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GPI-anchored Protein Cleavage in the Regulation of Transmembrane Signals

  • Chapter
Membrane Dynamics and Domains

Part of the book series: Subcellular Biochemistry ((SCBI,volume 37))

Abstract

The structure of covalently-linked glycosylphosphatidylinositol (GPI) anchors of membrane proteins displayed on the cell surface is described. Evidence of how the GPI-anchors are sorted into membrane rafts in the plasma membrane is reviewed. Proteins are released by hydrolysis of the linkage to the GPI anchor and phospholipases from different sources involved in this process are characterised. The regulation of protein conformation and function resulting from phospholipase cleavage of the GPI anchor is discussed in the context of its role in signal transduction by insulin. In this signalling system, re-distribution of critical membrane components, including GPI-anchored proteins and non-receptor tyrosine kinases, between different raft domains appears to play a central role in the signal transduction pathway.

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  1. Department of Chemistry and Biochemistry, University of Guelph, Guelph, Ontario, N1G 2W1, Canada

    Frances J. Sharom & Galina Radeva

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    Peter J. Quinn

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Sharom, F.J., Radeva, G. (2004). GPI-anchored Protein Cleavage in the Regulation of Transmembrane Signals. In: Quinn, P.J. (eds) Membrane Dynamics and Domains. Subcellular Biochemistry, vol 37. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-5806-1_9

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