Abstract：
:The PML tumor suppressor controls key pathways for growth suppression, induction of apoptosis, and cellular senescence. PML loss occurs frequently in human tumors through unknown posttranslational mechanisms. Casein kinase 2 (CK2) is oncogenic and frequently upregulated in human tumors. Here we show that CK2 regulates PML protein levels by promoting its ubiquitin-mediated degradation dependent on direct phosphorylation at Ser517. Consequently, PML mutants that are resistant to CK2 phosphorylation display increased tumor-suppressive functions. In a faithful mouse model of lung cancer, we demonstrate that Pml inactivation leads to increased tumorigenesis. Furthermore, CK2 pharmacological inhibition enhances the PML tumor-suppressive property in vivo. Importantly, we found an inverse correlation between CK2 kinase activity and PML protein levels in human lung cancer-derived cell lines and primary specimens. These data identify a key posttranslational mechanism that controls PML protein levels and provide therapeutic means toward PML restoration through CK2 inhibition.
journal_name
Celljournal_title
Cellauthors
Scaglioni PP,Yung TM,Cai LF,Erdjument-Bromage H,Kaufman AJ,Singh B,Teruya-Feldstein J,Tempst P,Pandolfi PPdoi
10.1016/j.cell.2006.05.041subject
Has Abstractpub_date
2006-07-28 00:00:00pages
269-83issue
2eissn
0092-8674issn
1097-4172pii
S0092-8674(06)00814-2journal_volume
126pub_type
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