Fig. 1

SIP protein expression is dysregulated in the striatum in YAC128 mice. a Detection of SIP monomer and dimer in protein extracts from the striatum in YAC128 mice (YAC128) vs. control mice (WT) using Western blot (WB) under denaturing conditions. SIP densitometry was calibrated based on the intensity of p-cadherin. m, SIP monomer; d, SIP dimer. b Increase in levels of SIP dimers in YAC128 mice vs. control mice presented as fold changes; **p < 0.01. c Protein levels of SIP monomers in YAC128 mice vs. control mice presented as fold changes. ns not significant. d Detection of SIP monomer in protein extracts from HEK293T cells. m, SIP monomer. e Interaction between SIP and huntingtin (HTT). Samples that were subjected to immunoprecipitation (IP) with anti-SIP antibody were obtained from the striata in YAC128 mice and control mice (WT). Blots were labeled using an anti-HTT antibody. Western blot analyses of total extracts from YAC128 mice were used as controls (Total). Ab, anti-SIP antibody used for IP; M, protein marker in kilodaltons (kDa); IgG, heavy chain of antibody. The results are expressed as mean ± SEM. The results were obtained from the striata of two or four independent YAC128 and control mice for the IP and WB experiments, respectively