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Biosynthesis and biology of mammalian GPI-anchored proteins

Open access
Kinoshita, Taroh·2020·Open Biology

Abstract

At least 150 human proteins are glycosylphosphatidylinositol-anchored proteins (GPI-APs). The protein moiety of GPI-APs lacking transmembrane domains is anchored to the plasma membrane with GPI covalently attached to the C-terminus. The GPI consists of the conserved core glycan, phosphatidylinositol and glycan side chains. The entire GPI-AP is anchored to the outer leaflet of the lipid bilayer by insertion of fatty chains of phosphatidylinositol. Because of GPI-dependent membrane anchoring, GPI-APs have some unique characteristics. The most prominent feature of GPI-APs is their association with membrane microdomains or membrane rafts. In the polarized cells such as epithelial cells, many GPI-APs are exclusively expressed in the apical surfaces, whereas some GPI-APs are preferentially expressed in the basolateral surfaces. Several GPI-APs act as transcytotic transporters carrying their ligands from one compartment to another. Some GPI-APs are shed from the membrane after cleavage within the GPI by a GPI-specific phospholipase or a glycosidase. In this review, I will summarize the current understanding of GPI-AP biosynthesis in mammalian cells and discuss examples of GPI-dependent functions of mammalian GPI-APs.

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Metadata

Authors
Kinoshita, T.
Venue
Open Biology
Published
2020-03
Volume
10
Issue
3
Pages
190290-190290
ISSN
2046-2441 (ISSN-L)
OpenAlex
W3012101911
Cited by
341
References
157
FWCI
16.21
Type
journal article
Language
en
Open access
gold

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CoChat. (2026). Citation check: Biosynthesis and biology of mammalian GPI-anchored proteins. https://app.cochat.ai/papers/10.1098/rsob.190290
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Kinoshita, T. (2020). Biosynthesis and biology of mammalian GPI-anchored proteins. Open Biology. https://doi.org/10.1098/rsob.190290

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