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Article

Human ZMPSTE24 disease mutations: residual proteolytic activity correlates with disease severity.

Human molecular genetics - 15 Sept 2012

Barrowman Jemima, Wiley Patricia A, Hudon-Miller Sarah E, Hrycyna Christine A, Michaelis Susan

Abstract excerpt

The zinc metalloprotease ZMPSTE24 plays a critical role in nuclear lamin biology by cleaving the prenylated and carboxylmethylated 15-amino acid tail from the C-terminus of prelamin A to yield mature lamin A. A defect in this proteolytic event, caused by a mutation in the lamin A gene (LMNA) that eliminates the ZMPSTE24 cleavage site, underlies the premature aging disease Hutchinson-Gilford Progeria Syndrome...

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Source

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Identifiers

PMID: 22718200
DOI: 10.1093/hmg/dds233
PMCID: PMC3428156

Genes

ZMPSTE24
LMNA

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Human ZMPSTE24 disease mutations: residual proteolytic activity correlates with disease severity.PMID 22718200Read ↗

ZMPSTE24 missense mutations that cause progeroid diseases decrease prelamin A cleavage activity and/or protein stability.Semantic proximity Read ↗

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Zinc metalloproteinase, ZMPSTE24, is mutated in mandibuloacral dysplasia.Semantic proximity Read ↗

A homozygous ZMPSTE24 null mutation in combination with a heterozygous mutation in the LMNA gene causes Hutchinson-Gilford progeria syndrome (HGPS): insights into the pathophysiology of HGPS.Semantic proximity Read ↗

Heterozygosity for Lmna deficiency eliminates the progeria-like phenotypes in Zmpste24-deficient mice.Semantic proximity Read ↗

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