Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Deficiency in ZMPSTE24 and resulting farnesyl-prelamin A accumulation only modestly affect mouse adipose tissue stores.

Journal of lipid research - 1 Mar 2020

Heizer Patrick J, Yang Ye, Tu Yiping, Kim Paul H, Chen Natalie Y, Hu Yan, Yoshinaga Yuko, de Jong Pieter J, Vergnes Laurent, Morales Jazmin E, Li Robert L, Jackson Nicholas, Reue Karen, Young Stephen G, Fong Loren G

Abstract excerpt

Zinc metallopeptidase STE24 (ZMPSTE24) is essential for the conversion of farnesyl-prelamin A to mature lamin A, a key component of the nuclear lamina. In the absence of ZMPSTE24, farnesyl-prelamin A accumulates in the nucleus and exerts toxicity, causing a variety of disease phenotypes. By ∼4 months of age, both male and female Zmpste24-/- mice manifest a near-complete loss of adipose tissue, but it has never...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adipose Tissue
Share to Cell Nucleus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lamin Type A

Share to Membrane Proteins

Share to Metalloendopeptidases

Share to Mice, Knockout

Share to Mice, Transgenic

Source

Open in PubMed Open full text

Identifiers

PMID: 31941672
DOI: 10.1194/jlr.RA119000593
PMCID: PMC7053845

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Deficiency in ZMPSTE24 and resulting farnesyl-prelamin A accumulation only modestly affect mouse adipose tissue stores.PMID 31941672Read ↗

Proteomic Profiling of Adipose Tissue from Zmpste24−/− Mice, a Model of Lipodystrophy and Premature Aging, Reveals Major Changes in Mitochondrial Function and Vimentin ProcessingSemantic proximity Read ↗

Defective prelamin A processing and muscular and adipocyte alterations in Zmpste24 metalloproteinase-deficient mice.Semantic proximity Read ↗

Abolishing the prelamin A ZMPSTE24 cleavage site leads to progeroid phenotypes with near-normal longevity in miceSemantic proximity Read ↗

Abolishing the prelamin A ZMPSTE24 cleavage site leads to progeroid phenotypes with near-normal longevity in mice.Semantic proximity Read ↗

Zmpste24 deficiency in mice causes spontaneous bone fractures, muscle weakness, and a prelamin A processing defect.Semantic proximity Read ↗

Reduced ZMPSTE24 expression leads to prelamin accumulation and development of steatosis in MASLD patientsSemantic proximity Read ↗

Deletion of Trim28 in committed adipocytes promotes obesity but preserves glucose tolerance.Semantic proximity Read ↗

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

Requirements for efficient proteolytic cleavage of prelamin A by ZMPSTE24.Semantic proximity Read ↗

Compound heterozygous ZMPSTE24 mutations reduce prelamin A processing and result in a severe progeroid phenotype.Semantic proximity Read ↗

Defining Substrate Requirements for Cleavage of Farnesylated Prelamin A by the Integral Membrane Zinc Metalloprotease ZMPSTE24Semantic proximity Read ↗

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

⌁Select a neighboring publication to make it the new centre.