Fig. 2
From: AIM1 is an actin-binding protein that suppresses cell migration and micrometastatic dissemination
The C terminus of AIM1 is required for the efficient interaction of AIM1 with the actin cytoskeleton. a Ideogram depicting the domain structure of AIM1 and the C-terminal deletion constructs used in the study (wt, denotes wild-type AIM1; Δ1287, indicates C-terminal deletion to amino acid 1287; Δ859, indicates C-terminal deletion to amino acid 859). b Reciprocal co-immunoprecipitations of wt AIM1 and AIM1 deletion mutants in HEK293 cells demonstrate that the Δ859 C-terminal deletion mutant, lacking all βγ-crystallin domains, fails to interact with the actin cytoskeleton, while full length and Δ1287 AIM1 retain binding to the actin cytoskeleton. Immunoblots shown here are representative of three independent experiments. c Confocal immunofluorescence microscopy demonstrates strong co-localization of actin (visualized by alexa-568-labeled phalloidin, shown in red) with YFP-tagged (shown in green) wt and Δ1287 AIM1 in transiently transfected COS7 cells. Scale bars indicate 5 μm. AIM1 Δ859 shows a predominant nuclear localization and no co-localization with actin. Two percent of TCL was loaded as control. IB immunoblot, IP immunoprecipitate, TCL total cell lysate
