantial growth suppression due to the increased stability of CHFR(K663R). Moreover, protein level of CHFR, not CHFR(K663R), is rapidly declined under SUMOylation-promoting conditions, and SENP2 deSUMOylating enzyme reverses its SUMO-modification. Collectively, we demonstrated that CHFR stability is regulated by SUMOylation-dependent proteasomal degradation. Therefore, our study underscores the importance of CHFR SUMOylation as a new regulatory mechanism of CHFR and highlights the emerging role of SUMOylation in modulating protein stability.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Kwon YE,Bae SJ,Kim M,Seol JHdoi
10.1016/j.bbrc.2012.10.111subject
Has Abstractpub_date
2013-01-04 00:00:00pages
213-7issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(12)02103-1journal_volume
430pub_type
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