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Stress-induced phosphorylation of CLIP-170 by JNK promotes microtubule rescue
The stress-induced c-Jun N-terminal kinase (JNK) controls microtubule dynamics by enhancing both microtubule growth and rescues. Here, we show that upon cell stress, JNK directly phosphorylates the microtubule rescue factor CLIP-170 in its microtubule-binding domain to increase its rescue-promoting...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Rockefeller University Press
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7337496/ https://www.ncbi.nlm.nih.gov/pubmed/32491151 http://dx.doi.org/10.1083/jcb.201909093 |
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author | Henrie, Hélène Bakhos-Douaihy, Dalal Cantaloube, Isabelle Pilon, Antoine Talantikite, Maya Stoppin-Mellet, Virginie Baillet, Anita Poüs, Christian Benoit, Béatrice |
author_facet | Henrie, Hélène Bakhos-Douaihy, Dalal Cantaloube, Isabelle Pilon, Antoine Talantikite, Maya Stoppin-Mellet, Virginie Baillet, Anita Poüs, Christian Benoit, Béatrice |
author_sort | Henrie, Hélène |
collection | PubMed |
description | The stress-induced c-Jun N-terminal kinase (JNK) controls microtubule dynamics by enhancing both microtubule growth and rescues. Here, we show that upon cell stress, JNK directly phosphorylates the microtubule rescue factor CLIP-170 in its microtubule-binding domain to increase its rescue-promoting activity. Phosphomimetic versions of CLIP-170 enhance its ability to promote rescue events in vitro and in cells. Furthermore, while phosphomimetic mutations do not alter CLIP-170’s capability to form comets at growing microtubule ends, both phosphomimetic mutations and JNK activation increase the occurrence of CLIP-170 remnants on the microtubule lattice at the rear of comets. As the CLIP-170 remnants, which are potential sites of microtubule rescue, display a shorter lifetime when CLIP-170 is phosphorylated, we propose that instead of acting at the time of rescue occurrence, CLIP-170 would rather contribute in preparing the microtubule lattice for future rescues at these predetermined sites. |
format | Online Article Text |
id | pubmed-7337496 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-73374962021-01-06 Stress-induced phosphorylation of CLIP-170 by JNK promotes microtubule rescue Henrie, Hélène Bakhos-Douaihy, Dalal Cantaloube, Isabelle Pilon, Antoine Talantikite, Maya Stoppin-Mellet, Virginie Baillet, Anita Poüs, Christian Benoit, Béatrice J Cell Biol Article The stress-induced c-Jun N-terminal kinase (JNK) controls microtubule dynamics by enhancing both microtubule growth and rescues. Here, we show that upon cell stress, JNK directly phosphorylates the microtubule rescue factor CLIP-170 in its microtubule-binding domain to increase its rescue-promoting activity. Phosphomimetic versions of CLIP-170 enhance its ability to promote rescue events in vitro and in cells. Furthermore, while phosphomimetic mutations do not alter CLIP-170’s capability to form comets at growing microtubule ends, both phosphomimetic mutations and JNK activation increase the occurrence of CLIP-170 remnants on the microtubule lattice at the rear of comets. As the CLIP-170 remnants, which are potential sites of microtubule rescue, display a shorter lifetime when CLIP-170 is phosphorylated, we propose that instead of acting at the time of rescue occurrence, CLIP-170 would rather contribute in preparing the microtubule lattice for future rescues at these predetermined sites. Rockefeller University Press 2020-06-03 /pmc/articles/PMC7337496/ /pubmed/32491151 http://dx.doi.org/10.1083/jcb.201909093 Text en © 2020 Henrie et al. http://www.rupress.org/terms/https://creativecommons.org/licenses/by-nc-sa/4.0/This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Article Henrie, Hélène Bakhos-Douaihy, Dalal Cantaloube, Isabelle Pilon, Antoine Talantikite, Maya Stoppin-Mellet, Virginie Baillet, Anita Poüs, Christian Benoit, Béatrice Stress-induced phosphorylation of CLIP-170 by JNK promotes microtubule rescue |
title | Stress-induced phosphorylation of CLIP-170 by JNK promotes microtubule rescue |
title_full | Stress-induced phosphorylation of CLIP-170 by JNK promotes microtubule rescue |
title_fullStr | Stress-induced phosphorylation of CLIP-170 by JNK promotes microtubule rescue |
title_full_unstemmed | Stress-induced phosphorylation of CLIP-170 by JNK promotes microtubule rescue |
title_short | Stress-induced phosphorylation of CLIP-170 by JNK promotes microtubule rescue |
title_sort | stress-induced phosphorylation of clip-170 by jnk promotes microtubule rescue |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7337496/ https://www.ncbi.nlm.nih.gov/pubmed/32491151 http://dx.doi.org/10.1083/jcb.201909093 |
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