作者: Kristi Krebs , Anu Ruusmann , Grethel Simonlatser , Teet Velling
DOI: 10.1016/J.EJCB.2015.10.006
关键词:
摘要: FLNa is a ubiquitous cytoskeletal protein that links transmembrane receptors, including integrins, to F-actin and functions as signalling intermediate. We investigated FLNa's role in the function of integrin-type collagen EGF-EGFR regulation PKB/Akt ERK1/2. Using FLNa-deficient M2 human melanoma cells, same cells expressing EGFP-FLNa (M2F) or its Ig-like repeats 1-8+24, 8-15+24 16-24, we found M2F EGF induced increased phosphorylation In localisation these kinases cell nucleus lamellipodia, respectively, ERK1/2 phosphorylation-dependent co-immunoprecipitation with Only adhered spread on type I whereas fibronectin all behaved similarly. α1β1 α2β1 were receptors expressed primarily localising focal contacts affecting adhesion migration manner dependent 8-15. Our results suggest for 8-15 α1-subunit-dependent integrin function, ERK1/2, identify EGF-induced FLNa-associated complexes, show different integrins subjected differential by FLNa.