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. 2005 Dec 2;33(21):6805–6815. doi: 10.1093/nar/gki985

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© The Author 2005. Published by Oxford University Press. All rights reserved

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CtBP1 interacts directly with Glis2. GST and GST-CtBP1 fusion proteins were bound to glutathione–Sepharose 4B beads and then incubated with [³⁵S]methionine-labeled Glis2 or Glis3. After 1 h incubation, beads were washed extensively and bound proteins solubilized and examined by PAGE. Radiolabeled proteins were visualized by autoradiography. Lane 1 and 2, 5% input of radiolabeled Glis2 (asterisk) and Glis3 (double asterisk), respectively; lanes 3 and 4, radiolabeled protein retained by GST; lane 5 and 6, protein retained by GST-CtBP1. Results show that only radiolabeled Glis2 was retained by GST-CtBP1.