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    PIP5K-driven PtdIns(4,5)P2 synthesis: regulation and cellular functions.

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    Authors
    Van den Bout, Iman
    Divecha, Nullin
    Affiliation
    Inositide Laboratory, Paterson Institute for Cancer Research, Wilmslow Road, Manchester M20 4BX, UK. ivbout@picr.man.ac.uk
    Issue Date
    2009-11-01
    
    Metadata
    Show full item record
    Abstract
    It has long been known that phosphoinositides are present in cellular membranes, but only in the past four decades has our understanding of their importance for proper cell function advanced significantly. Key to determining the biological roles of phosphoinositides is understanding the enzymes involved in their metabolism. Although many such enzymes have now been identified, there is still much to learn about their cellular functions. Phosphatidylinositol 4-phosphate 5-kinases (PIP5Ks) are a group of kinases that catalyse the production of phosphatidylinositol (4,5)-bisphosphate [PtdIns(4,5)P(2)]. As well as being a substrate for the enzymes phospholipase C (PLC) and phosphatidylinositol 3-kinase (PI3K), PtdIns(4,5)P(2) acts as a second messenger in its own right, influencing a variety of cellular processes. In this Commentary, we review how PIP5Ks are modulated to achieve regulated PtdIns(4,5)P(2) production, and discuss the role of these proteins in different cellular processes.
    Citation
    PIP5K-driven PtdIns(4,5)P2 synthesis: regulation and cellular functions. 2009, 122 (Pt 21):3837-50 J. Cell. Sci.
    Journal
    Journal of Cell Science
    URI
    http://hdl.handle.net/10541/109306
    DOI
    10.1242/jcs.056127
    PubMed ID
    19889969
    Type
    Article
    Language
    en
    ISSN
    1477-9137
    ae974a485f413a2113503eed53cd6c53
    10.1242/jcs.056127
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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