ArticleBiophysical journal2013
Calcium causes a conformational change in lamin A tail domain that promotes farnesyl-mediated membrane association.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Nuclear Mechanotransduction in Skeletal Muscle.Cells · 2021Review
- Lamin microaggregates lead to altered mechanotransmission in progerin-expressing cells.Nucleus (Austin, Tex.) · 2020Article
- A molecular model for LINC complex regulation: activation of SUN2 for KASH binding.Molecular biology of the cell · 2018Article
- Differentiation alters stem cell nuclear architecture, mechanics, and mechano-sensitivity.eLife · 2016Article
- Lamins at the crossroads of mechanosignaling.Genes & development · 2015Review
- The tail domain of lamin B1 is more strongly modulated by divalent cations than lamin A.Nucleus (Austin, Tex.) · 2015Article
- Nuclear stiffening inhibits migration of invasive melanoma cells.Cellular and molecular bioengineering · 2014Article
- Interfacial binding and aggregation of lamin A tail domains associated with Hutchinson-Gilford progeria syndrome.Biophysical chemistry · 2014Article
- The nuclear lamina is mechano-responsive to ECM elasticity in mature tissue.Journal of cell science · 2014Review
- Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
Lamin proteins contribute to nuclear structure and function, primarily at the inner nuclear membrane. The posttranslational processing pathway of lamin A includes farnesylation of the C-terminus, likely to increase membrane association, and subsequent proteolytic cleavage of the C-terminus. Hutchinson Gilford progeria syndrome is a premature aging disorder wherein a mutant version of lamin A, Δ50 lamin A, retains its farnesylation. We report here that membrane association of farnesylated Δ50 lamin A tail domains requires calcium. Experimental evidence and molecular dynamics simulations collectively suggest that the farnesyl group is sequestered within a hydrophobic region in the tail domain in the absence of calcium. Calcium binds to the tail domain with an affinity KD ≈ 250 μM where it alters the structure of the Ig-fold and increases the solvent accessibility of the C-terminus. In 2 mM CaCl2, the affinity of the farnesylated protein to a synthetic membrane is KD ≈ 2 μM, as measured with surface plasmon resonance, but showed a combination of aggregation and binding. Membrane binding in the absence of calcium could not be detected. We suggest that a conformational change induced in Δ50 lamin A with divalent cations plays a regulatory role in the posttranslational processing of lamin A, which may be important in disease pathogenesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.