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Article

Peters plus syndrome mutations disrupt a noncanonical ER quality-control mechanism.

Current biology : CB - 2 Feb 2015

Vasudevan Deepika, Takeuchi Hideyuki, Johar Sumreet Singh, Majerus Elaine, Haltiwanger Robert S

Abstract excerpt

BACKGROUND: O-fucose is added to cysteine-rich domains called thrombospondin type 1 repeats (TSRs) by protein O-fucosyltransferase 2 (POFUT2) and is elongated with glucose by β3-glucosyltransferase (B3GLCT). Mutations in B3GLCT result in Peters plus syndrome (PPS), an autosomal recessive disorder characterized by eye and other developmental defects. Although 49 putative targets are known, the function of the...

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Source

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Identifiers

PMID: 25544610
DOI: 10.1016/j.cub.2014.11.049
PMCID: PMC4318717

Genes

POFUT2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Peters plus syndrome mutations disrupt a noncanonical ER quality-control mechanism.PMID 25544610Read ↗

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Peters plus syndrome mutations affect the function and stability of human β1,3-glucosyltransferase.Semantic proximity Read ↗

Peters Plus syndrome is a new congenital disorder of glycosylation and involves defective Omicron-glycosylation of thrombospondin type 1 repeats.Semantic proximity Read ↗

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