Decoding the role of coiled-coil motifs in human prion-like proteins

Prions are self-propagating proteins that cause fatal neurodegenerative diseases in humans. However, increasing evidence suggests that eukaryotic cells exploit prion conformational conversion for functional purposes. A recent study delineated a group of twenty prion-like proteins in humans, characte...

Descripción completa

Detalles Bibliográficos
Autores: Behbahanipour, Molood|||0000-0002-7889-6105, Garcia-Pardo, Javier|||0000-0001-9179-6371, Ventura, Salvador|||0000-0002-9652-6351
Tipo de recurso: artículo
Fecha de publicación:2021
País:España
Institución:Universitat Autònoma de Barcelona
Repositorio:Dipòsit Digital de Documents de la UAB
Idioma:inglés
OAI Identifier:oai:ddd.uab.cat:271675
Acceso en línea:https://ddd.uab.cat/record/271675
https://dx.doi.org/urn:doi:10.1080/19336896.2021.1961569
Access Level:acceso abierto
Palabra clave:Prions
Amyloids
Prion-like domains
Coiled-coils
Protein aggregation
id ES_05f662bcddba0fec9d7f88dec89a53bb
oai_identifier_str oai:ddd.uab.cat:271675
network_acronym_str ES
network_name_str España
repository_id_str
spelling Decoding the role of coiled-coil motifs in human prion-like proteinsBehbahanipour, Molood|||0000-0002-7889-6105Garcia-Pardo, Javier|||0000-0001-9179-6371Ventura, Salvador|||0000-0002-9652-6351PrionsAmyloidsPrion-like domainsCoiled-coilsProtein aggregationPrions are self-propagating proteins that cause fatal neurodegenerative diseases in humans. However, increasing evidence suggests that eukaryotic cells exploit prion conformational conversion for functional purposes. A recent study delineated a group of twenty prion-like proteins in humans, characterized by the presence of low-complexity glutamine-rich sequences with overlapping coiled-coil (CCs) motifs. This is the case of Mediator complex subunit 15 (MED15), which is overexpressed in a wide range of human cancers. Biophysical studies demonstrated that the prion-like domain (PrLD) of MED15 forms homodimers in solution, sustained by CCs interactions. Furthermore, the same coiled-coil (CC) region plays a crucial role in the PrLD structural transition to a transmissible β-sheet amyloid state. In this review, we discuss the role of CCs motifs and their contribution to amyloid transitions in human prion-like domains (PrLDs), while providing a comprehensive overview of six predicted human prion-like proteins involved in transcription, gene expression, or DNA damage response and associated with human disease, whose PrLDs contain or overlap with CCs sequences. Finally, we try to rationalize how these molecular signatures might relate to both their function and involvement in disease. 22021-01-0120212021-01-01Articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://ddd.uab.cat/record/271675https://dx.doi.org/urn:doi:10.1080/19336896.2021.1961569reponame:Dipòsit Digital de Documents de la UABinstname:Universitat Autònoma de BarcelonaInglésengAgencia Estatal de Investigación https://doi.org/10.13039/501100011033 PID2019-105017RB-I00Ministerio de Ciencia e Innovación https://doi.org/10.13039/501100004837 IJC2019-041039-Iopen accesshttp://purl.org/coar/access_right/c_abf2Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original.https://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:ddd.uab.cat:2716752026-06-06T12:50:31Z
dc.title.none.fl_str_mv Decoding the role of coiled-coil motifs in human prion-like proteins
title Decoding the role of coiled-coil motifs in human prion-like proteins
spellingShingle Decoding the role of coiled-coil motifs in human prion-like proteins
Behbahanipour, Molood|||0000-0002-7889-6105
Prions
Amyloids
Prion-like domains
Coiled-coils
Protein aggregation
title_short Decoding the role of coiled-coil motifs in human prion-like proteins
title_full Decoding the role of coiled-coil motifs in human prion-like proteins
title_fullStr Decoding the role of coiled-coil motifs in human prion-like proteins
title_full_unstemmed Decoding the role of coiled-coil motifs in human prion-like proteins
title_sort Decoding the role of coiled-coil motifs in human prion-like proteins
dc.creator.none.fl_str_mv Behbahanipour, Molood|||0000-0002-7889-6105
Garcia-Pardo, Javier|||0000-0001-9179-6371
Ventura, Salvador|||0000-0002-9652-6351
author Behbahanipour, Molood|||0000-0002-7889-6105
author_facet Behbahanipour, Molood|||0000-0002-7889-6105
Garcia-Pardo, Javier|||0000-0001-9179-6371
Ventura, Salvador|||0000-0002-9652-6351
author_role author
author2 Garcia-Pardo, Javier|||0000-0001-9179-6371
Ventura, Salvador|||0000-0002-9652-6351
author2_role author
author
dc.subject.none.fl_str_mv Prions
Amyloids
Prion-like domains
Coiled-coils
Protein aggregation
topic Prions
Amyloids
Prion-like domains
Coiled-coils
Protein aggregation
description Prions are self-propagating proteins that cause fatal neurodegenerative diseases in humans. However, increasing evidence suggests that eukaryotic cells exploit prion conformational conversion for functional purposes. A recent study delineated a group of twenty prion-like proteins in humans, characterized by the presence of low-complexity glutamine-rich sequences with overlapping coiled-coil (CCs) motifs. This is the case of Mediator complex subunit 15 (MED15), which is overexpressed in a wide range of human cancers. Biophysical studies demonstrated that the prion-like domain (PrLD) of MED15 forms homodimers in solution, sustained by CCs interactions. Furthermore, the same coiled-coil (CC) region plays a crucial role in the PrLD structural transition to a transmissible β-sheet amyloid state. In this review, we discuss the role of CCs motifs and their contribution to amyloid transitions in human prion-like domains (PrLDs), while providing a comprehensive overview of six predicted human prion-like proteins involved in transcription, gene expression, or DNA damage response and associated with human disease, whose PrLDs contain or overlap with CCs sequences. Finally, we try to rationalize how these molecular signatures might relate to both their function and involvement in disease.
publishDate 2021
dc.date.none.fl_str_mv 2
2021-01-01
2021
2021-01-01
dc.type.none.fl_str_mv Article
http://purl.org/coar/resource_type/c_6501
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://ddd.uab.cat/record/271675
https://dx.doi.org/urn:doi:10.1080/19336896.2021.1961569
url https://ddd.uab.cat/record/271675
https://dx.doi.org/urn:doi:10.1080/19336896.2021.1961569
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.relation.none.fl_str_mv Agencia Estatal de Investigación https://doi.org/10.13039/501100011033 PID2019-105017RB-I00
Ministerio de Ciencia e Innovación https://doi.org/10.13039/501100004837 IJC2019-041039-I
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Dipòsit Digital de Documents de la UAB
instname:Universitat Autònoma de Barcelona
instname_str Universitat Autònoma de Barcelona
reponame_str Dipòsit Digital de Documents de la UAB
collection Dipòsit Digital de Documents de la UAB
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869402888154906624
score 15,300719

Similares en LA Referencia