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. 2018 Aug 3;9:1070. doi: 10.3389/fphys.2018.01070

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Copyright © 2018 Taneja, Ma, Kim and Welling.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Golgin-97 GRIP domain directly interacts with Kir2.1. (A) Domain structure of Golgin-97, showing the GRIP domain and the coiled-coil domain. (B) Anti-myc immunoprecipitation (IP) followed by anti-HA immunoblotting (IB) from COS cells co-transfected with myc-Golgi 97 (Full length, Grip domain only, or coiled-coiled domain only) and HA-Kir2.1 wild type, WT, or the TGN-export mutant (Δ314–315) or (D) the HA-tagged Kir2.1 COOH-terminal cytoplasmic domain (CTCD). (C,E) Quantitative summaries comparing relative amounts of Kir2.1 (WT or Δ314–315) immunoprecipitated with full-length Golgin-97, or GRIP or Coiled-Coil domain, ^∗P < 0.05. (F) GST pulldowns: GST alone or GST fusion proteins of the Kir2.1 CTCD were used to test for direct interaction with His-tagged GRIP domains of Golgin-97 or Golgin-245 purified from bacteria. Protein bound is shown relative to 5% input.