EMERGING FUNCTIONAL ROLES FOR THE GLYCOSYL-PHOSPHATIDYLINOSITOL MEMBRANE-PROTEIN ANCHOR

被引:96
作者
LISANTI, MP [1 ]
RODRIGUEZBOULAN, E [1 ]
SALTIEL, AR [1 ]
机构
[1] ROCKEFELLER UNIV,MOLEC ONCOL LAB,NEW YORK,NY 10021
关键词
cell surface polarity; hormone action; lateral mobility; phospholipase;
D O I
10.1007/BF01871561
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. © 1990 Springer-Verlag New York Inc.
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页码:1 / 10
页数:10
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