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Emerging functional roles for the glycosyl-phosphatidylinositol membrane protein anchor

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Conclusion

Experimental evidence has accumulated over the past few years to suggest that the GPI protein anchor may play a broad role in the regulation of membrane protein function. The significant changes in the biophysical properties of proteins that are membrane-anchored through GPI in lieu of a hydrophobic transmembrane peptide indicates a variety phobic transmembrane peptide indicates a variety of potential new functions served by the anchor structure itself. Moreover, the number of structural variations within the family of GPI molecules indicates a further opportunity for subspecialization of such anchored proteins, especially regarding cellular localization, mobility, metabolism and susceptibility to enzymatically-induced release. It is likely that further exploration of the structure and function of the GPI anchor may reveal additional roles for this unusual mechanism of membrane-protein attachment.

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  1. Department of Cell Biology and Anatomy, Cornell University Medical College, New York, New York

    Michael P. Lisanti & Enrique Rodriguez-Boulan

  2. Laboratory of Molecular Oncology, Rockefeller University, 10021, New York, New York

    Alan R. Saltiel

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Lisanti, M.P., Rodriguez-Boulan, E. & Saltiel, A.R. Emerging functional roles for the glycosyl-phosphatidylinositol membrane protein anchor. J. Membrain Biol. 117, 1–10 (1990). https://doi.org/10.1007/BF01871561

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