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    FEBS Lett. 2011 Jul 21;585(14):2151-7. Epub 2011 May 24.

    PI3K-dependent phosphorylation of Fbw7 modulates substrate degradation and activity.

    Schülein C, Eilers M, Popov N.

    Source

    Theodor Boveri Institute, Biocenter, University of Würzburg, Würzburg, Germany.

    Abstract

    The Fbw7 tumor suppressor gene encodes the substrate recognition subunit of the SCF ubiquitin ligase, which targets for degradation a range of oncogenic proteins in a phosphorylation-dependent manner. Substrate phosphorylation is thought to be the main mechanism that ensures timely destruction of Fbw7 substrates. We show here that PI3K dependent phosphorylation of Fbw7 stimulates its ability to ubiquitinate and degrade its substrates. Mutation of the phosphorylation site destabilizes Fbw7 and attenuates degradation of cyclin E and Myc leading to the enhanced expression of a subset of Myc target genes. We suggest that PI3K-dependent phosphorylation of Fbw7 controls the balance between turnover of Fbw7 and its substrates to fine-tune their activity.

    Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

    PMID:
    21620836
    [PubMed - indexed for MEDLINE]

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