The DOI matches its Crossref record; 157 of the 157 references it cites were found in a registry or an index.
Biosynthesis and biology of mammalian GPI-anchored proteins
Open accessAbstract
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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Cites
Functional rafts in cell membranes
Simons, K., & Ikonen, E. (1997) · Nature · doi:10.1038/42408 · Cited by 9,757 · cited 1×
“A prominent feature of GPI-APs is their association with membrane microdomains or membrane rafts [5,6].”
BackgroundUniProt: a hub for protein information
The UniProt Consortium (2015) · Nucleic Acids Research · doi:10.1093/nar/gku989 · Cited by 5,106
Wiederschain, G. Y. (2009) · Biochemistry (Moscow) · doi:10.1134/s0006297909090156 · Cited by 4,083
Brown, D. A., & Rose, J. K. (1992) · Cell · doi:10.1016/0092-8674(92)90189-j · Cited by 2,921
GPI-anchored proteins are organized in submicron domains at the cell surface
Varma, R., & Mayor, S. (1998) · Nature · doi:10.1038/29563 · Cited by 1,209
Takeda, J., Miyata, T., Kawagoe, K., Iida, Y., Endo, Y., Fujita, T., Takahashi, M., Kitani, T., & Kinoshita, T. (1993) · Cell · doi:10.1016/0092-8674(93)90250-t · Cited by 1,029
Self-citationGPI-Anchored Cell-Surface Molecules Complexed to Protein Tyrosine Kinases
Štefanová, I., Hořejši, V., Ansotegui, I. J., Knapp, W., & Stockinger, H. (1991) · Science · doi:10.1126/science.1719635 · Cited by 826
Schroeder, R., London, E., & Brown, D. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12130 · Cited by 691
The Cloning of PIG-A, a Component in the Early Step of GPI-Anchor Biosynthesis
Miyata, T., Takeda, J., Iida, Y., Yamada, N., Inoue, N., Takahashi, M., Maeda, K., Kitani, T., & Kinoshita, T. (1993) · Science · doi:10.1126/science.7680492 · Cited by 522
Self-citationTakahashi, C., Sheng, Z., Horan, T. P., Kitayama, H., Maki, M., Hitomi, K., Kitaura, Y., Takai, S., Sasahara, R. M., Horimoto, A., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.22.13221 · Cited by 492
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Zhang, J., Humphreys, I. R., Pei, J., Kim, J., Choi, C., Yuan, R., Durham, J., Liu, S., Choi, H.-J., Baek, M., et al. (2025) · Science · doi:10.1126/science.adt1630 · Cited by 87
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Fossa, S. L., Anton, B. P., Kneller, D. W., Petralia, L. M. C., Ganatra, M. B., Boisvert, M. L., Vainauskas, S., Chan, S.-H., Hokke, C. H., Foster, J. M., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105437 · Cited by 7
Metadata
- Authors
- Kinoshita, T.
- Venue
- Open Biology
- Publisher
- The Royal Society
- 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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