Systematic interaction network filtering identifies CRMP1 as a novel suppressor of huntingtin misfolding and neurotoxicity

(Downloading may take up to 30 seconds. If the slide opens in your browser, select File -> Save As to save it.)

Click on image to view larger version.

Figure 2.
Figure 2.

Expression of CRMP1 in brains of HD transgenic mice and cell models. (A) Endogenous CRMP1 protein levels are reduced in brain tissues of 12-mo-old YAC128 HD transgenic mice compared to controls. Protein extracts prepared from striatal tissues of wild-type and transgenic HD mice were analyzed by SDS-PAGE and immunoblotting using the anti-CRMP1 antibody 504-518. (B) Quantification of ∼65 kDa CRMP1 bands in A. Values represent the means of three independent experiments. (**) P ≤ 0.01, two-sided t-test with unequal variance. (C) Endogenous CRMP1 levels are altered in brains of R6/2 HD transgenic mice compared to controls. Protein extracts were analyzed by SDS-PAGE and immunoblotting using the anti-CRMP1 antibody 504-518. (D) Quantification of CRMP1 protein bands shown in C. Values represent the means of three independent experiments. (*) P < 0.1; (**) P ≤ 0.01, two-sided t-test with unequal variance. (E) Heat stress induces endogenous CRMP1 protein levels in SH-SY5Y neuroblastoma cells. Cell lysates were analyzed by SDS-PAGE and immunoblotting. (F) Quantification of CRMP1 and HSPA1A protein bands shown in E. Values represent the means of three independent experiments. (**) P ≤ 0.01, two-sided t-test with unequal variance. (G) Analysis of CRMP1 and HSPA1A protein expression in SH-SY5Y cells under heat stress conditions by immunofluorescence microscopy. Data in B, D, and F are represented as mean ± SEM.

This Article

  1. Genome Res. 25: 701-713

Preprint Server