GPI-anchored protein cleavage in the regulation of transmembrane signals.
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.
Sharom
Frances J
FJ
Department of Chemistry and Biochemistry, University of Guelph, Guelph, Ontario, N1G 2W1 Canada.
Radeva
Galina
G
D000818:Animals; D002450:Cell Communication; D002462:Cell Membrane / Q000502:physiology*; D017261:Glycosylphosphatidylinositols / Q000502:physiology*; D006801:Humans; D021962:Membrane Microdomains / Q000502:physiology*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D010740:Phospholipases / Q000378:metabolism; D011487:Protein Conformation; D015398:Signal Transduction / Q000502:physiology*
D017261:Glycosylphosphatidylinositols; D008565:Membrane Proteins; D010740:Phospholipases