Analysis of a non-lethal biallelic frameshift mutation in ZMPSTE24 reveals utilization of alternative translation initiation codons.

alternative start codon genotype-phenotype correlation lethal restrictive dermopathy mandibuloacral dysplasia mutation analysis progeria variant interpretation

Journal

Clinical genetics
ISSN: 1399-0004
Titre abrégé: Clin Genet
Pays: Denmark
ID NLM: 0253664

Informations de publication

Date de publication:
10 2023
Historique:
revised: 12 05 2023
received: 27 03 2023
accepted: 23 05 2023
medline: 5 9 2023
pubmed: 4 6 2023
entrez: 4 6 2023
Statut: ppublish

Résumé

Restrictive dermopathy (RD) is a lethal condition caused by biallelic loss-of-function mutations in ZMPSTE24, whereas mutations preserving residual enzymatic activity of the ZMPSTE24 protein lead to the milder mandibuloacral dysplasia with type B lipodystrophy (MADB) phenotype. Remarkably, we identified a homozygous, presumably loss-of-function mutation in ZMPSTE24 [c.28_29insA, p.(Leu10Tyrfs*37)] in two consanguineous Pakistani families segregating MADB. To clarify how lethal consequences are prevented in affected individuals, functional analysis was performed. Expression experiments supported utilization of two alternative translation initiation sites, preventing complete loss of protein function consistent with the relatively mild phenotypic outcome in affected patients. One of these alternative start codons is newly formed at the insertion site. Our findings indicate that the creation of new potential start codons through N-terminal mutations in other disease-associated genes should generally be taken into consideration in the variant interpretation process.

Identifiants

pubmed: 37270786
doi: 10.1111/cge.14381
doi:

Substances chimiques

Codon, Initiator 0
Metalloendopeptidases EC 3.4.24.-
monoaminocarboxydihydroborane 98169-69-8
Codon 0
ZMPSTE24 protein, human EC 3.4.24.84
Membrane Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

491-496

Informations de copyright

© 2023 The Authors. Clinical Genetics published by John Wiley & Sons Ltd.

Références

Schmidt WK, Tam A, Fujimura-Kamada K, Michaelis S. Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage. Proc Natl Acad Sci U S A. 1998;95:11175-11180. doi:10.1073/pnas.95.19.11175
Spear ED, Hsu ET, Nie L, Carpenter EP, Hrycyna CA, Michaelis S. ZMPSTE24 missense mutations that cause progeroid diseases decrease prelamin A cleavage activity and/or protein stability. Dis Model Mech. 2018;11. doi:10.1242/dmm.033670
Barrowman J, Wiley PA, Hudon-Miller SE, Hrycyna CA, Michaelis S. Human ZMPSTE24 disease mutations: residual proteolytic activity correlates with disease severity. Hum Mol Genet. 2012;21:4084-4093. doi:10.1093/hmg/dds233
Cenni V, D'Apice MR, Garagnani P, et al. Mandibuloacral dysplasia: a premature ageing disease with aspects of physiological ageing. Ageing Res Rev. 2018;42:1-13. doi:10.1016/j.arr.2017.12.001
Agarwal AK, Fryns JP, Auchus RJ, Garg A. Zinc metalloproteinase, ZMPSTE24, is mutated in mandibuloacral dysplasia. Hum Mol Genet. 2003;12:1995-2001. doi:10.1093/hmg/ddg213
Restrictive dermopathy. Orphanet encyclopedia. 2019 https://www.orpha.net/consor/cgi-bin/OC_Exp.php?lng=EN&Expert=1662
Schaflinger E, Blatterer J, Khan AS, et al. An exceptional biallelic N-terminal frame shift mutation in ZMPSTE24 leads to non-lethal progeria due to possible utilization of a downstream alternative start codon. Gene. 2022;833:146582. doi:10.1016/j.gene.2022.146582
Miyoshi Y, Akagi M, Agarwal AK, et al. Severe mandibuloacral dysplasia caused by novel compound heterozygous ZMPSTE24 mutations in two Japanese siblings. Clin Genet. 2008;73:535-544. doi:10.1111/j.1399-0004.2008.00992.x
Ben Yaou R, Navarro C, Quijano-Roy S, et al. Type B mandibuloacral dysplasia with congenital myopathy due to homozygous ZMPSTE24 missense mutation. Eur J Hum Genet. 2011;19:647-654. doi:10.1038/ejhg.2010.256
Matulevičienė A, Meškienė R, Morkūnienė A, et al. Frame shift mutations of the ZMPSTE24 gene in two siblings with restrictive dermopathy. Clin Dysmorphol. 2016;25:7-11. doi:10.1097/mcd.0000000000000100
Moulson CL, Go G, Gardner JM, et al. Homozygous and compound heterozygous mutations in ZMPSTE24 cause the laminopathy restrictive dermopathy. J Invest Dermatol. 2005;125:913-919. doi:10.1111/j.0022-202X.2005.23846.x

