RAIDD mutations underlie the pathogenesis of thin lissencephaly (TLIS)

Abnormal regulation of caspase-2-mediated neuronal cell death causes neurodegenerative diseases and defective brain development. PIDDosome is caspase-2 activating complex composed of PIDD, RAIDD, and caspase-2. Recent whole-exome sequencing study showed that the RAIDD mutations in the death domain (...

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Autores principales: Ha, Hyun Ji, Park, Hyun Ho
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2018
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6169973/
https://www.ncbi.nlm.nih.gov/pubmed/30281648
http://dx.doi.org/10.1371/journal.pone.0205042
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author Ha, Hyun Ji
Park, Hyun Ho
author_facet Ha, Hyun Ji
Park, Hyun Ho
author_sort Ha, Hyun Ji
collection PubMed
description Abnormal regulation of caspase-2-mediated neuronal cell death causes neurodegenerative diseases and defective brain development. PIDDosome is caspase-2 activating complex composed of PIDD, RAIDD, and caspase-2. Recent whole-exome sequencing study showed that the RAIDD mutations in the death domain (DD), including G128R, F164C, R170C, and R170H mutations, cause thin lissencephaly (TLIS) by reducing caspase-2-mediated neuronal apoptosis. Given that the molecular structure of the RAIDD DD:PIDD DD complex is available, in this study, we analyzed the molecular mechanisms underlying TLIS caused by the RAIDD TLIS variants by performing mutagenesis and biochemical assays.
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spelling pubmed-61699732018-10-19 RAIDD mutations underlie the pathogenesis of thin lissencephaly (TLIS) Ha, Hyun Ji Park, Hyun Ho PLoS One Research Article Abnormal regulation of caspase-2-mediated neuronal cell death causes neurodegenerative diseases and defective brain development. PIDDosome is caspase-2 activating complex composed of PIDD, RAIDD, and caspase-2. Recent whole-exome sequencing study showed that the RAIDD mutations in the death domain (DD), including G128R, F164C, R170C, and R170H mutations, cause thin lissencephaly (TLIS) by reducing caspase-2-mediated neuronal apoptosis. Given that the molecular structure of the RAIDD DD:PIDD DD complex is available, in this study, we analyzed the molecular mechanisms underlying TLIS caused by the RAIDD TLIS variants by performing mutagenesis and biochemical assays. Public Library of Science 2018-10-03 /pmc/articles/PMC6169973/ /pubmed/30281648 http://dx.doi.org/10.1371/journal.pone.0205042 Text en © 2018 Ha, Park http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Ha, Hyun Ji
Park, Hyun Ho
RAIDD mutations underlie the pathogenesis of thin lissencephaly (TLIS)
title RAIDD mutations underlie the pathogenesis of thin lissencephaly (TLIS)
title_full RAIDD mutations underlie the pathogenesis of thin lissencephaly (TLIS)
title_fullStr RAIDD mutations underlie the pathogenesis of thin lissencephaly (TLIS)
title_full_unstemmed RAIDD mutations underlie the pathogenesis of thin lissencephaly (TLIS)
title_short RAIDD mutations underlie the pathogenesis of thin lissencephaly (TLIS)
title_sort raidd mutations underlie the pathogenesis of thin lissencephaly (tlis)
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6169973/
https://www.ncbi.nlm.nih.gov/pubmed/30281648
http://dx.doi.org/10.1371/journal.pone.0205042
work_keys_str_mv AT hahyunji raiddmutationsunderliethepathogenesisofthinlissencephalytlis
AT parkhyunho raiddmutationsunderliethepathogenesisofthinlissencephalytlis

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