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. 2014 Jan 29;5(3):214–223. doi: 10.1007/s13238-013-0010-3

Figure 5.

Figure 5

HDAC6 interacts with CLIP-170. (A) Cells were transfected with HA-HDAC6 and GFP or GFP-CLIP-170. Immunoprecipitation (IP) was then performed to examine the interaction between HA-HDAC6 and GFP-CLIP-170. (B) Cells were transfected with GFP or GFP-HDAC6, and immunoprecipitation was performed to examine the interaction between GFP-HDAC6 and endogenous CLIP-170. (C) Cells were treated with DMSO, tubacin, or TSA. Immunoprecipitation and immunoblotting were then performed with antibodies against CLIP-170 and acetylated lysine (Ac-Lys). Cell lysates were immunoblotted with antibodies against α-tubulin, acetylated α-tubulin (Ac-tubulin), and CLIP-170. (D) Cells were transfected with GFP-CLIP-170 and various forms of HDAC6 tagged with HA. Cell lysates and anti-GFP immunoprecipitates were immunoblotted with anti-GFP and anti-HA antibodies. Left panel shows various forms of HA-HDAC6 used. DD, deacetylase domain; CT, carboxyl terminus. (E) Cells were transfected with HA-HDAC6 and various forms of CLIP-170 tagged with GFP. Cell lysates and anti-GFP immunoprecipitates were immunoblotted with anti-GFP and anti-HA antibodies. Left panel shows various forms of CLIP-170 used. CG, CAP-Gly; CC, coiled coil; ZnF, zinc finger