Auteurs

Lukas Kaufmann (L)

Diagnostic and Research Institute of Human Genetics, Medical University of Graz, Graz, Austria.

Johannes Pilic (J)

Gottfried Schatz Research Center, Department of Molecular Biology and Biochemistry, Medical University of Graz, Graz, Austria.

Lisa Auinger (L)

Division of Haematology, Medical University of Graz, Graz, Austria.

Anna-Lena Mayer (AL)

Diagnostic and Research Institute of Human Genetics, Medical University of Graz, Graz, Austria.

Jasmin Blatterer (J)

Diagnostic and Research Institute of Human Genetics, Medical University of Graz, Graz, Austria.

Johann Semmler-Bruckner (J)

Neurogenetics Laboratory, Department of Neurology, Medical University of Graz, Graz, Austria.

Safdar Abbas (S)

Gomal Centre of Biochemistry and Biotechnology, Gomal University, Dera Ismail Khan, Pakistan.

Khurram Rehman (K)

Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Gomal University, Dera Ismail Khan, Pakistan.

Muhammad Ayaz (M)

Department of Biological Sciences, Gomal University, Dera Ismail Khan, Pakistan.

Wolfgang F Graier (WF)

Gottfried Schatz Research Center, Department of Molecular Biology and Biochemistry, Medical University of Graz, Graz, Austria.
BioTechMed Graz, Graz, Austria.

Roland Malli (R)

Gottfried Schatz Research Center, Department of Molecular Biology and Biochemistry, Medical University of Graz, Graz, Austria.
BioTechMed Graz, Graz, Austria.

Erwin Petek (E)

Diagnostic and Research Institute of Human Genetics, Medical University of Graz, Graz, Austria.

Klaus Wagner (K)

Diagnostic and Research Institute of Human Genetics, Medical University of Graz, Graz, Austria.

Ali Al Kaissi (A)

Pediatric Orthopedic Department, Speising Hospital, Vienna, Austria.

Muzammil Ahmad Khan (MA)

Gomal Centre of Biochemistry and Biotechnology, Gomal University, Dera Ismail Khan, Pakistan.

Christian Windpassinger (C)

Diagnostic and Research Institute of Human Genetics, Medical University of Graz, Graz, Austria.
Neurogenetics Laboratory, Department of Neurology, Medical University of Graz, Graz, Austria.

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Lisanne N van Merendonk, Kübra Akgöl, Bastiaan Nuijen
1.00
Humans Antineoplastic Agents Administration, Oral Drug Costs Counterfeit Drugs

Smoking Cessation and Incident Cardiovascular Disease.

Jun Hwan Cho, Seung Yong Shin, Hoseob Kim et al.
1.00
Humans Male Smoking Cessation Cardiovascular Diseases Female
Humans United States Aged Cross-Sectional Studies Medicare Part C
1.00
Humans Yoga Low Back Pain Female Male

Classifications MeSH