Interplay in neural functions of cell adhesion molecule close homolog of L1 (CHL1) and Programmed Cell Death 6 (PDCD6).
Autor: | Loers G; Zentrum für Molekulare Neurobiologie Universitätsklinikum Hamburg-Eppendorf Hamburg Germany., Theis T; Keck Center for Collaborative Neuroscience and Department of Cell Biology and Neuroscience Rutgers University Piscataway NJ USA., Baixia Hao H; Keck Center for Collaborative Neuroscience and Department of Cell Biology and Neuroscience Rutgers University Piscataway NJ USA., Kleene R; Zentrum für Molekulare Neurobiologie Universitätsklinikum Hamburg-Eppendorf Hamburg Germany., Arsha S; Keck Center for Collaborative Neuroscience and Department of Cell Biology and Neuroscience Rutgers University Piscataway NJ USA., Samuel N; Keck Center for Collaborative Neuroscience and Department of Cell Biology and Neuroscience Rutgers University Piscataway NJ USA., Arsha N; Keck Center for Collaborative Neuroscience and Department of Cell Biology and Neuroscience Rutgers University Piscataway NJ USA., Young W; Keck Center for Collaborative Neuroscience and Department of Cell Biology and Neuroscience Rutgers University Piscataway NJ USA., Schachner M; Keck Center for Collaborative Neuroscience and Department of Cell Biology and Neuroscience Rutgers University Piscataway NJ USA. |
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Jazyk: | angličtina |
Zdroj: | FASEB bioAdvances [FASEB Bioadv] 2021 Nov 03; Vol. 4 (1), pp. 43-59. Date of Electronic Publication: 2021 Nov 03 (Print Publication: 2022). |
DOI: | 10.1096/fba.2021-00027 |
Abstrakt: | Close homolog of L1 (CHL1) is a cell adhesion molecule of the immunoglobulin superfamily. It promotes neuritogenesis and survival of neurons in vitro. In vivo, CHL1 promotes nervous system development, regeneration after trauma, and synaptic function and plasticity. We identified programmed cell death 6 (PDCD6) as a novel binding partner of the CHL1 intracellular domain (CHL1-ICD). Co-immunoprecipitation, pull-down assay with CHL1-ICD, and proximity ligation in cerebellum and pons of 3-day-old and 6-month-old mice, as well as in cultured cerebellar granule neurons and cortical astrocytes indicate an association between PDCD6 and CHL1. The Ca 2+ -chelator BAPTA-AM inhibited the association between CHL1 and PDCD6. The treatment of cerebellar granule neurons with a cell-penetrating peptide comprising the cell surface proximal 30 N-terminal amino acids of CHL1-ICD inhibited the association between CHL1 and PDCD6 and PDCD6- and CHL1-triggered neuronal survival. These results suggest that PDCD6 contributes to CHL1 functions in the nervous system. Competing Interests: None declared. (© 2021 The Authors. FASEB BioAdvances published by Wiley Periodicals LLC on behalf of The Federation of American Societies for Experimental Biology.) |
Databáze: | MEDLINE |
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