Structural insights into full-length human fascin1: a target for cancer treatment

13 pages, 7 figures, 2 tables

Detalles Bibliográficos
Autores: Giraldo-Ruiz, Lucía, Quereda-Moraleda, Isabel, Grieco, Alice, Ruiz-Sanz, Javier, Luque, Irene, Martín-García, José M.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2025
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/397089
Acceso en línea:http://hdl.handle.net/10261/397089
https://api.elsevier.com/content/abstract/scopus_id/105009988881
Access Level:acceso abierto
Palabra clave:X-ray crystallography
Actin-binding proteins
Cancer
Dynamics
Human fascin1
Metastasis
Plasticity
http://metadata.un.org/sdg/3
Ensure healthy lives and promote well-being for all at all ages
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spelling Structural insights into full-length human fascin1: a target for cancer treatmentGiraldo-Ruiz, LucíaQuereda-Moraleda, IsabelGrieco, AliceRuiz-Sanz, JavierLuque, IreneMartín-García, José M.X-ray crystallographyActin-binding proteinsCancerDynamicsHuman fascin1MetastasisPlasticityhttp://metadata.un.org/sdg/3Ensure healthy lives and promote well-being for all at all ages13 pages, 7 figures, 2 tablesFascin1 proteins are a family of globular proteins with actin-bundling activity that cross-link actin filaments together, allowing the formation of actin-rich structures involved in cell migration and adhesion, such as filopodia, invadopodia, stress fibers, micro-spikes and podocytes. The overexpression of human fascin1 has been linked to tumor progression in most human cancers, particularly during the epithelial-mesenchymal transition, making it a promising biomarker for cancer metastasis and a major target for the development of novel cancer therapies. X-ray crystallography has been instrumental in human fascin1-inhibition research since it provides detailed insights into the structure of the protein and its interactions with small-molecule inhibitors. This technique has allowed the characterization of a range of molecular conformations in which the protein naturally exists. However, human fascin1 has never been fully modeled until now. To the best of our knowledge, this study presents the first full-length structure of human fascin1 in which both copies are fully resolved. Comparison of this structure with the available wild-type and complexed structures provides new insights into the conformational plasticity of fascin1 that will facilitate subsequent studies on human fascin1 in the context of drug design for cancer-related therapies.The following funding is acknowledged: The European UnionNextGenerationEU/PRTR (grant No. CNS2022-135713),Ayuda de Atraccion y Retencion de Talento Investigadorfrom the Community of Madrid (No. 2019-T1/BMD-15552)and FEDER/Junta de Andalucia-Consejerıa de Transforma-cion Economica, Industria, Conocimiento y Universidades(grant Nos. PY20_00678 and B-BIO-18-UGR20).Peer reviewedWiley-VCHComunidad de MadridJunta de AndalucíaMinisterio de Ciencia e Innovación (España)#NODATA##NODATA##NODATA##NODATA##NODATA##NODATA#Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202520252025info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/397089https://api.elsevier.com/content/abstract/scopus_id/105009988881reponame: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//CNS2022-1357132019-T1/BMD-15552-CMhttps://doi.org/10.1107/S2053230X25005254Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3970892026-05-22T06:33:51Z
dc.title.none.fl_str_mv Structural insights into full-length human fascin1: a target for cancer treatment
title Structural insights into full-length human fascin1: a target for cancer treatment
spellingShingle Structural insights into full-length human fascin1: a target for cancer treatment
Giraldo-Ruiz, Lucía
X-ray crystallography
Actin-binding proteins
Cancer
Dynamics
Human fascin1
Metastasis
Plasticity
http://metadata.un.org/sdg/3
Ensure healthy lives and promote well-being for all at all ages
title_short Structural insights into full-length human fascin1: a target for cancer treatment
title_full Structural insights into full-length human fascin1: a target for cancer treatment
title_fullStr Structural insights into full-length human fascin1: a target for cancer treatment
title_full_unstemmed Structural insights into full-length human fascin1: a target for cancer treatment
title_sort Structural insights into full-length human fascin1: a target for cancer treatment
dc.creator.none.fl_str_mv Giraldo-Ruiz, Lucía
Quereda-Moraleda, Isabel
Grieco, Alice
Ruiz-Sanz, Javier
Luque, Irene
Martín-García, José M.
author Giraldo-Ruiz, Lucía
author_facet Giraldo-Ruiz, Lucía
Quereda-Moraleda, Isabel
Grieco, Alice
Ruiz-Sanz, Javier
Luque, Irene
Martín-García, José M.
author_role author
author2 Quereda-Moraleda, Isabel
Grieco, Alice
Ruiz-Sanz, Javier
Luque, Irene
Martín-García, José M.
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Comunidad de Madrid
Junta de Andalucía
Ministerio de Ciencia e Innovación (España)
#NODATA#
#NODATA#
#NODATA#
#NODATA#
#NODATA#
#NODATA#
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv X-ray crystallography
Actin-binding proteins
Cancer
Dynamics
Human fascin1
Metastasis
Plasticity
http://metadata.un.org/sdg/3
Ensure healthy lives and promote well-being for all at all ages
topic X-ray crystallography
Actin-binding proteins
Cancer
Dynamics
Human fascin1
Metastasis
Plasticity
http://metadata.un.org/sdg/3
Ensure healthy lives and promote well-being for all at all ages
description 13 pages, 7 figures, 2 tables
publishDate 2025
dc.date.none.fl_str_mv 2025
2025
2025
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/10261/397089
https://api.elsevier.com/content/abstract/scopus_id/105009988881
url http://hdl.handle.net/10261/397089
https://api.elsevier.com/content/abstract/scopus_id/105009988881
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//CNS2022-135713
2019-T1/BMD-15552-CM
https://doi.org/10.1107/S2053230X25005254
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Wiley-VCH
publisher.none.fl_str_mv Wiley-VCH
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
repository.name.fl_str_mv
repository.mail.fl_str_mv
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