The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Zinc metalloproteinase, ZMPSTE24, is mutated in mandibuloacral dysplasia
Open accessAbstract
Mandibuloacral dysplasia (MAD; OMIM 248370) is a rare, genetically and phenotypically heterogeneous, autosomal recessive disorder characterized by skeletal abnormalities including hypoplasia of the mandible and clavicles, acro-osteolysis, cutaneous atrophy and lipodystrophy. A homozygous missense mutation, Arg527His, in the LMNA gene which encodes nuclear lamina proteins lamins A and C has been reported in patients with MAD and partial lipodystrophy. We studied four patients with MAD who had no mutations in the LMNA gene. We now show compound heterozygous mutations, Phe361fsX379 and Trp340Arg, in the zinc metalloproteinase (ZMPSTE24) gene in one of the four patients who had severe MAD associated with progeroid appearance and generalized lipodystrophy. ZMPSTE24 is involved in post-translational proteolytic cleavage of carboxy terminal residues of farnesylated prelamin A in two steps to form mature lamin A. Deficiency of Zmpste24 in mice causes accumulation of prelamin A and phenotypic features similar to MAD. The yeast homolog, Ste24, has a parallel role in processing of prenylated mating pheromone a-factor. Since human ZMPSTE24 can also process a-factor when expressed in yeast, we assessed the functional significance of the two ZMPSTE24 mutations in the yeast to complement the mating defect of the haploid MATa yeast lacking STE24 and Ras-converting enzyme 1 (RCE1; another prenylprotein-specific endoprotease) genes. The ZMPSTE24 mutant construct, Phe361fsX379, was inactive in complementing the yeast a-factor but the mutant, Trp340Arg, was partially active compared to the wild type ZMPSTE24 construct. We conclude that mutations in ZMPSTE24 may cause MAD by affecting prelamin A processing.
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Cites
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Mandibuloacral Dysplasia Is Caused by a Mutation in LMNA-Encoding Lamin A/C
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Cited by
Genomic instability in laminopathy-based premature aging
Liu, B., Wang, J., Chan, K. M., Tjia, W. M., Deng, W., Guan, X., Huang, J.-D., Li, K. M., Chau, P. Y., Chen, D. J., et al. (2005) · Nature Medicine · doi:10.1038/nm1266 · Cited by 650
Human laminopathies: nuclei gone genetically awry
Capell, B. C., & Collins, F. S. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1906 · Cited by 527
Accelerated ageing in mice deficient in Zmpste24 protease is linked to p53 signalling activation
Varela, I., Cadiñanos, J., Pendás, A. M., Gutiérrez-Fernández, A., Folgueras, A. R., Sánchez, L. M., Zhou, Z., Rodríguez, F. J., Stewart, C. L., Vega, J. A., et al. (2005) · Nature · doi:10.1038/nature04019 · Cited by 466
Capell, B. C., Erdos, M. R., Madigan, J. P., Fiordalisi, J. J., Varga, R., Conneely, K. N., Gordon, L. B., Der, C. J., Cox, A. D., & Collins, F. S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506001102 · Cited by 398
When Lamins Go Bad: Nuclear Structure and Disease
Schreiber, K. H., & Kennedy, B. K. (2013) · Cell · doi:10.1016/j.cell.2013.02.015 · Cited by 391
Metadata
- Authors
- Agarwal, A. K.
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2003-07-01
- Volume
- 12
- Issue
- 16
- Pages
- 1995-2001
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- OpenAlex
- W2137564725
- Cited by
- 401
- References
- 20
- FWCI
- 9.33
- Type
- journal article
- Language
- en
- Open access
- bronze
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