Glycosylphosphatidylinositol (GPI)-Anchored Proteins.

Ikezawa, Hiroh

doi:10.1248/bpb.25.409

Cited by 286 publications

(205 citation statements)

References 71 publications

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“…The length and the hydrophobic character of the tail, rather than its specific sequence, therefore seem to be relevant for GPI anchoring (Ikezawa, 2002). Consistent with this, Coyne et al (1993) showed GPI modification of a truncated protein with a synthetic tail of at least 11 Leu residues, whereas introduction of a single charge in the middle of the hydrophobic tail blocks GPI anchoring (Nuoffer et al, 1991).…”

Section: Introductionmentioning

confidence: 92%

Genome‐wide identification of fungal GPI proteins

Groot

Hellingwerf

Klis

2003

Yeast

254

283

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Glycosylphosphatidylinositol-modified (GPI) proteins share structural features that allow their identification using a genomic approach. From the known S. cerevisiae and C. albicans GPI proteins, the following consensus sequence for the GPI attachment site and its downstream region was derived: This consensus sequence, which recognized known GPI proteins from various fungi, was used to screen the genomes of the yeasts S. cerevisiae, C. albicans, Sz. pombe and the filamentous fungus N. crassa for putative GPI proteins. The subsets of proteins so obtained were further screened for the presence of an N-terminal signal sequence for the secretion and absence of internal transmembrane domains. In this way, we identified 66 putative GPI proteins in S. cerevisiae. Some of these are known GPI proteins that were not identified by earlier genomic analyses, indicating that this selection procedure renders a more complete image of the S. cerevisiae GPI proteome. Using the same approach, 104 putative GPI proteins were identified in the human pathogen C. albicans. Among these were the proteins Gas/Phr, Ecm33, Crh and Plb, all members of GPI protein families that are also present in S. cerevisiae. In addition, several proteins and protein families with no significant homology to S. cerevisiae proteins were identified, including the cell wallassociated Als, Csa1/Rbt5, Hwp1/Rbt1 and Hyr1 protein families. In Sz. pombe, which has a low level of (galacto)mannan in the cell wall compared to C. albicans and S. cerevisiae, only 33 GPI candidates were identified and in N. crassa 97. BLAST searches revealed that about half of the putative GPI proteins that were identified in Sz. pombe and N. crassa are homologous to known or putative GPI proteins from other fungi. We conclude that our algorithm is selective and can also be used for GPI protein identification in other fungi.

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Section: Introductionmentioning

confidence: 92%

Genome‐wide identification of fungal GPI proteins

Groot

Hellingwerf

Klis

2003

Yeast

254

283

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“…GPI anchoring can confer localized or polarized targeting and therefore can dramatically alter the functional properties of proteins. In animals, GPIanchored proteins (GAPs) include a broad range of cell surface proteins, such as enzymes, receptors, complement regulators, and adhesion molecules (Ikezawa, 2002). In plants, GAPs form a relatively abundant class of proteins present in the plasma membrane (Sherrier et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

“…GPI anchors are synthesized in the endoplasmic reticulum via the sequential addition of monosaccharides, fatty acids, and phosphoethanolamines to phosphatidylinositol (reviewed by Schultz et al, 2000;Ikezawa, 2002). The proteins that catalyze this pathway have been well studied in mammalian cells, yeast, and protozoa, but essentially nothing is known about them in plants.…”

Section: Introductionmentioning

confidence: 99%

SETH1andSETH2, Two Components of the Glycosylphosphatidylinositol Anchor Biosynthetic Pathway, Are Required for Pollen Germination and Tube Growth in Arabidopsis [W]

et al. 2004

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Glycosylphosphatidylinositol (GPI) anchoring provides an alternative to transmembrane domains for anchoring proteins to the cell surface in eukaryotes. GPI anchors are synthesized in the endoplasmic reticulum via the sequential addition of monosaccharides, fatty acids, and phosphoethanolamines to phosphatidylinositol. Deficiencies in GPI biosynthesis lead to embryonic lethality in animals and to conditional lethality in eukaryotic microbes by blocking cell growth, cell division, or morphogenesis. We report the genetic and phenotypic analysis of insertional mutations disrupting SETH1 and SETH2 , which encode Arabidopsis homologs of two conserved proteins involved in the first step of the GPI biosynthetic pathway. seth1 and seth2 mutations specifically block male transmission and pollen function. This results from reduced pollen germination and tube growth, which are associated with abnormal callose deposition. This finding suggests an essential role for GPI anchor biosynthesis in pollen tube wall deposition or metabolism. Using transcriptomic and proteomic approaches, we identified 47 genes that encode potential GPI-anchored proteins that are expressed in pollen and demonstrated that at least 11 of these proteins are associated with pollen membranes by GPI anchoring. Many of the identified candidate proteins are homologous with proteins involved in cell wall synthesis and remodeling or intercellular signaling and adhesion, and they likely play important roles in the establishment and maintenance of polarized pollen tube growth.

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“…A huge and sometimes confusing array of proteins bind to inositol phosphatides, perhaps the most wellknown of which are glycosylphosphatidylinositol (GPI)-anchored proteins (19). Certain GPI-anchored proteins, such as Thy-1 and CD59, are incorporated into the HIV-1 virion during budding of the virus from lipid rafts (24).…”

mentioning

confidence: 99%

Monoclonal Antibodies to Phosphatidylinositol Phosphate Neutralize Human Immunodeficiency Virus Type 1: Role of Phosphate-Binding Subsites

Brown

Karasavvas

Beck

et al. 2007

J Virol

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Both a murine monoclonal antibody to phosphatidylinositol phosphate (PIP) and a human monoclonal antibody (4E10) that is known to have broadly neutralizing capabilities against primary isolates of human immunodeficiency virus type 1 (HIV-1) bound to PIP, as determined by enzyme-linked immunosorbent assay. Each of the antibodies had antigen subsite binding specificities in aqueous medium for small phosphatecontaining molecules and for inositol. The anti-PIP monoclonal antibody inhibited infection by two HIV-1 primary isolates in neutralization assays employing primary human peripheral blood mononuclear cells. The data suggest that PIP or related lipids having free phosphates could serve as targets for the neutralization of HIV-1.

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Glycosylphosphatidylinositol (GPI)-Anchored Proteins.

Cited by 286 publications

References 71 publications

Genome‐wide identification of fungal GPI proteins

Genome‐wide identification of fungal GPI proteins

SETH1andSETH2, Two Components of the Glycosylphosphatidylinositol Anchor Biosynthetic Pathway, Are Required for Pollen Germination and Tube Growth in Arabidopsis [W]

Monoclonal Antibodies to Phosphatidylinositol Phosphate Neutralize Human Immunodeficiency Virus Type 1: Role of Phosphate-Binding Subsites

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