Methods to Study GPI Anchoring of Proteins

Varma, Yug; Hendrickson, Tamara L.

doi:10.1002/cbic.200900704

Cited by 21 publications

(16 citation statements)

References 127 publications

(205 reference statements)

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“…Three putative GPI-anchored proteins were identified in this study, one from mycelial cell wall fractions and two from mycelial membranes, suggesting that proteins are attached to the plasma membrane, or cell wall, in this manner in P. infestans. GPI-anchored proteins have been identified in Triton X-114 phase partitioning experiments (Hooper & Bashir 1991), however, more recently, methods have been developed to incorporate the use of multiple enzymatic steps for the specific cleavage of the GPI anchor into these protocols (Varma & Hendrickson 2010). Therefore, the future identification of further GPI-anchored proteins in P. infestans may require methods that seek to specifically enrich for these proteins or to cleave them from the membrane.…”

Section: Discussionmentioning

confidence: 99%

Identification of appressorial and mycelial cell wall proteins and a survey of the membrane proteome of Phytophthora infestans

Grenville‐Briggs

Avrova²,

Hay

et al. 2010

Fungal Biology

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Section: Discussionmentioning

confidence: 99%

Identification of appressorial and mycelial cell wall proteins and a survey of the membrane proteome of Phytophthora infestans

Grenville‐Briggs

Avrova²,

Hay

et al. 2010

Fungal Biology

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“…Sensitivity to bacterial phosphoinositol-specific phospholipase C (PI-PLC) is frequently used as a diagnostic tool for GPI anchoring (Varma and Hendrickson, 2010). Treatment with PI-PLC did not release MMPnat from membranes, thus failing to provide direct evidence for GPI anchoring (Fig.…”

Section: Cloning Of Sl2-mmp and Sl3-mmpmentioning

confidence: 99%

Cell death control by matrix metalloproteinases in tomato

et al. 2016

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In contrast to mammalian matrix metalloproteinases (MMPs) that play important roles in the remodeling of the extracellular matrix in animals, the proteases responsible for dynamic modifications of the plant cell wall are largely unknown. A possible involvement of MMPs was addressed by cloning and functional characterization of Sl2-MMP and Sl3-MMP from tomato (Solanum lycopersicum). The two tomato MMPs were found to resemble mammalian homologs with respect to gelatinolytic activity, substrate preference for hydrophobic amino acids on both sides of the scissile bond, and catalytic properties. In transgenic tomato seedlings silenced for Sl2/3-MMP expression, necrotic lesions were observed at the base of the hypocotyl. Cell death initiated in the epidermis and proceeded to include outer cortical cell layers. In later developmental stages, necrosis spread, covering the entire stem and extending into the leaves of MMP-silenced plants. The subtilisin-like protease P69B was identified as a substrate of Sl2-and Sl3-MMP. P69B was shown to colocalize with Sl-MMPs in the apoplast of the tomato hypocotyl, it exhibited increased stability in transgenic plants silenced for Sl-MMP activity, and it was cleaved and inactivated by Sl-MMPs in vitro. The induction of cell death in Sl2/3-MMP-silenced plants depended on P69B, indicating that Sl2-and Sl3-MMP act upstream of P69B in an extracellular proteolytic cascade that contributes to the regulation of cell death in tomato.

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“…3). 1,13) After protein-attachment, GPI-APs are structurally remodeled at both lipid and glycan parts of GPI, recruited into COPII-coated transport vesicles at the ER exit sites, transported to the Golgi, further modified in the lipid part of GPI, and finally expressed on the cell surface (Fig. 4).…”

Section: Introductionmentioning

confidence: 99%

Biosynthesis and deficiencies of glycosylphosphatidylinositol

Kinoshita

2014

Proc. Jpn. Acad., Ser. B

123

111

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At least 150 different human proteins are anchored to the outer leaflet of the plasma membrane via glycosylphosphatidylinositol (GPI). GPI preassembled in the endoplasmic reticulum is attached to the protein’s carboxyl-terminus as a post-translational modification by GPI transamidase. Twenty-two PIG (for Phosphatidyl Inositol Glycan) genes are involved in the biosynthesis and protein-attachment of GPI. After attachment to proteins, both lipid and glycan moieties of GPI are structurally remodeled in the endoplasmic reticulum and Golgi apparatus. Four PGAP (for Post GPI Attachment to Proteins) genes are involved in the remodeling of GPI. GPI-anchor deficiencies caused by somatic and germline mutations in the PIG and PGAP genes have been found and characterized. The characteristics of the 26 PIG and PGAP genes and the GPI deficiencies caused by mutations in these genes are reviewed.

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Methods to Study GPI Anchoring of Proteins

Cited by 21 publications

References 127 publications

Identification of appressorial and mycelial cell wall proteins and a survey of the membrane proteome of Phytophthora infestans

Identification of appressorial and mycelial cell wall proteins and a survey of the membrane proteome of Phytophthora infestans

Cell death control by matrix metalloproteinases in tomato

Biosynthesis and deficiencies of glycosylphosphatidylinositol

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