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    Stress-induced phosphorylation of S. pombe Atf1 abrogates its interaction with F box protein Fbh1.

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    Authors
    Lawrence, Clare L
    Jones, Nic
    Wilkinson, Caroline R M
    Affiliation
    Paterson Institute for Cancer Research, University of Manchester, UK.
    Issue Date
    2009-12-01
    
    Metadata
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    Abstract
    The Atf1 transcription factor is critical for directing stress-induced gene expression in fission yeast [1]. Upon exposure to stress, Atf1 is hyperphosphorylated by the mitogen-activated protein kinase (MAPK) Sty1 [2, 3], which results in its stabilization [4]. The resulting increase in Atf1 is vital for a robust response to certain stresses [4]. Here we investigated the mechanism by which phosphorylation stabilizes Atf1. We show that Atf1 is a target for the ubiquitin-proteasome system and that its degradation is dependent upon an SCF E3 ligase containing the F box protein Fbh1. Turnover of Atf1 requires an intact F box, but not DNA helicase activity of Fbh1. Accordingly, disruption of Fbh1 F box function suppresses phenotypes associated with loss of Atf1 phosphorylation. Atf1 and Fbh1 interact under basal conditions, but this binding is lost upon stress. In contrast, a version of Atf1 lacking all intact MAPK sites still interacts with Fbh1 upon stress, indicating that the association between the F box protein and substrate is disrupted by stress-induced phosphorylation. Most F box protein-substrate interactions described to date are mediated positively by phosphorylation [5]. Thus, our findings represent a novel means of regulating the interaction between an F box protein and its substrate. Moreover, Atf1 is the first target described in any organism for the Fbh1 F box protein.
    Citation
    Stress-induced phosphorylation of S. pombe Atf1 abrogates its interaction with F box protein Fbh1. 2009, 19 (22):1907-11 Curr. Biol.
    Journal
    Current Biology
    URI
    http://hdl.handle.net/10541/109305
    DOI
    10.1016/j.cub.2009.09.044
    PubMed ID
    19836238
    Type
    Article
    Language
    en
    ISSN
    1879-0445
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.cub.2009.09.044
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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