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    Epidermal growth factor stimulates translocation of the class II phosphoinositide 3-kinase PI3K-C2beta to the nucleus.

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    Authors
    Banfic, Hrvoje
    Visnjic, Dora
    Mise, Nikica
    Balakrishnan, Sanjeevi
    Deplano, Simona
    Korchev, Yuri E.
    Domin, Jan
    Affiliation
    Imperial College London
    Issue Date
    2009-08-15
    
    Metadata
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    Abstract
    Although the class II phosphoinositide 3-kinase enzymes PI3K-C2alpha and PI3K-C2beta act acutely downstream of cell surface receptors they have also been localized to nuclei in mammalian cells. As with the class I PI3K enzymes, the relationship between the pools of enzyme present in cytoplasm and nuclei remains poorly understood. In this study we test the hypothesis that PI3K-C2beta translocates to nuclei in response to growth factor stimulation. Fractionating homogenates of quiescent cells revealed that less than 5% of total PI3K-C2beta resides in nuclei. Stimulation with epidermal growth factor sequentially increased levels of this enzyme, firstly in the cytosol and secondly in the nuclei. Using detergent-treated nuclei, we showed that PI3K-C2beta co-localized with lamin A/C in the nuclear matrix. This was confirmed biochemically, and a phosphoinositide kinase assay showed a statistically significant increase in nuclear PI3K-C2beta levels and lipid kinase activity following epidermal growth factor stimulation. C-terminal deletion and point mutations of PI3K-C2beta demonstrated that epidermal growth factor-driven translocation to the nucleus is dependent on a sequence of basic amino acid residues (KxKxK) that form a nuclear localization motif within the C-terminal C2 domain. Furthermore, when this sequence was expressed as an EGFP (enhanced green fluorescent protein) fusion protein, it translocated fluorescence into nuclei with an efficiency dependent upon copy number. These data demonstrate that epidermal growth factor stimulates the appearance of PI3K-C2beta in nuclei. Further, this effect is dependent on a nuclear localization signal present within the C-terminal C2 domain, indicating its bimodal function regulating phospholipid binding and shuttling PI3K-C2beta into the nucleus.
    Citation
    Banfic, H. et al (2009) 'Epidermal growth factor stimulates translocation of the class II phosphoinositide 3-kinase PI3K-C2beta to the nucleus' Biochem. J. 422 (1):53-60
    Publisher
    Portland Press
    Journal
    Biochemical journal
    URI
    http://hdl.handle.net/10547/227186
    DOI
    10.1042/BJ20090654
    PubMed ID
    19496756
    Additional Links
    http://www.biochemj.org/content/422/1/53.long
    Type
    Article
    Language
    en
    ISSN
    1470-8728
    ae974a485f413a2113503eed53cd6c53
    10.1042/BJ20090654
    Scopus Count
    Collections
    Cell and Cryobiology Research Group

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