Identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cells

The double membrane nuclear envelope (NE), which is contiguous with the ER, contains nuclear pore complexes (NPCs) - the channels for nucleocytoplasmic transport, and the nuclear lamina (NL) - a scaffold for NE and chromatin organization. Since numerous human diseases linked to NE proteins occur in...

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Autores: Cheng, Li-Chun, Baboo, Sabyasachi, Lindsay, Cory, Brusman, Liza, Martinez-Bartolomé, Salvador, Tapia Martínez, Olga, Zhang, Xi, Yates, John R. 3o, Gerace, Larry
Tipo de recurso: artículo
Fecha de publicación:2019
País:España
Institución:Universidad de Cantabria (UC)
Repositorio:UCrea Repositorio Abierto de la Universidad de Cantabria
Idioma:inglés
OAI Identifier:oai:repositorio.unican.es:10902/20196
Acceso en línea:http://hdl.handle.net/10902/20196
Access Level:acceso abierto
Palabra clave:Nuclear Envelope
Nuclear Pore Complex (NPC)
Proteomics
Mesenchymal Stem Cell (MSC)
Adipocyte
Myocyte
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spelling Identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cellsCheng, Li-ChunBaboo, SabyasachiLindsay, CoryBrusman, LizaMartinez-Bartolomé, SalvadorTapia Martínez, OlgaZhang, XiYates, John R. 3oGerace, LarryNuclear EnvelopeNuclear Pore Complex (NPC)ProteomicsMesenchymal Stem Cell (MSC)AdipocyteMyocyteThe double membrane nuclear envelope (NE), which is contiguous with the ER, contains nuclear pore complexes (NPCs) - the channels for nucleocytoplasmic transport, and the nuclear lamina (NL) - a scaffold for NE and chromatin organization. Since numerous human diseases linked to NE proteins occur in mesenchyme-derived cells, we used proteomics to characterize NE and other subcellular fractions isolated from mesenchymal stem cells and from adipocytes and myocytes. Based on spectral abundance, we calculated enrichment scores for proteins in the NE fractions. We demonstrated by quantitative immunofluorescence microscopy that five little-characterized proteins with high enrichment scores are substantially concentrated at the NE, with Itprip exposed at the outer nuclear membrane, Smpd4 enriched at the NPC, and Mfsd10, Tmx4, and Arl6ip6 likely residing in the inner nuclear membrane. These proteins provide new focal points for studying the functions of the NE. Moreover, our datasets provide a resource for evaluating additional potential NE proteins.Taylor & FrancisUniversidad de Cantabria20192019-01-01journal articlehttp://purl.org/coar/resource_type/c_6501NAhttp://purl.org/coar/version/c_be7fb7dd8ff6fe43info:eu-repo/semantics/articlehttp://hdl.handle.net/10902/20196Nucleus . 2019 Dec;10(1):126-143.reponame:UCrea Repositorio Abierto de la Universidad de Cantabriainstname:Universidad de Cantabria (UC)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Attribution 4.0 Internationalhttp://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:repositorio.unican.es:10902/201962026-06-02T12:39:31Z
dc.title.none.fl_str_mv Identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cells
title Identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cells
spellingShingle Identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cells
Cheng, Li-Chun
Nuclear Envelope
Nuclear Pore Complex (NPC)
Proteomics
Mesenchymal Stem Cell (MSC)
Adipocyte
Myocyte
title_short Identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cells
title_full Identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cells
title_fullStr Identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cells
title_full_unstemmed Identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cells
title_sort Identification of new transmembrane proteins concentrated at the nuclear envelope using organellar proteomics of mesenchymal cells
dc.creator.none.fl_str_mv Cheng, Li-Chun
Baboo, Sabyasachi
Lindsay, Cory
Brusman, Liza
Martinez-Bartolomé, Salvador
Tapia Martínez, Olga
Zhang, Xi
Yates, John R. 3o
Gerace, Larry
author Cheng, Li-Chun
author_facet Cheng, Li-Chun
Baboo, Sabyasachi
Lindsay, Cory
Brusman, Liza
Martinez-Bartolomé, Salvador
Tapia Martínez, Olga
Zhang, Xi
Yates, John R. 3o
Gerace, Larry
author_role author
author2 Baboo, Sabyasachi
Lindsay, Cory
Brusman, Liza
Martinez-Bartolomé, Salvador
Tapia Martínez, Olga
Zhang, Xi
Yates, John R. 3o
Gerace, Larry
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidad de Cantabria
dc.subject.none.fl_str_mv Nuclear Envelope
Nuclear Pore Complex (NPC)
Proteomics
Mesenchymal Stem Cell (MSC)
Adipocyte
Myocyte
topic Nuclear Envelope
Nuclear Pore Complex (NPC)
Proteomics
Mesenchymal Stem Cell (MSC)
Adipocyte
Myocyte
description The double membrane nuclear envelope (NE), which is contiguous with the ER, contains nuclear pore complexes (NPCs) - the channels for nucleocytoplasmic transport, and the nuclear lamina (NL) - a scaffold for NE and chromatin organization. Since numerous human diseases linked to NE proteins occur in mesenchyme-derived cells, we used proteomics to characterize NE and other subcellular fractions isolated from mesenchymal stem cells and from adipocytes and myocytes. Based on spectral abundance, we calculated enrichment scores for proteins in the NE fractions. We demonstrated by quantitative immunofluorescence microscopy that five little-characterized proteins with high enrichment scores are substantially concentrated at the NE, with Itprip exposed at the outer nuclear membrane, Smpd4 enriched at the NPC, and Mfsd10, Tmx4, and Arl6ip6 likely residing in the inner nuclear membrane. These proteins provide new focal points for studying the functions of the NE. Moreover, our datasets provide a resource for evaluating additional potential NE proteins.
publishDate 2019
dc.date.none.fl_str_mv 2019
2019-01-01
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
NA
http://purl.org/coar/version/c_be7fb7dd8ff6fe43
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10902/20196
url http://hdl.handle.net/10902/20196
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution 4.0 International
http://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
Attribution 4.0 International
http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Taylor & Francis
publisher.none.fl_str_mv Taylor & Francis
dc.source.none.fl_str_mv Nucleus . 2019 Dec;10(1):126-143.
reponame:UCrea Repositorio Abierto de la Universidad de Cantabria
instname:Universidad de Cantabria (UC)
instname_str Universidad de Cantabria (UC)
reponame_str UCrea Repositorio Abierto de la Universidad de Cantabria
collection UCrea Repositorio Abierto de la Universidad de Cantabria
repository.name.fl_str_mv
repository.mail.fl_str_mv
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