Cell-Surface Anchoring of Proteins Via Glycosyl-Phosphatidylinositol Structures

A class of membrane molecules has been identified whose primary translation product includes a COOH-terminal protein sequence that signals attachment of a glycosyl-phosphatidylinositol anchor at a COOH-terminal residue that is newly formed by cleavage of the signaling sequence. This class includes a...

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Bibliographic Details
Published in:	Annual review of biochemistry Vol. 57; no. 1; pp. 285 - 320
Main Authors:	Ferguson, M A J, Williams, A F
Format:	Journal Article
Language:	English
Published:	Palo Alto, CA 94303-0139 Annual Reviews 01-01-1988 4139 El Camino Way, P.O. Box 10139 USA
Subjects:	Animals Biological and medical sciences Cell coat. Cell surface Cell Membrane - metabolism Cell structures and functions Fundamental and applied biological sciences. Psychology Humans Membrane Proteins - physiology Molecular and cellular biology Phosphatidylinositols - physiology Enzyme Cleavage site Article Biosynthesis Cell surface Glycolipid Ripening Phosphatidylinositol Phospholipase Endocytosis Transportation problem Dynamics Plasma membrane Anchoring
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Summary:	A class of membrane molecules has been identified whose primary translation product includes a COOH-terminal protein sequence that signals attachment of a glycosyl-phosphatidylinositol anchor at a COOH-terminal residue that is newly formed by cleavage of the signaling sequence. This class includes a wide diversity of protein types from eukaryotes at many stages of evolution. The structures of the glycosyl-phosphatidylinositol anchors are being resolved, but their functions aside from membrane attachment and dynamics remain to be determined.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1
ISSN:	0066-4154 1545-4509
DOI:	10.1146/annurev.bi.57.070188.001441