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    PIP4Kbeta interacts with and modulates nuclear localization of the high-activity PtdIns5P-4-kinase isoform PIP4Kalpha.

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    Authors
    Bultsma, Yvette
    Keune, Willem-Jan
    Divecha, Nullin
    Affiliation
    CRUK Inositide Laboratory, the Paterson Institute for Cancer Research, Wilmslow Road, Manchester, UK.
    Issue Date
    2010-08-13
    
    Metadata
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    Abstract
    The beta-isoform of PIP4K (PtdIns5P-4-kinase) regulates the levels of nuclear PtdIns5P, which in turn modulates the acetylation of the tumour suppressor p53. The crystal structure of PIP4Kbeta demonstrated that it can form a homodimer with the two subunits arranged in opposite orientations. Using MS, isoform-specific antibodies against PIP4Ks, RNAi (RNA interference) suppression and overexpression studies, we show that PIP4Kbeta interacts in vitro and in vivo with the PIP4Kalpha isoform. As the two isoforms phosphorylate the same substrate to generate the same product, the interaction could be considered to be functionally redundant. However, contrary to expectation, we find that PIP4Kbeta has 2000-fold less activity towards PtdIns5P compared with PIP4Kalpha, and that the majority of PIP4K activity associated with PIP4Kbeta comes from its interaction with PIP4Kalpha. Furthermore, PIP4Kbeta can modulate the nuclear localization of PIP4Kalpha, and PIP4Kalpha has a role in regulating PIP4Kbeta functions. The results of the present study suggest a rationale for the functional interaction between PIP4Kalpha and PIP4Kbeta and provide insight into how the relative levels of the two enzymes may be important in their physiological and pathological roles.
    Citation
    PIP4Kbeta interacts with and modulates nuclear localization of the high-activity PtdIns5P-4-kinase isoform PIP4Kalpha. 2010, 430 (2):223-35 Biochem J
    Journal
    The Biochemical Journal
    URI
    http://hdl.handle.net/10541/111378
    DOI
    10.1042/BJ20100341
    PubMed ID
    20583997
    Type
    Article
    Language
    en
    ISSN
    0264-6021
    EISSN
    1470-8728
    ae974a485f413a2113503eed53cd6c53
    10.1042/BJ20100341
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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