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. 2017 Jan 20;19(1):43–53. doi: 10.1016/j.neo.2016.11.007

Figure 2.

Figure 2

GRP78 interacts with GALNT6. (A and B) HA-tagged GALNT6 was co-immunoprecipitated with endogenous GRP78 in HeLa-GALNT6-WT and -H271D stable cells, but not in -mock stable cells. However, interaction of GRP78 with GALNT6-H271D was much weaker than that with GALNT6-WT. (A) Endogenous GRP78 was pulled down using anti-GRP78 antibody, followed by western blots for HA-tagged GALNT6 and endogenous GRP78. (B) HA-tagged GALNT6 was pulled down by anti-HA, and then endogenous GRP78 and HA-tagged GALNT6 were detected by western blot. (C) To map the binding domain on GRP78, four expressing vectors for Flag-tagged full-length wild-type GRP78 (WT) and three Flag-tagged partial GRP78 fragments with or without ATPase domain were generated. (D) Forty-eight hours after transfection with these four vectors in HeLa-GALNT6-WT stable cells, immunoprecipitation with anti-Flag antibody was performed followed by western blots.