Ankyrin repeat-rich membrane spanning/Kidins220 protein interacts with mammalian Septin 5 |
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Authors: | Han Jeong Park Hwan-Woo Park Shin-Jae Lee Juan Carlos Arevalo Young-Seok Park Seung-Pyo Lee Ki-Suk Paik Moses V Chao Mi-Sook Chang |
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Institution: | (1) Department of Cellular and Molecular Neuroscience, Division of Neuroscience and Mental Health, School of Medicine, Imperial College London, Burlington Danes Building, Hammersmith Campus, Du Cane Road, London, W12 0NN, UK |
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Abstract: | Neurotrophin receptors utilize specific adaptor proteins to activate signaling pathways involved in various neuronal functions,
such as neurite outgrowth and cytoskeletal remodeling. The Ankyrin-Repeat Rich Membrane Spanning (ARMS)/kinase D-interacting
substrate-220 kDa (Kidins220) serves as a unique downstream adaptor protein of Trk receptor tyrosine kinases. To gain insight
into the role of ARMS/Kidins220, a yeast two-hybrid screen of a rat dorsal root ganglion library was performed using the C-terminal
region of ARMS/Kidins220 as bait. The screen identified a mammalian septin, Septin 5 (Sept5), as an interacting protein. Co-immunoprecipitation
using lysates from transiently transfected HEK-293 cells revealed the specific interaction between ARMS/Kidins220 and Sept5.
Endogenous ARMS/Kidins220 and Sept5 proteins were colocalized in primary hippocampal neurons and were also predominantly expressed
at the plasma membrane and in the tips of growing neurites in nerve growth factor-treated PC12 cells. Mapping of Sept5 domains
important for ARMS/Kidins220 binding revealed a highly conserved N-terminal region of Sept5. The direct interaction between
ARMS/Kidins220 and Sept5 suggests a possible role of ARMS/Kidins220 as a functional link between neurotrophin receptors and
septins to mediate neurotrophin-induced intracellular signaling events, such as neurite outgrowth and cytoskeletal remodeling. |
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