Allosteric control of dynamin-related protein 1 through a disordered C-terminal Short Linear Motif

© The Author(s) 2024. 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, p...

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Autores: Pérez-Jover, Isabel, Rochon, Kristy, Hu, Di, Mahajan, Mukesh, Madan Mohan, Pooja, Santos-Pérez, Isaac, Ormaetxea Gisasola, Julene, Martínez Gálvez, Juan Manuel, Agirre, Jon, Qi, Xin, Mears, Jason A., Shnyrova, Anna V., Ramachandran, Rajesh
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2024
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/355255
Acceso en línea:http://hdl.handle.net/10261/355255
Access Level:acceso abierto
Palabra clave:Intrinsically disordered proteins
Membrane proteins
Mitochondrial proteins
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dc.title.none.fl_str_mv Allosteric control of dynamin-related protein 1 through a disordered C-terminal Short Linear Motif
title Allosteric control of dynamin-related protein 1 through a disordered C-terminal Short Linear Motif
spellingShingle Allosteric control of dynamin-related protein 1 through a disordered C-terminal Short Linear Motif
Pérez-Jover, Isabel
Intrinsically disordered proteins
Membrane proteins
Mitochondrial proteins
title_short Allosteric control of dynamin-related protein 1 through a disordered C-terminal Short Linear Motif
title_full Allosteric control of dynamin-related protein 1 through a disordered C-terminal Short Linear Motif
title_fullStr Allosteric control of dynamin-related protein 1 through a disordered C-terminal Short Linear Motif
title_full_unstemmed Allosteric control of dynamin-related protein 1 through a disordered C-terminal Short Linear Motif
title_sort Allosteric control of dynamin-related protein 1 through a disordered C-terminal Short Linear Motif
dc.creator.none.fl_str_mv Pérez-Jover, Isabel
Rochon, Kristy
Hu, Di
Mahajan, Mukesh
Madan Mohan, Pooja
Santos-Pérez, Isaac
Ormaetxea Gisasola, Julene
Martínez Gálvez, Juan Manuel
Agirre, Jon
Qi, Xin
Mears, Jason A.
Shnyrova, Anna V.
Ramachandran, Rajesh
author Pérez-Jover, Isabel
author_facet Pérez-Jover, Isabel
Rochon, Kristy
Hu, Di
Mahajan, Mukesh
Madan Mohan, Pooja
Santos-Pérez, Isaac
Ormaetxea Gisasola, Julene
Martínez Gálvez, Juan Manuel
Agirre, Jon
Qi, Xin
Mears, Jason A.
Shnyrova, Anna V.
Ramachandran, Rajesh
author_role author
author2 Rochon, Kristy
Hu, Di
Mahajan, Mukesh
Madan Mohan, Pooja
Santos-Pérez, Isaac
Ormaetxea Gisasola, Julene
Martínez Gálvez, Juan Manuel
Agirre, Jon
Qi, Xin
Mears, Jason A.
Shnyrova, Anna V.
Ramachandran, Rajesh
author2_role author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia, Innovación y Universidades (España)
Ministerio de Ciencia e Innovación (España)
Agencia Estatal de Investigación (España)
European Commission
Eusko Jaurlaritza
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Intrinsically disordered proteins
Membrane proteins
Mitochondrial proteins
topic Intrinsically disordered proteins
Membrane proteins
Mitochondrial proteins
description © The Author(s) 2024. 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/.
publishDate 2024
dc.date.none.fl_str_mv 2024
2024
2024
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/355255
url http://hdl.handle.net/10261/355255
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PGC2018-099971-B-I00
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2021-127844NB-I00
Previously published high-resolution Drp1 structures referred to in our manuscript are readily accessible from the protein data bank (PDB) via accession codes: 4BEJ and 5WP9. The particle numbers analyzed for generating 2D class averages and their relative percentages are noted in Methods. Source data are provided with this paper.
The underlying dataset has been published as supplementary material of the article in the publisher platform at https://doi.org/10.1038/s41467-023-44413-6
https://doi.org/10.1038/s41467-023-44413-6
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
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spelling Allosteric control of dynamin-related protein 1 through a disordered C-terminal Short Linear MotifPérez-Jover, IsabelRochon, KristyHu, DiMahajan, MukeshMadan Mohan, PoojaSantos-Pérez, IsaacOrmaetxea Gisasola, JuleneMartínez Gálvez, Juan ManuelAgirre, JonQi, XinMears, Jason A.Shnyrova, Anna V.Ramachandran, RajeshIntrinsically disordered proteinsMembrane proteinsMitochondrial proteins© The Author(s) 2024. 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/.The mechanochemical GTPase dynamin-related protein 1 (Drp1) catalyzes mitochondrial and peroxisomal fission, but the regulatory mechanisms remain ambiguous. Here we find that a conserved, intrinsically disordered, six-residue Short Linear Motif at the extreme Drp1 C-terminus, named CT-SLiM, constitutes a critical allosteric site that controls Drp1 structure and function in vitro and in vivo. Extension of the CT-SLiM by non-native residues, or its interaction with the protein partner GIPC-1, constrains Drp1 subunit conformational dynamics, alters self-assembly properties, and limits cooperative GTP hydrolysis, surprisingly leading to the fission of model membranes in vitro. In vivo, the involvement of the native CT-SLiM is critical for productive mitochondrial and peroxisomal fission, as both deletion and non-native extension of the CT-SLiM severely impair their progression. Thus, contrary to prevailing models, Drp1-catalyzed membrane fission relies on allosteric communication mediated by the CT-SLiM, deceleration of GTPase activity, and coupled changes in subunit architecture and assembly-disassembly dynamics.Work in the A.V.S. laboratory was supported by the PGC2018-099971-B-I00 and PID2021-127844NB-I00 grants funded by MCIN/AEI/10.13039/501100011033/ and by “ERDF A way of making Europe” and by the Basque Government Grant IT1625-22.Peer reviewedNature Publishing GroupMinisterio de Ciencia, Innovación y Universidades (España)Ministerio de Ciencia e Innovación (España)Agencia Estatal de Investigación (España)European CommissionEusko JaurlaritzaConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202420242024info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10261/355255reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PGC2018-099971-B-I00info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2021-127844NB-I00Previously published high-resolution Drp1 structures referred to in our manuscript are readily accessible from the protein data bank (PDB) via accession codes: 4BEJ and 5WP9. The particle numbers analyzed for generating 2D class averages and their relative percentages are noted in Methods. Source data are provided with this paper.The underlying dataset has been published as supplementary material of the article in the publisher platform at https://doi.org/10.1038/s41467-023-44413-6https://doi.org/10.1038/s41467-023-44413-6Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3552552026-05-22T06:33:51Z
score 15,811543

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