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Phosphorylation-dependent degradation of c-Myc is mediated by the F-box protein Fbw7.

The EMBO journal (2004-04-23)
Masayoshi Yada, Shigetsugu Hatakeyama, Takumi Kamura, Masaaki Nishiyama, Ryosuke Tsunematsu, Hiroyuki Imaki, Noriko Ishida, Fumihiko Okumura, Keiko Nakayama, Keiichi I Nakayama

The F-box protein Skp2 mediates c-Myc ubiquitylation by binding to the MB2 domain. However, the turnover of c-Myc is largely dependent on phosphorylation of threonine-58 and serine-62 in MB1, residues that are often mutated in cancer. We now show that the F-box protein Fbw7 interacts with and thereby destabilizes c-Myc in a manner dependent on phosphorylation of MB1. Whereas wild-type Fbw7 promoted c-Myc turnover in cells, an Fbw7 mutant lacking the F-box domain delayed it. Furthermore, depletion of Fbw7 by RNA interference increased both the abundance and transactivation activity of c-Myc. Accumulation of c-Myc was also apparent in mouse Fbw7-/- embryonic stem cells. These observations suggest that two F-box proteins, Fbw7 and Skp2, differentially regulate c-Myc stability by targeting MB1 and MB2, respectively.

Product Number
Product Description

Anti-hFBXW7 antibody , Mouse monoclonal, clone FB407, purified from hybridoma cell culture
Monoclonal Anti-hFBXW7γ antibody produced in mouse, ~2 mg/mL, clone FB343, purified immunoglobulin, buffered aqueous solution
Anti-phospho-c-Myc (pThr58/pSer62) antibody produced in rabbit, affinity isolated antibody, liquid

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