INTRACELLULAR DISTRIBUTION OF TYROSINE-PHOSPHORYLATED
ACTIN-BINDING PROTEINS IN A431 CELLS SPREAD ON DIFFERENT LIGANDS
V. N. Babakov, I. V. Kropacheva, O. A. Petukhova, L. V. Turoverova, G. P. Pinaev 1
Institute of Cytology, RAS, St. Petersburg, Russia;
1 e-mail: pinaev@mail.cytspb.rssi.ru
Spreading A431 cells on extracellular matrix elements fibronectin, laminin 2/4 and antibody to EOF receptor (5A9 clone)
leads to tyrosine phosphorylation of actin-binding proteins, which participate in focal adhesions formation. Tyrosine phosphorylation of
the proteins is retained for 1 h of cell spreading. When cells interact with ligands, focal adhesion kinase (FAK) becomes tyrosine
phosphorylated, and eventually phosphorylates the target proteins. The cooperative effect of integrins and EOF receptor in FAK
autophosphorylation at cell spreading on antibody to EOF receptor is discussed.
Key words: A431 cells, cell adhesion, FAK, EGF receptor, integrins
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