ArticlePloS one2012
The different function of single phosphorylation sites of Drosophila melanogaster lamin Dm and lamin C.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 19 citations in OpenAlex.
- Baculoviruses exploit the mitotic kinase CDK1 to disrupt the nuclear lamina.PLoS pathogens · 2026Article
- Selection of specific and efficient siRNAs in new cellular model for Hutchinson-Gilford progeria syndrome therapy.Molecular therapy. Nucleic acids · 2025Article
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- Developmental changes in nuclear lamina components during germ cell differentiation.Nucleus (Austin, Tex.) · 2024Article
- Drosophila p38 MAPK interacts with BAG-3/starvin to regulate age-dependent protein homeostasis.Aging cell · 2021Article
- Chemical Decorations of "MARs" Residents in Orchestrating Eukaryotic Gene Regulation.Frontiers in cell and developmental biology · 2020Review
- Article
- Laminopathies: what can humans learn from fruit flies.Cellular & molecular biology letters · 2018Review
- Review
- PKC-mediated phosphorylation of nuclear lamins at a single serine residue regulates interphase nuclear size inMolecular biology of the cell · 2017Article
- Review
- Lamins at the crossroads of mechanosignaling.Genes & development · 2015Review
- Muscle development, regeneration and laminopathies: how lamins or lamina-associated proteins can contribute to muscle development, regeneration and disease.Cellular and molecular life sciences : CMLS · 2013Review
- Partners and post-translational modifications of nuclear lamins.Chromosoma · 2013Review
- Isocitrate dehydrogenase from Streptococcus mutans: biochemical properties and evaluation of a putative phosphorylation site at Ser102.PloS one · 2013Article
- Diverse lamin-dependent mechanisms interact to control chromatin dynamics. Focus on laminopathies.Nucleus (Austin, Tex.)Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lamins' functions are regulated by phosphorylation at specific sites but our understanding of the role of such modifications is practically limited to the function of cdc 2 (cdk1) kinase sites in depolymerization of the nuclear lamina during mitosis. In our study we used Drosophila lamin Dm (B-type) to examine the function of particular phosphorylation sites using pseudophosphorylated mutants mimicking single phosphorylation at experimentally confirmed in vivo phosphosites (S(25)E, S(45)E, T(435)E, S(595)E). We also analyzed lamin C (A-type) and its mutant S(37)E representing the N-terminal cdc2 (mitotic) site as well as lamin Dm R(64)H mutant as a control, non-polymerizing lamin. In the polymerization assay we could observe different effects of N-terminal cdc2 site pseudophosphorylation on A- and B-type lamins: lamin Dm S(45)E mutant was insoluble, in contrast to lamin C S(37)E. Lamin Dm T(435)E (C-terminal cdc2 site) and R(64)H were soluble in vitro. We also confirmed that none of the single phosphorylation site modifications affected the chromatin binding of lamin Dm, in contrast to the lamin C N-terminal cdc2 site. In vivo, all lamin Dm mutants were incorporated efficiently into the nuclear lamina in transfected Drosophila S2 and HeLa cells, although significant amounts of S(45)E and T(435)E were also located in cytoplasm. When farnesylation incompetent mutants were expressed in HeLa cells, lamin Dm T(435)E was cytoplasmic and showed higher mobility in FRAP assay.
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