Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan-anchored membrane proteins determined by site-specific mutagenesis at Asp-484 of placental alkaline phosphatase.

doi:10.1073/pnas.87.1.157

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Article

Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan-anchored membrane proteins determined by site-specific mutagenesis at Asp-484 of placental alkaline phosphatase.

Proceedings of the National Academy of Sciences of the United States of America - 1 Jan 1990

Micanovic R, Gerber L D, Berger J, Kodukula K, Udenfriend S

Abstract excerpt

Many proteins are now known to be anchored to the plasma membrane by a phosphatidylinositol-glycan (PI-G) moiety that is attached to their COOH termini. Placental alkaline phosphatase (PLAP) has been used as a model for investigating mechanisms involved in the COOH-terminal processing of PI-G-tai...

Topics

Alkaline Phosphatase
Amino Acid Sequence
Animals
Aspartic Acid
Bromelains
Cell Line
Ethanolamine
Ethanolamines
Female
Glycosylphosphatidylinositols
Humans
Isoenzymes
Membrane Proteins
Molecular Sequence Data

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Phosphatidylinositol Diacylglycerol-Lyase

Phosphatidylinositols

Phosphoric Diester Hydrolases

Source

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Identifiers

PMID: 2153284
DOI: 10.1073/pnas.87.1.157
PMCID: PMC53219

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-2153284-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.