ArticleThe Journal of cell biology1993
Phosphorylation on protein kinase C sites inhibits nuclear import of lamin B2.
Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 122 citations in OpenAlex.
- Identification and Functional Analysis of Dual Nuclear Localization Signals on Desmin.ACS omega · 2026Article
- Dynamic Post-translational Modifications of Nuclear Lamins in Cellular Function and Pathophysiology.Sub-cellular biochemistry · 2025Review
- Post-Translational Modification of Lamins: Mechanisms and Functions.Frontiers in cell and developmental biology · 2022Review
- Chemical Decorations of "MARs" Residents in Orchestrating Eukaryotic Gene Regulation.Frontiers in cell and developmental biology · 2020Review
- Recent advances in understanding nuclear size and shape.Nucleus (Austin, Tex.) · 2016Review
- Review
- Lamins at the crossroads of mechanosignaling.Genes & development · 2015Review
- Numb-dependent integration of pre-TCR and p53 function in T-cell precursor development.Cell death & disease · 2014Article
- cPKC regulates interphase nuclear size during Xenopus development.The Journal of cell biology · 2014Article
- Interphase phosphorylation of lamin A.Journal of cell science · 2014Article
- The intracellular fate of zonula occludens 2 is regulated by the phosphorylation of SR repeats and the phosphorylation/O-GlcNAcylation of S257.Molecular biology of the cell · 2013Article
- Partners and post-translational modifications of nuclear lamins.Chromosoma · 2013Review
- The different function of single phosphorylation sites of Drosophila melanogaster lamin Dm and lamin C.PloS one · 2012Article
- Developmental downregulation of Xenopus cyclin E is phosphorylation and nuclear import dependent and is mediated by ubiquitination.Developmental biology · 2011Article
- Nuclear lamins.Cold Spring Harbor perspectives in biology · 2010Review
- Seven kinds of intermediate filament networks in the cytoplasm of polarized cells: structure and function.Acta histochemica et cytochemica · 2010Article
- Akt finds its new path to regulate cell cycle through modulating Skp2 activity and its destruction by APC/Cdh1.Cell division · 2009Article
- Regulation of nuclear import and export of negative cofactor 2.The Journal of biological chemistry · 2009Article
- Phosphorylation by Akt1 promotes cytoplasmic localization of Skp2 and impairs APCCdh1-mediated Skp2 destruction.Nature cell biology · 2009Article
- Phosphorylation by casein kinase 1 regulates tonicity-induced osmotic response element-binding protein/tonicity enhancer-binding protein nucleocytoplasmic trafficking.The Journal of biological chemistry · 2008Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nuclear lamina is a karyoskeletal structure at the nucleoplasmic surface of the inner nuclear membrane. Its assembly state is regulated by phosphorylation of the intermediate filament type lamin proteins. Strong evidence has been obtained for a causal link between phosphorylation of lamins by the p34cdc2 protein kinase and disassembly of the nuclear lamina during mitosis. In contrast, no information is currently available on the role of lamin phosphorylation during interphase of the cell cycle. Here, we have identified four protein kinase C phosphorylation sites in purified chicken lamin B2 as serines 400, 404, 410, and 411. In vivo, the tryptic peptide containing serines 400 and 404 is phosphorylated throughout interphase, whereas serines 410 and 411 become phosphorylated specifically in response to activation of protein kinase C by phorbol ester. Prompted by the close proximity of serines 410/411 to the nuclear localization signal of lamin B2, we have studied the influence of phosphorylation of these residues on nuclear transport. Using an in vitro assay, we show that phosphorylation of lamin B2 by protein kinase C strongly inhibits transport to the nucleus. Moreover, phorbol ester treatment of intact cells leads to a substantial reduction of the rate of nuclear import of newly synthesized lamin B2 in vivo. These findings have implications for the dynamic structure of the nuclear lamina, and they suggest that the modulation of nuclear transport rates by cytoplasmic phosphorylation may represent a general mechanism for regulating nuclear activities.
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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.