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TRIP6 functions in brain ciliogenesis
TRIP6, a member of the ZYXIN-family of LIM domain proteins, is a focal adhesion component. Trip6 deletion in the mouse, reported here, reveals a function in the brain: ependymal and choroid plexus epithelial cells are carrying, unexpectedly, fewer and shorter cilia, are poorly differentiated, and th...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8497538/ https://www.ncbi.nlm.nih.gov/pubmed/34620853 http://dx.doi.org/10.1038/s41467-021-26057-6 |
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author | Shukla, Shalmali Haenold, Ronny Urbánek, Pavel Frappart, Lucien Monajembashi, Shamci Grigaravicius, Paulius Nagel, Sigrun Min, Woo Kee Tapias, Alicia Kassel, Olivier Heuer, Heike Wang, Zhao-Qi Ploubidou, Aspasia Herrlich, Peter |
author_facet | Shukla, Shalmali Haenold, Ronny Urbánek, Pavel Frappart, Lucien Monajembashi, Shamci Grigaravicius, Paulius Nagel, Sigrun Min, Woo Kee Tapias, Alicia Kassel, Olivier Heuer, Heike Wang, Zhao-Qi Ploubidou, Aspasia Herrlich, Peter |
author_sort | Shukla, Shalmali |
collection | PubMed |
description | TRIP6, a member of the ZYXIN-family of LIM domain proteins, is a focal adhesion component. Trip6 deletion in the mouse, reported here, reveals a function in the brain: ependymal and choroid plexus epithelial cells are carrying, unexpectedly, fewer and shorter cilia, are poorly differentiated, and the mice develop hydrocephalus. TRIP6 carries numerous protein interaction domains and its functions require homodimerization. Indeed, TRIP6 disruption in vitro (in a choroid plexus epithelial cell line), via RNAi or inhibition of its homodimerization, confirms its function in ciliogenesis. Using super-resolution microscopy, we demonstrate TRIP6 localization at the pericentriolar material and along the ciliary axoneme. The requirement for homodimerization which doubles its interaction sites, its punctate localization along the axoneme, and its co-localization with other cilia components suggest a scaffold/co-transporter function for TRIP6 in cilia. Thus, this work uncovers an essential role of a LIM-domain protein assembly factor in mammalian ciliogenesis. |
format | Online Article Text |
id | pubmed-8497538 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-84975382021-10-22 TRIP6 functions in brain ciliogenesis Shukla, Shalmali Haenold, Ronny Urbánek, Pavel Frappart, Lucien Monajembashi, Shamci Grigaravicius, Paulius Nagel, Sigrun Min, Woo Kee Tapias, Alicia Kassel, Olivier Heuer, Heike Wang, Zhao-Qi Ploubidou, Aspasia Herrlich, Peter Nat Commun Article TRIP6, a member of the ZYXIN-family of LIM domain proteins, is a focal adhesion component. Trip6 deletion in the mouse, reported here, reveals a function in the brain: ependymal and choroid plexus epithelial cells are carrying, unexpectedly, fewer and shorter cilia, are poorly differentiated, and the mice develop hydrocephalus. TRIP6 carries numerous protein interaction domains and its functions require homodimerization. Indeed, TRIP6 disruption in vitro (in a choroid plexus epithelial cell line), via RNAi or inhibition of its homodimerization, confirms its function in ciliogenesis. Using super-resolution microscopy, we demonstrate TRIP6 localization at the pericentriolar material and along the ciliary axoneme. The requirement for homodimerization which doubles its interaction sites, its punctate localization along the axoneme, and its co-localization with other cilia components suggest a scaffold/co-transporter function for TRIP6 in cilia. Thus, this work uncovers an essential role of a LIM-domain protein assembly factor in mammalian ciliogenesis. Nature Publishing Group UK 2021-10-07 /pmc/articles/PMC8497538/ /pubmed/34620853 http://dx.doi.org/10.1038/s41467-021-26057-6 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Shukla, Shalmali Haenold, Ronny Urbánek, Pavel Frappart, Lucien Monajembashi, Shamci Grigaravicius, Paulius Nagel, Sigrun Min, Woo Kee Tapias, Alicia Kassel, Olivier Heuer, Heike Wang, Zhao-Qi Ploubidou, Aspasia Herrlich, Peter TRIP6 functions in brain ciliogenesis |
title | TRIP6 functions in brain ciliogenesis |
title_full | TRIP6 functions in brain ciliogenesis |
title_fullStr | TRIP6 functions in brain ciliogenesis |
title_full_unstemmed | TRIP6 functions in brain ciliogenesis |
title_short | TRIP6 functions in brain ciliogenesis |
title_sort | trip6 functions in brain ciliogenesis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8497538/ https://www.ncbi.nlm.nih.gov/pubmed/34620853 http://dx.doi.org/10.1038/s41467-021-26057-6 |
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