Nanocompartmentalization of the Nuclear Pore Lumen

Autores
Huang, Kai; Tagliazucchi, Mario Eugenio; Park, Sung Hyun; Rabin, Yitzhak; Szleifer, Igal
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The nuclear pore complex (NPC) employs the intrinsically disordered regions (IDRs) from a family of phenylalanine-glycine-rich nucleoporins (FG-Nups) to control nucleocytoplasmic transport. It has been a long-standing mystery how the IDR-mediated mass exchange can be rapid yet selective. Here, we use a computational microscope to show that nanocompartmentalization of IDR subdomains leads to a remarkably elaborate gating structure as programmed by the amino acid sequences. In particular, we reveal a heterogeneous permeability barrier that combines an inner ring barrier with two vestibular condensates. Throughout the NPC, we find a polarized electrostatic potential and a diffuse thermoreversible FG network featuring mosaic FG territories with low FG-FG pairing fraction. Our theoretical anatomy of the central transporter sheds light into the sequence-structure-function relationship of the FG-Nups and provides a picture of nucleocytoplasmic mass exchange that allows a reconciliation of transport efficiency and specificity.
Fil: Huang, Kai. Northwestern University; Estados Unidos
Fil: Tagliazucchi, Mario Eugenio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Park, Sung Hyun. Northwestern University; Estados Unidos
Fil: Rabin, Yitzhak. Bar-Ilan University; Israel
Fil: Szleifer, Igal. Northwestern University; Estados Unidos
Materia
Nanopore
Nuclear pore complex
PROTEIN
Molecular theory
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/142584
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Nanocompartmentalization of the Nuclear Pore LumenHuang, KaiTagliazucchi, Mario EugenioPark, Sung HyunRabin, YitzhakSzleifer, IgalNanoporeNuclear pore complexPROTEINMolecular theoryhttps://purl.org/becyt/ford/1.3https://purl.org/becyt/ford/1The nuclear pore complex (NPC) employs the intrinsically disordered regions (IDRs) from a family of phenylalanine-glycine-rich nucleoporins (FG-Nups) to control nucleocytoplasmic transport. It has been a long-standing mystery how the IDR-mediated mass exchange can be rapid yet selective. Here, we use a computational microscope to show that nanocompartmentalization of IDR subdomains leads to a remarkably elaborate gating structure as programmed by the amino acid sequences. In particular, we reveal a heterogeneous permeability barrier that combines an inner ring barrier with two vestibular condensates. Throughout the NPC, we find a polarized electrostatic potential and a diffuse thermoreversible FG network featuring mosaic FG territories with low FG-FG pairing fraction. Our theoretical anatomy of the central transporter sheds light into the sequence-structure-function relationship of the FG-Nups and provides a picture of nucleocytoplasmic mass exchange that allows a reconciliation of transport efficiency and specificity.Fil: Huang, Kai. Northwestern University; Estados UnidosFil: Tagliazucchi, Mario Eugenio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; ArgentinaFil: Park, Sung Hyun. Northwestern University; Estados UnidosFil: Rabin, Yitzhak. Bar-Ilan University; IsraelFil: Szleifer, Igal. Northwestern University; Estados UnidosCell Press2020-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/142584Huang, Kai; Tagliazucchi, Mario Eugenio; Park, Sung Hyun; Rabin, Yitzhak; Szleifer, Igal; Nanocompartmentalization of the Nuclear Pore Lumen; Cell Press; Biophysical Journal; 118; 1; 5-2020; 219-2310006-3495CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpj.2019.11.024info:eu-repo/semantics/altIdentifier/url/https://www.cell.com/biophysj/fulltext/S0006-3495(19)30947-6info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:57:12Zoai:ri.conicet.gov.ar:11336/142584instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:57:12.725CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Nanocompartmentalization of the Nuclear Pore Lumen
title Nanocompartmentalization of the Nuclear Pore Lumen
spellingShingle Nanocompartmentalization of the Nuclear Pore Lumen
Huang, Kai
Nanopore
Nuclear pore complex
PROTEIN
Molecular theory
title_short Nanocompartmentalization of the Nuclear Pore Lumen
