Fig. 6

DYNLT1 antagonizes the interaction between Parkin and VDAC1 and stabilizing the expression of VDAC1

A-B WB results showed that DYNLT1 knockdown affected the protein stability of VDAC1. Line plots showed the relative protein levels of VDAC1 after DYNLT1 knockdown. (A): MCF-7 DYNLT1 knockdown cell; (B): MDA-MB-468 DYNLT1 knockdown cell. C-D Protein levels of DYNLT1, VDAC1 and GAPDH in stable DYNLT1 knockdown MCF-7 (C) or MDA-MB-468 (D) breast cancer cells treated with MG132. E Ubiquitination experiments showed that exogenous DYNLT1 overexpression in 293T cells significantly inhibited the ubiquitination degradation of VDAC1. F-G Co-IP results showed that Parkin can interact with VDAC1 in MCF-7 (F) or MDA-MB-468 (G) breast cancer cells. H-I Co-IP results showed that inhibition of DYNLT1 strength the interaction between Parkin and VDAC1 in stable DYNLT1 knockdown MCF-7 (H) or MDA-MB-468 (I) breast cancer cells. *, p < 0.05. All experiments were performed at least three replicates