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Phosphoinositides and Disease pp 87–98Cite as

Phosphoinositides in Neuroexocytosis and Neuronal Diseases

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Part of the book series: Current Topics in Microbiology and Immunology ((CT MICROBIOLOGY,volume 362))

Abstract

Phosphoinositides (PIs) are a family of phospholipids derived from phosphatidylinositol (PtdIns), whose location, synthesis, and degradation depend on specific PI kinases and phosphatases. PIs have emerged as fundamental regulators of secretory processes, such as neurotransmitter release, hormone secretion, and histamine release in allergic responses. In neurons and neuroendocrine cells, regulated secretion requires the calcium-dependent fusion of transmitter-containing vesicles with the plasma membrane. The role played by PIs in exocytosis is best exemplified by the Ca2+-dependent binding of vesicular Synaptotagmin1 to the plasma membrane PtdIns(4,5)P2, and the recently demonstrated role of PtdIns(4,5)P2 in the mobilization of secretory vesicles to the plasma membrane. New evidence has also recently emerged of an alternative PI pathway that can control exocytosis positively (via PtdIn3P) or negatively (via PtdIns(3,5)P2). However, the positive or negative effectors for these pathways remain to be established. Reducing PtdIns(3,5)P2 potentiates neuroexocytosis but leads to neuronal degeneration and has been linked to certain forms of Charcot-Marie-Tooth disease and amyotrophic lateral sclerosis. The goal of this review is to describe the role of PIs in neuroexocytosis and explore the current hypotheses linking these effects to human diseases.

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Abbreviations

\( {\text{A}}\beta{\text{-}1}\;42 \) :

Amyloid beta peptide

Arf-1:

ADP-ribosylation factor 1

CAPS:

Ca2+-dependent activator protein for secretion

Cdc42:

Cell division control protein 42 homolog

CMT:

Charcot-Marie-Tooth

ER:

Endoplasmic reticulum

FAD:

Familial Alzheimer’s disease

FYVE:

Fab1, YGL023,VPS27, and EEA1

GLUT4:

Glucose transporter type 4

LDCVs:

Large dense core vesicles

Mtmr:

Myotubularin-related protein

NCS-1:

Neuronal calcium sensor 1

PIKfyve:

Phosphoinositide kinase for five positions containing a Fyve finger

TGN:

Trans-Golgi network

PI:

Phosphoinositide

SNARE:

Soluble NSF attachment protein receptor

Syt:

Synaptotagmin

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Acknowledgments

This work was supported by two National Health and Medical Research Council (NHMRC) project grants (to F.A.M. and S.L.O.). F.A.M. is a Senior Research Fellow of the NHMRC.

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  1. Queensland Brain Institute, The University of Queensland, Brisbane, QLD, 4072, Australia

    Peter J. Wen, Shona L. Osborne & Frederic A. Meunier

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  1. Peter J. Wen
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  2. Shona L. Osborne
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  3. Frederic A. Meunier
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Correspondence to Frederic A. Meunier .

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  1. CTR DIABETES BARTS, Queen Mary University of London, UK, NEWARK ST 4, LONDON E1 2AT, United Kingdom

    MARCO FALASCA

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© 2012 Springer Science+Business Media Dordrecht

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Wen, P.J., Osborne, S.L., Meunier, F.A. (2012). Phosphoinositides in Neuroexocytosis and Neuronal Diseases. In: FALASCA, M. (eds) Phosphoinositides and Disease. Current Topics in Microbiology and Immunology, vol 362. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-5025-8_4

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