Emerging functional roles for the glycosyl-phosphatidylinositol membrane protein anchor |
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Authors: | Michael P. Lisanti Enrique Rodriguez-Boulan Alan R. Saltiel |
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Affiliation: | (1) Department of Cell Biology and Anatomy, Cornell University Medical College, New York, New York;(2) Laboratory of Molecular Oncology, Rockefeller University, 10021 New York, New York |
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Abstract: | 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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Keywords: | phospholipase cell surface polarity lateral mobility hormone action |
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