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Review article

Inositol lipid phosphatases in membrane trafficking and human disease

Peter G. Billcliff, Martin Lowe
Biochemical Journal Jun 26, 2014, 461 (2) 159-175; DOI: 10.1042/BJ20140361
Peter G. Billcliff
Faculty of Life Sciences, University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, U.K.
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Martin Lowe
Faculty of Life Sciences, University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, U.K.
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  • For correspondence: martin.lowe@manchester.ac.uk
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Abstract

The specific interaction of phosphoinositides with proteins is critical for a plethora of cellular processes, including cytoskeleton remodelling, mitogenic signalling, ion channel regulation and membrane traffic. The spatiotemporal restriction of different phosphoinositide species helps to define compartments within the cell, and this is particularly important for membrane trafficking within both the secretory and endocytic pathways. Phosphoinositide homoeostasis is tightly regulated by a large number of inositol kinases and phosphatases, which respectively phosphorylate and dephosphorylate distinct phosphoinositide species. Many of these enzymes have been implicated in regulating membrane trafficking and, accordingly, their dysregulation has been linked to a number of human diseases. In the present review, we focus on the inositol phosphatases, concentrating on their roles in membrane trafficking and the human diseases with which they have been associated.

  • endocytosis
  • human disease
  • inositol phosphatase
  • membrane traffic
  • phosphoinositide
  • secretory pathway

Abbreviations: Aβ, amyloid β-peptide; AD, Alzheimer’s disease; ALS, amyotrophic lateral sclerosis; AP, adaptor protein; CCP, clathrin-coated pit; CMT, Charcot–Marie–Tooth; EGFR, epidermal growth factor receptor; ER, endoplasmic reticulum; ERGIC, endoplasmic reticulum–Golgi intermediate compartment; GLUT4, glucose transporter type 4; INPP4, inositol polyphosphate 4-phosphatase; INPP5, inositol polyphosphate 5-phosphatase; LAMP2, lysosome-associated membrane protein 2; MORM, mental retardation, truncal obesity, retinal dystrophy and micropenis; MTM, myotubularin; MTMR, myotubularin-related; MVB, multivesicular body; NMDAR, N-methyl-D-aspartate receptor; OCRL, oculocerebrorenal syndrome of Lowe; PI3K, phosphoinositide 3-kinase; PIPP, proline-rich inositol polyphosphate 5-phosphatase; PM, plasma membrane; PTEN, phosphatase and tensin homologue deleted on chromosome 10; SAC, suppressor of actin; SH2, Src homology 2; SHIP, SH2 domain-containing inositol 5-phosphatase; SKIP, skeletal muscle and kidney inositol phosphatase; SNP, single nucleotide polymorphism; SNX9, sorting nexin 9; SYNJ, synaptojanin; TGN, trans-Golgi network; TMEM55, transmembrane protein 55; T-tubule, transverse tubule; Vps, vacuolar protein sorting; XLCNM, X-linked recessive form of centronuclear myopathy; YVS, Yunis–Varón syndrome

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July 2014

Volume: 461 Issue: 2

Biochemical Journal: 461 (2)
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Inositol lipid phosphatases in membrane trafficking and human disease
Peter G. Billcliff, Martin Lowe
Biochemical Journal Jul 2014, 461 (2) 159-175; DOI: 10.1042/BJ20140361
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Inositol lipid phosphatases in membrane trafficking and human disease
Peter G. Billcliff, Martin Lowe
Biochemical Journal Jul 2014, 461 (2) 159-175; DOI: 10.1042/BJ20140361

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  • Article
    • Abstract
    • INTRODUCTION
    • PHOSPHOINOSITIDES AND MEMBRANE TRAFFIC
    • INOSITOL POLYPHOSPHATE 3-PHOSPHATASES
    • INOSITOL POLYPHOSPHATE 4-PHOSPHATASES
    • INOSITOL POLYPHOSPHATE 5-PHOSPHATASES
    • SAC PHOSPHATASES
    • BACTERIAL EXPLOITATION OF INOSITOL PHOSPHATASES
    • CONCLUDING REMARKS
    • FUNDING
    • Acknowledgments
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Keywords

endocytosis
human disease
inositol phosphatase
membrane traffic
phosphoinositide
secretory pathway

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