Fig. 6
From: ULK1 phosphorylates Sec23A and mediates autophagy-induced inhibition of ER-to-Golgi traffic
The interactions between the ULK1 phosphorylation mutants of Sec23A and endogenous Sec31A. a S207 and T405 mutants of Sec23A were tested for their interaction with Sec31A in normal growth condition. The indicated Myc-His-Sec23A mutants were transfected into cells and tested for their ability to bring down endogenous Sec31A in co-IP experiment. b Wildtype Sec23A, S207A and T405A mutants were tested for the interaction with Sec31A in growth medium or in amino acid starved medium EBSS. c Combinations of S207 and T405 double mutants were tested for the interaction with Sec31A. Overexpression of the indicated protein was carried in HEK293T cells, followed by immunoprecipitation of Myc-His-Sec23A by anti-Myc antibody. Co-precipitated endogenous Sec31A was detected by anti-Sec31A antibody