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Glycosyl‐phosphatidylinositol: a versatile anchor for cell surface proteins 1

Low, Martin G.·1989·The FASEB Journal

Abstract

Covalent linkage of proteins to glycosyl‐phosphatidylinositol (GPI) molecules is now recognized as an important mechanism for anchoring proteins to membranes. Recent structural work on the GPI anchors indicates that the structure of the glycan connecting the protein and the phosphatidylinositol molecule has been conserved during evolution. Attachment of the protein to the GPI molecule is directed by a signal sequence at the COOH terminus of the polypeptide that is removed during the attachment process. Alternative processing of the same RNA transcript may lead to mRNA species encoding for the same protein but not utilizing GPI for membrane anchoring. One function of the GPI anchor may be to offer a site for degradation by specific endogenous phospholipases with release of the protein from the cell surface. The products of GPI anchor degradation may also have biological activity and be involved in cell communication. Although the physiological role of these events is not certain, the available evidence suggests that the GPI anchors play a dynamic and versatile role in the regulation of cell surface protein expression.— Low, M. G. Glycosyl‐phosphatidylinositol: a versatile anchor for cell surface proteins. FASEB J. 3: 1600‐1608; 1989.

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Metadata

Authors
Low, M. G.
Venue
The FASEB Journal
Publisher
Wiley
Published
1989-03
Volume
3
Issue
5
Pages
1600-1608
ISSN
  • 0892-6638 (ISSN-L)
  • 1530-6860
OpenAlex
W1580141785
Cited by
267
References
0
FWCI
13.64
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Glycosyl‐phosphatidylinositol: a versatile anchor for cell surface proteins 1. https://app.cochat.ai/papers/10.1096/fasebj.3.5.2522071
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Low, M. G. (1989). Glycosyl‐phosphatidylinositol: a versatile anchor for cell surface proteins 1. The FASEB Journal. https://doi.org/10.1096/fasebj.3.5.2522071

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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