Int J Biochem Mol Biol 2011;2(2):168-182
Class II Phosphoinositide 3-kinase C2alpha: what we learned so far?
Simona Mazza, Tania Maffucci
Queen Mary University of London, Barts and The London School of Medicine and Dentistry, Blizard Institute of Cell and Molecular Science,
Centre for Diabetes, Inositide Signalling Group, London E1 2AT, UK.
Received April 13, 2011; accepted April 20, 2011; Epub April 22, 2011; Published April 30, 2011
Abstract: More than fifteen years after the first identification of a class II isoform of phosphoinositide 3-kinase (PI3K) in Drosophila
melanogaster this subfamily remains the most enigmatic among all PI3Ks. What are the functions of these enzymes? What are their
mechanisms of activation? Which downstream effectors are specifically regulated by these isoforms? Are class I and class II PI3Ks redundant
or do they control different intracellular processes? And, more important, do class II PI3Ks have a role in human diseases? The recent
increased interest on class II PI3Ks has started providing some answers to these questions but still a lot needs to be done to completely
uncover the contribution of these enzymes to physiological processes and possibly to pathological conditions. Here we will summarise the
recent findings on the alpha isoform of mammalian class II PI3Ks (PI3K-C2alpha) and we will discuss the potential involvement of this enzyme
in human diseases. (IJBMB1104003).
Keywords: Phosphoinositide 3-kinase, phosphoinositides, glucose transport, insulin secretion, neurosecretion, exocytosis
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Address all correspondence to:
Tania Maffucci, PhD
Inositide Signalling Group, Centre for Diabetes
Blizard Institute of Cell and Molecular Science
Barts and The London School of Medicine and Dentistry
Queen Mary University of London
4 Newark Street, London E1 2AT, UK.
Tel: +44(0)2078828423; Fax: +44(0)2078822186