ArticleThe Journal of cell biology1999
Dissociation of FAK/p130(CAS)/c-Src complex during mitosis: role of mitosis-specific serine phosphorylation of FAK.
Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 120 citations in OpenAlex.
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- An asymmetric junctional mechanoresponse coordinates mitotic rounding with epithelial integrity.The Journal of cell biology · 2021Article
- Cdk1 phosphorylation negatively regulates the activity of Net1 towards RhoA during mitosis.Cellular signalling · 2021Article
- Boolean model of anchorage dependence and contact inhibition points to coordinated inhibition but semi-independent induction of proliferation and migration.Computational and structural biotechnology journal · 2020Article
- The Cytotoxicity Effect of Resveratrol: Cell Cycle Arrest and Induced Apoptosis of Breast Cancer 4T1 Cells.Toxins · 2019Article
- Connections between the cell cycle, cell adhesion and the cytoskeleton.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019Review
- The interaction of p130Cas with PKN3 promotes malignant growth.Molecular oncology · 2019Article
- The balance between adhesion and contraction during cell division.Current opinion in cell biology · 2019Review
- Cell adhesion is regulated by CDK1 during the cell cycle.The Journal of cell biology · 2018Article
- Mitosis-Mediated Intravasation in a Tissue-Engineered Tumor-Microvessel Platform.Cancer research · 2017Article
- Coupling changes in cell shape to chromosome segregation.Nature reviews. Molecular cell biology · 2016Review
- Cdk1-dependent mitotic enrichment of cortical myosin II promotes cell rounding against confinement.Nature cell biology · 2015Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
At mitosis, focal adhesions disassemble and the signal transduction from focal adhesions is inactivated. We have found that components of focal adhesions including focal adhesion kinase (FAK), paxillin, and p130(CAS) (CAS) are serine/threonine phosphorylated during mitosis when all three proteins are tyrosine dephosphorylated. Mitosis-specific phosphorylation continues past cytokinesis and is reversed during post-mitotic cell spreading. We have found two significant alterations in FAK-mediated signal transduction during mitosis. First, the association of FAK with CAS or c-Src is greatly inhibited, with levels decreasing to 16 and 13% of the interphase levels, respectively. Second, mitotic FAK shows decreased binding to a peptide mimicking the cytoplasmic domain of beta-integrin when compared with FAK of interphase cells. Mitosis-specific phosphorylation is responsible for the disruption of FAK/CAS binding because dephosphorylation of mitotic FAK in vitro by protein serine/threonine phosphatase 1 restores the ability of FAK to associate with CAS, though not with c-Src. These results suggest that mitosis-specific modification of FAK uncouples signal transduction pathways involving integrin, CAS, and c-Src, and may maintain FAK in an inactive state until post-mitotic spreading.
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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.