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Mol. Cells 2010; 30(2): 143-148

Published online August 31, 2010

https://doi.org/10.1007/s10059-010-0099-7

© The Korean Society for Molecular and Cellular Biology

Ankyrin Repeat-Rich Membrane Spanning/Kidins220 Protein Interacts with Mammalian Septin 5

Han Jeong Park, Hwan-Woo Park, Shin-Jae Lee1, Juan Carlos Arevalo2, Young-Seok Park,Seung-Pyo Lee, Ki-Suk Paik, Moses V. Chao3, and Mi-Sook Chang*

Department of Oral Anatomy, School of Dentistry and Dental Research Institute, Seoul National University, Seoul 110-749, Korea, 1Department of Orthodontics, School of Dentistry and Dental Research Institute, Seoul National University, Seoul 110-749, Korea, 2Institute of Neurosciences Castilla y Leon, University of Salamanca, 37007 Salamanca, Spain, 3Molecular Neurobiology Program, Skirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, USA

Correspondence to : *Correspondence: mschang@snu.ac.kr

Received: April 7, 2010; Revised: May 6, 2010; Accepted: May 7, 2010

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 Mem-brane 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 co-localized 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.

Keywords adaptor protein, neurotrophin, receptor, septin, signal transduction

Article

Research Article

Mol. Cells 2010; 30(2): 143-148

Published online August 31, 2010 https://doi.org/10.1007/s10059-010-0099-7

Copyright © The Korean Society for Molecular and Cellular Biology.

Ankyrin Repeat-Rich Membrane Spanning/Kidins220 Protein Interacts with Mammalian Septin 5

Han Jeong Park, Hwan-Woo Park, Shin-Jae Lee1, Juan Carlos Arevalo2, Young-Seok Park,Seung-Pyo Lee, Ki-Suk Paik, Moses V. Chao3, and Mi-Sook Chang*

Department of Oral Anatomy, School of Dentistry and Dental Research Institute, Seoul National University, Seoul 110-749, Korea, 1Department of Orthodontics, School of Dentistry and Dental Research Institute, Seoul National University, Seoul 110-749, Korea, 2Institute of Neurosciences Castilla y Leon, University of Salamanca, 37007 Salamanca, Spain, 3Molecular Neurobiology Program, Skirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, USA

Correspondence to:*Correspondence: mschang@snu.ac.kr

Received: April 7, 2010; Revised: May 6, 2010; Accepted: May 7, 2010

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 Mem-brane 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 co-localized 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.

Keywords: adaptor protein, neurotrophin, receptor, septin, signal transduction

Mol. Cells
Sep 30, 2022 Vol.45 No.9, pp. 603~672
COVER PICTURE
The Target of Rapamycin Complex (TORC) is a central regulatory hub in eukaryotes, which is well conserved in diverse plant species, including tomato (Solanum lycopersicum). Inhibition of TORC genes (SlTOR, SlLST8, and SlRAPTOR) by VIGS (virus-induced gene silencing) results in early fruit ripening in tomato. The red/ orange tomatoes are early-ripened TORC-silenced fruits, while the green tomato is a control fruit. Top, left, control fruit (TRV2-myc); top, right, TRV2-SlLST8; bottom, left, TRV2-SlTOR; bottom, right, TRV2-SlRAPTOR(Choi et al., pp. 660-672).

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