ArticleThe Biochemical journal2002
Actopaxin is phosphorylated during mitosis and is a substrate for cyclin B1/cdc2 kinase.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- Parvin is essential for indirect flight muscle (IFM) performance and Zasp52 localisation to the Z-disc in Drosophila melanogaster.Cell and tissue research · 2025Article
- Matrix Remodeling Associated Genes (MXRAs): structural diversity, functional significance, and therapeutic potential in tumor microenvironments.Discover oncology · 2025Review
- A cyclin-dependent kinase-mediated phosphorylation switch of disordered protein condensation.Nature communications · 2023Article
- Identification of Phosphorylated Proteins Regulated by SDF2L1 in Nasopharyngeal Carcinoma Cells.Evolutionary bioinformatics online · 2022Article
- Connections between the cell cycle, cell adhesion and the cytoskeleton.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019Review
- α-Parvin and β-parvin in the rat uterus during decidualisation and uterine receptivity.Histochemistry and cell biology · 2019Article
- Coupling changes in cell shape to chromosome segregation.Nature reviews. Molecular cell biology · 2016Review
- Defining the phospho-adhesome through the phosphoproteomic analysis of integrin signalling.Nature communications · 2015Article
- Actopaxin (α-parvin) phosphorylation is required for matrix degradation and cancer cell invasion.The Journal of biological chemistry · 2012Article
- Computational drug discovery.Acta pharmacologica Sinica · 2012Review
- The parvins.Cellular and molecular life sciences : CMLS · 2006Review
- Modulation of gene expression in MHCC97 cells by interferon alpha.World journal of gastroenterology · 2005Article
- Phosphorylation of actopaxin regulates cell spreading and migration.The Journal of cell biology · 2004Article
- Contributions of integrin-linked kinase to breast cancer metastasis and tumourigenesis.Journal of cellular and molecular medicineReview
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Prior to cell division, normal adherent cells adopt a round morphology that is associated with a loss of actin stress fibres and disassembly of focal adhesions. In this study, we investigate the mitotic phosphorylation of the recently described paxillin and actin-binding focal-adhesion protein actopaxin [Nikolopoulos and Turner (2000) J. Cell Biol. 151, 1435-1448]. Actopaxin is comprised of an N-terminus containing six putative cdc2 phosphorylation sites and a C-terminus consisting of tandem calponin homology domains. Here we show that the N-terminus of actopaxin is phosphorylated by cyclin B1/cdc2 kinase in vitro and that this region of actopaxin precipitates cdc2 kinase activity from mitotic lysates. Actopaxin exhibits reduced electrophoretic mobility during mitosis that is dependent on phosphorylation within the first two consensus cdc2 phosphorylation sites. Finally, as cells progress from mitosis to G(1) there is an adhesion-independent dephosphorylation of actopaxin, suggesting that actopaxin dephosphorylation precedes cell spreading and the reformation of focal adhesions. Taken together, these results suggest a role for cyclin B1/cdc2-dependent phosphorylation of actopaxin in regulating actin cytoskeleton reorganization during cell division.
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