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. 2017 May 1;130(9):1637–1651. doi: 10.1242/jcs.198267

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© 2017. Published by The Company of Biologists Ltd

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.

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Fig. 1. — SKIP interacts directly with KHC. (A) Schematic showing domain organization of SKIP and CSTN1. (B) Western blot (IB) showing that GST–KHC(815-955) retains GFP–SKIP(1-310) from 293T cell extracts but not the cytoplasmic domain of CSTN1(879-971). Data are representative of three independent experiments. (C) Top: Coomassie-stained SDS-PAGE gel showing results from a GST pulldown experiment showing a direct interaction between GST–KHC(815-955) and SKIP(1-310). Bottom left: graph showing relative binding of SKIP(1-310) to GST and GST–KHC(815-955) at the 3.5 μM concentration shown in the top panel. Data is mean±s.e.m. of three independent experiments. ***P<0.001 (two-tailed t-test). Bottom right: graph showing quantification of SKIP(1-310) band density from three independent experiments as shown in the top panel. Error bars show ±s.e.m. Results are fitted to a one-site specific binding model with a hill slope [EQ Y=B_max×X^h/(K_d^h+X^h) where B_max=4.23, K_d=1.53] (h)=2.04. R²=0.98.