The self-association of two N-terminal interaction domains plays an important role in the tetramerization of TRPC4 |
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| Authors: | Pascale K Lepage Marc P Lussier François-Olivier McDuff Pierre Lavigne Guylain Boulay |
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| Institution: | 1. Department of Biochemistry, Kobe Pharmaceutical University, Higashinada-ku, Kobe 658-8558, Japan;2. Department of Neurology, Kinki University School of Medicine, Osaka-Sayama, Osaka 589-8511, Japan;3. Department of Neurology, Graduate School of Medicine, University of Tokyo, Bunkyo-ku, Tokyo 113-8655, Japan;1. Department of Life Science, Sogang University, Seoul, Republic of Korea;2. Department of Neurology, National Cancer Center, 809 Madu 1-dong, Ilsandong-gu, Gyeonggi-do 410-769, Republic of Korea;3. Department of Genetic Epidemiology, SNP Genetics, Inc., Seoul, Republic of Korea;1. Department of Plant and Soil Sciences, University of Kentucky, Lexington, KY 40546, USA;2. Instituto de Biotecnologia Aplicada à Agropecuária, Universidade Federal de Viçosa, Viçosa, MG, Brazil;1. Spinal Cord and Brain Injury Research Center, and Department of Anatomy and Neurobiology, University of Kentucky, Lexington, KY 40536, USA;2. Seattle Children''s Research Institute, Seattle, WA 98101, USA |
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| Abstract: | Transient receptor potential canonical (TRPC) channels function as cation channels. In a previous study, we identified the molecular determinants involved in promoting TRPC subunit assembly. In the present study, we used size-exclusion chromatography assays to show that the N-terminus of TRPC4 can self-associate and form a tetramer in cellulo. We further showed that the N-terminus of TRPC4 self-associates via the ankyrin repeat domain and the region downstream from the coiled-coil domain. GST pull-down, yeast two-hybrid, and circular dichroism approaches demonstrated that both domains can self-associate. These findings indicated that the self-association of two distinct domains in the N-terminus of TRPC4 is involved in the assembly of the tetrameric channel. |
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