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EGF-induced dynamics of NF-kappa B and F-actin in A431 cells spread on fibronectin
Linköping University, Department of Clinical and Experimental Medicine, Division of Microbiology and Molecular Medicine. Linköping University, Faculty of Medicine and Health Sciences. Russian Academic Science, Russia; St Petersburg State Polytech University, Russia.
Linköping University, Department of Clinical and Experimental Medicine, Division of Microbiology and Molecular Medicine. Linköping University, Faculty of Medicine and Health Sciences.
Russian Academic Science, Russia.
Russian Academic Science, Russia.
2015 (English)In: Histochemistry and Cell Biology, ISSN 0948-6143, E-ISSN 1432-119X, Vol. 144, no 3, 223-235 p.Article in journal (Refereed) Published
Abstract [en]

To evaluate the role of actin cytoskeleton in the regulation of NF-kappa B transcription factor, we analyzed its involvement in the intracellular transport and nuclear translocation of the NF-kappa B RelA/p65 subunit in A431 epithelial cells stimulated with fibronectin and EGF. Live cell imaging and confocal microscopy showed that EGF activated the movement of RelA/p65 in the cytoplasm. Upon cell adhesion to fibronectin, RelA/p65 concentrated onto stress fibers, and EGF stimulated its subsequent allocation to membrane ruffles, newly organized stress fibers, and discrete cytoplasmic actin-rich patches. These patches also contained alpha-actinin-1 and alpha-actinin-4, vinculin, paxillin, alpha-tubulin, and PI3-kinase. Cytochalasin D treatment resulted in RelA/p65 redistribution to actin-containing aggregates, with the number of cells with RelA/p65-containing clusters in the cytoplasm increasing under the effect of EGF. Furthermore, EGF proved to induce RelA/p65 accumulation in the nucleus after cell pretreatment with actin-stabilizing and actin-destabilizing agents, which was accompanied by changes in its DNA-binding activity after either EGF stimulation or cytochalasin D treatment. Thus, EGF treatment of A431 cells results in simultaneous nuclear RelA/p65 translocation and cytoplasmic redistribution, with part of RelA/p65 pool forming a very tight association with actin-rich structures. Apparently, nuclear transport is independent on drug stabilization or destabilization of the actin.

Place, publisher, year, edition, pages
Springer Verlag (Germany) , 2015. Vol. 144, no 3, 223-235 p.
Keyword [en]
RelA/p65; Actin cytoskeleton; Fibronectin; EGF; Cytochalasin D; Jasplakinolide
National Category
Clinical Medicine
Identifiers
URN: urn:nbn:se:liu:diva-121098DOI: 10.1007/s00418-015-1331-5ISI: 000359650000003PubMedID: 25990946OAI: oai:DiVA.org:liu-121098DiVA: diva2:851859
Note

Funding Agencies|Swedish Institute [879/2009]; wedish Research Council [2010-3045]; Faculty of Health Science, Linkoping University; European Science Foundation; Molecular and Cellular Biology Program of Russian Academy of Sciences; Russian Foundation for Basic Research [13-04-00497]

Available from: 2015-09-07 Created: 2015-09-07 Last updated: 2016-04-12

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Bolshakova, AnastayiaMagnusson, Karl-Eric
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