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. 1993 May 1;90(9):3973–3977. doi: 10.1073/pnas.90.9.3973

Evidence that the putative COOH-terminal signal transamidase involved in glycosylphosphatidylinositol protein synthesis is present in the endoplasmic reticulum.

R Amthauer 1, K Kodukula 1, L Gerber 1, S Udenfriend 1
PMCID: PMC46428  PMID: 8387204

Abstract

Nascent proteins destined to be processed to a glycosylphosphatidylinositol (GPI)-anchored membrane form contain NH2-terminal and COOH-terminal signal peptides. The first directs a nascent protein into the endoplasmic reticulum; the second peptide targets the protein to a putative COOH-terminal signal transamidase where cleavage of the peptide and addition of the GPI anchor occur. We recently showed that ATP hydrolysis is required for maturation of GPI proteins at a stage prior to transamidation. Here we show that one of the ATP-requiring proteins involved in processing of GPI-anchored proteins in the endoplasmic reticulum is the immunoglobulin heavy chain binding protein (BiP; GRP 78). This and related findings indicate that GPI transamidase is localized in the endoplasmic reticulum.

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