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Extra‐cellular matrix proteins induce re‐distribution of α‐actinin‐1 and α‐actinin‐4 in A431 cells
Author(s) -
Bolshakova Anastasia,
Petukhova Olga,
Turoverova Lidia,
Tentler Dmitri,
Babakov Vladimir,
Magnusson KarlEric,
Pinaev George
Publication year - 2007
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1016/j.cellbi.2007.01.021
Subject(s) - actinin , fibronectin , microbiology and biotechnology , actin , extracellular matrix , laminin , chemistry , actin binding protein , cytoskeleton , nuclear matrix , actin cytoskeleton , chromatin , cell , biology , biochemistry , dna
Alpha‐actinins are actin‐binding proteins of non‐muscle cells, which can participate in the regulation of transcription factor activity. We describe the distribution of α‐actinin‐1 and −4 depending on different actin cytoskeleton formed as a result of cell adhesion to extracellular matrix proteins, such as fibronectin and laminin 2/4. Immunofluorescent studies show a difference in the distribution of α‐actinin and −4. Both isoforms localise along stress‐fibres, but α‐actinin‐1 localises in the perinuclear region more abundantly than α‐actinin‐4. Western blot analysis demonstrated existence of truncated forms of both isoforms. Truncated α‐actinin‐1 appears in cells spread on fibronectin or laminin. Cell spreading also correlated with more tight association of α‐actinin‐4 with chromatin. Basing on our previous finding of an interaction of α‐actinin‐4 with p65 subunit of the NF‐κB, we checked the possible influence of immobilised ligands on its redistribution in nuclear complexes containing p65. α‐Actinin‐4 seems to be present in some but not all nuclear complexes containing p65. Immobilised ligands may affect the interaction of α‐actinin‐4/p65 complexes with chromatin. The data suggest that adhesion to extra‐cellular matrix may interfere in cellular reactions mediated by α‐actinin‐1 and −4.