ArticleProceedings of the National Academy of Sciences of the United States of America1992
Nucleoplasmic localization of prelamin A: implications for prenylation-dependent lamin A assembly into the nuclear lamina.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed.
- Protein farnesylation: from molecular mechanisms to therapeutic targeting in cancer, aging, and beyond.Frontiers in pharmacology · 2026Review
- Computational Characterization of Pathogenic LMNA Missense Variants: Structural Instability, Altered Binding, and Conformational Dynamics.Human mutation · 2026Article
- Nuclear and genome dynamics underlying DNA double-strand break repair.Nature reviews. Molecular cell biology · 2025Review
- Roles of the lamin A-specific tail region in the localization to sites of nuclear envelope rupture.PNAS nexus · 2024Article
- Protein Farnesylation on Nasopharyngeal Carcinoma, Molecular Background and Its Potential as a Therapeutic Target.Cancers · 2022Review
- Progerin-Induced Impairment in Wound Healing and Proliferation in Vascular Endothelial Cells.Frontiers in aging · 2022Article
- Lamin post-translational modifications: emerging toggles of nuclear organization and function.Trends in biochemical sciences · 2021Review
- Non-farnesylated B-type lamin can tether chromatin inside the nucleus and its chromatin interaction requires the Ig-fold region.Chromosoma · 2017Article
- Modulation of LMNA splicing as a strategy to treat prelamin A diseases.The Journal of clinical investigation · 2016Article
- Prelamin A processing, accumulation and distribution in normal cells and laminopathy disorders.Nucleus (Austin, Tex.) · 2016Article
- Skin Disease in Laminopathy-Associated Premature Aging.The Journal of investigative dermatology · 2015Review
- Differential roles of the mevalonate pathway in the development and survival of mouse Purkinje cells in culture.Molecular neurobiology · 2015Article
- Unprenylated RhoA contributes to IL-1β hypersecretion in mevalonate kinase deficiency model through stimulation of Rac1 activity.The Journal of biological chemistry · 2014Article
- Calcium causes a conformational change in lamin A tail domain that promotes farnesyl-mediated membrane association.Biophysical journal · 2013Article
- Defective nuclear import of Tpr in Progeria reflects the Ran sensitivity of large cargo transport.The Journal of cell biology · 2013Article
- Targeting protein prenylation in progeria.Science translational medicine · 2013Review
- Nifedipine prevents etoposide-induced caspase-3 activation, prenyl transferase degradation and loss in cell viability in pancreatic β-cells.Apoptosis : an international journal on programmed cell death · 2013Article
- Investigation of splicing changes and post-translational processing of LMNA in sporadic inclusion body myositis.International journal of clinical and experimental pathology · 2013Article
- Potential therapeutic approaches for modulating expression and accumulation of defective lamin A in laminopathies and age-related diseases.Journal of molecular medicine (Berlin, Germany) · 2012Review
- Expression of the Hutchinson-Gilford progeria mutation during osteoblast development results in loss of osteocytes, irregular mineralization, and poor biomechanical properties.The Journal of biological chemistry · 2012Article
10 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
5 authors.
Funding
Abstract
The synthesis of the nuclear lamina protein lamin A requires the prenylation-dependent processing of its precursor protein, prelamin A. Unlike p21ras, which undergoes similar initial posttranslational modifications, maturation of lamin A results in the proteolytic removal of the prenylated portion of the molecule. We have used an in vitro prenylation system to demonstrate the nature of the prenyl substituent on prelamin A to be a farnesyl group. Further, the in vitro farnesylation of prelamin A requires an intact cysteine-aliphatic-aliphatic-other (CAAX) amino acid sequence motif at its carboxyl terminus. The effect of blocking the prenylation of prelamin A on its localization and assembly into the nuclear lamina was investigated by indirect immunofluorescence. Expression of wild-type prelamin A in lovastatin-treated cells showed that nonprenylated prelamin A accumulated as nucleoplasmic particles. Upon addition of mevalonate to lovastatin-treated cells, the wild-type lamin A was incorporated into the lamina within 3 hr. Expression of a mutant lamin A in which the carboxyl-terminal 21 amino acids were deleted resulted in a lamin molecule that was directly assembled into the lamina. These results indicate that the carboxyl-terminal peptide of prelamin A blocks its proper assembly into the nuclear lamina and that the prenylation-initiated removal of this peptide can occur in the nucleus.
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