作者: Miguel Garcia-Guzman , Fabrizio Dolfi , Michael Russello , Kristiina Vuori
关键词: Phosphatase 、 Signal transduction 、 Extracellular matrix 、 Cell adhesion 、 Cell biology 、 Fibronectin 、 Cell 、 Subcellular localization 、 Cell adhesion molecule 、 Biology
摘要: Integrin ligand binding induces a signaling complex formation via the direct association of docking protein p130Cas (Cas) with diverse molecules. We report here that 14-3-3ζ interacts Cas in yeast two-hybrid assay. also found two proteins associate mammalian cells and this interaction takes place phosphoserine-dependent manner, because treatment serine phosphatase greatly reduced its ability to bind 14-3-3ζ. Furthermore, Cas-14-3-3ζ was be regulated by integrin-mediated cell adhesion. Thus, when are detached from extracellular matrix, is diminished, whereas replating onto fibronectin rapidly association. Consistent these results, we subcellular localization 14-3-3 integrin display significant co-localization during attachment matrix. In conclusion, our results demonstrate participate integrin-activated pathways through their Cas, which, turn, may contribute important biological responses adhesion