The interaction between focal adhesion kinase (FAK) and integrin β4 in carcinoma cells

• Main Authors: Hui-Yuan Tseng, 曾暉元
• Other Authors: 沈湯龍
• Format: Others
• Language: en_US
• Published: 2007
• Online Access: http://ndltd.ncl.edu.tw/handle/71056181565987161914

碩士 === 國立臺灣大學 === 植物病理與微生物學研究所 === 95 === A numerous studies have shown that integrin β4 involved in tumor progression and clustering of integrin β4 might lead to the activation of focal adhesion kinase (FAK) and its downstream signaling. These findings are consistent with the roles of FAK in cell proliferation, migration and tumor development. Hence, we were further pursuing the possibility of direct interaction between integrin β4 and FAK. Indeed, we demonstrated that in several tumor cell lines, such as MDA-MB-231 and HCT116 but not HeLa, MCF7 and A549, integrin β4 could co-immuoprecipitate FAK protein endogenously. Besides, this integrin β4-FAK interaction is independent of FAK activity. It implicated the participation of this interaction in tumorigenesis. Moreover, the interaction required an 11-amino-acids motif within FAK’s amino-terminus. By using the in vitro binding assay and competition approach, this association is further confirmed. Among them, two out of 11 amino acids exhibited a critical role in interaction with integrin β4. And the further observations showed that this interaction existed only as cells are adherent.Our data resolved for the first time a physical interaction between integrins and FAK, suggesting a strong link regarding integrin-FAK signaling events. Future work will decipher the signaling pathway(s) and biological significance through the integrin β4-FAK interaction, which will shed a light on better strategies for cancer therapies.