title_full Nanocompartmentalization of the Nuclear Pore Lumen
title_fullStr Nanocompartmentalization of the Nuclear Pore Lumen
title_full_unstemmed Nanocompartmentalization of the Nuclear Pore Lumen
title_sort Nanocompartmentalization of the Nuclear Pore Lumen
dc.creator.none.fl_str_mv Huang, Kai
Tagliazucchi, Mario Eugenio
Park, Sung Hyun
Rabin, Yitzhak
Szleifer, Igal
author Huang, Kai
author_facet Huang, Kai
Tagliazucchi, Mario Eugenio
Park, Sung Hyun
Rabin, Yitzhak
Szleifer, Igal
author_role author
author2 Tagliazucchi, Mario Eugenio
Park, Sung Hyun
Rabin, Yitzhak
Szleifer, Igal
author2_role author
author
author
author
dc.subject.none.fl_str_mv Nanopore
Nuclear pore complex
PROTEIN
Molecular theory
topic Nanopore
Nuclear pore complex
PROTEIN
Molecular theory
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.3
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The nuclear pore complex (NPC) employs the intrinsically disordered regions (IDRs) from a family of phenylalanine-glycine-rich nucleoporins (FG-Nups) to control nucleocytoplasmic transport. It has been a long-standing mystery how the IDR-mediated mass exchange can be rapid yet selective. Here, we use a computational microscope to show that nanocompartmentalization of IDR subdomains leads to a remarkably elaborate gating structure as programmed by the amino acid sequences. In particular, we reveal a heterogeneous permeability barrier that combines an inner ring barrier with two vestibular condensates. Throughout the NPC, we find a polarized electrostatic potential and a diffuse thermoreversible FG network featuring mosaic FG territories with low FG-FG pairing fraction. Our theoretical anatomy of the central transporter sheds light into the sequence-structure-function relationship of the FG-Nups and provides a picture of nucleocytoplasmic mass exchange that allows a reconciliation of transport efficiency and specificity.
Fil: Huang, Kai. Northwestern University; Estados Unidos
Fil: Tagliazucchi, Mario Eugenio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Park, Sung Hyun. Northwestern University; Estados Unidos
Fil: Rabin, Yitzhak. Bar-Ilan University; Israel
Fil: Szleifer, Igal. Northwestern University; Estados Unidos
description The nuclear pore complex (NPC) employs the intrinsically disordered regions (IDRs) from a family of phenylalanine-glycine-rich nucleoporins (FG-Nups) to control nucleocytoplasmic transport. It has been a long-standing mystery how the IDR-mediated mass exchange can be rapid yet selective. Here, we use a computational microscope to show that nanocompartmentalization of IDR subdomains leads to a remarkably elaborate gating structure as programmed by the amino acid sequences. In particular, we reveal a heterogeneous permeability barrier that combines an inner ring barrier with two vestibular condensates. Throughout the NPC, we find a polarized electrostatic potential and a diffuse thermoreversible FG network featuring mosaic FG territories with low FG-FG pairing fraction. Our theoretical anatomy of the central transporter sheds light into the sequence-structure-function relationship of the FG-Nups and provides a picture of nucleocytoplasmic mass exchange that allows a reconciliation of transport efficiency and specificity.
publishDate 2020
dc.date.none.fl_str_mv 2020-05
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/142584
Huang, Kai; Tagliazucchi, Mario Eugenio; Park, Sung Hyun; Rabin, Yitzhak; Szleifer, Igal; Nanocompartmentalization of the Nuclear Pore Lumen; Cell Press; Biophysical Journal; 118; 1; 5-2020; 219-231
0006-3495
CONICET Digital
CONICET
url http://hdl.handle.net/11336/142584
identifier_str_mv Huang, Kai; Tagliazucchi, Mario Eugenio; Park, Sung Hyun; Rabin, Yitzhak; Szleifer, Igal; Nanocompartmentalization of the Nuclear Pore Lumen; Cell Press; Biophysical Journal; 118; 1; 5-2020; 219-231
0006-3495
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpj.2019.11.024
info:eu-repo/semantics/altIdentifier/url/https://www.cell.com/biophysj/fulltext/S0006-3495(19)30947-6
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Cell Press
publisher.none.fl_str_mv Cell Press
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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