Skip to main content
. Author manuscript; available in PMC: 2015 Aug 1.
Published in final edited form as: Exp Cell Res. 2014 May 28;326(1):78–89. doi: 10.1016/j.yexcr.2014.05.018

Figure 2.

Figure 2

Identification of HSP90β domains involved in FAK interaction. (A) Different domains of HSP90β interact with Myc-tagged FAK in HEK293T cells. Myc-tagged FAK, immobilized on protein-G agarose beads, was incubated with lysates from HEK293T cells expressing Flag-tagged HSP90β derivatives. Precipitated proteins and input lysates were immunoblotted with anti-Flag antibody. IgG H, IgG heavy chain. (B) HSP90β constructs and FAK binding activity. (C) Direct interaction between HSP90β and FAK. HEK293T cells expressing Myc-tagged FAK were lysed and resulting lysates were incubated with indicated GST-fusion proteins immobilized on Glutathione-Sepharose beads. Bound proteins were probed with anti-Myc antibodies (top). GST-fusion proteins were revealed by SDS-PAGE method and stained with Coomassie Brilliant Blue (bottom). (D) Structural domains of HSP90β used in these experiments and FAK binding activity. The corresponding bands are indicated with stars.