The Ectodomains of rBAT and 4F2hc Are Fake or Orphan α-Glucosidases

It is known that 4F2hc and rBAT are the heavy subunits of the heteromeric amino acid transporters (HATs). These heavy subunits are N-glycosylated proteins, with an N-terminal domain, one transmembrane domain and a bulky extracellular domain (ectodomain) that belongs to the α-amylase family. The heav...

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Autores: Fort i Baixeras, Joana, Nicolàs-Aragó, Adrià, Palacín Prieto, Manuel
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2021
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/184216
Acceso en línea:https://hdl.handle.net/2445/184216
Access Level:acceso abierto
Palabra clave:Proteïnes portadores
Proteïnes de membrana
Carrier proteins
Membrane proteins
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spelling The Ectodomains of rBAT and 4F2hc Are Fake or Orphan α-GlucosidasesFort i Baixeras, JoanaNicolàs-Aragó, AdriàPalacín Prieto, ManuelProteïnes portadoresProteïnes de membranaCarrier proteinsMembrane proteinsIt is known that 4F2hc and rBAT are the heavy subunits of the heteromeric amino acid transporters (HATs). These heavy subunits are N-glycosylated proteins, with an N-terminal domain, one transmembrane domain and a bulky extracellular domain (ectodomain) that belongs to the α-amylase family. The heavy subunits are covalently linked to a light subunit from the SLC7 family, which is responsible for the amino acid transport activity, forming a heterodimer. The functions of 4F2hc and rBAT are related mainly to the stability and trafficking of the HATs in the plasma membrane of vertebrates, where they exert the transport activity. Moreover, 4F2hc is a modulator of integrin signaling, has a role in cell fusion and it is overexpressed in some types of cancers. On the other hand, some mutations in rBAT are found to cause the malfunctioning of the b0,+ transport system, leading to cystinuria. The ectodomains of 4F2hc and rBAT share both sequence and structure homology with α-amylase family members. Very recently, cryo-EM has revealed the structure of several HATs, including the ectodomains of rBAT and 4F2hc. Here, we analyze available data on the ectodomains of rBAT and 4Fhc and their relationship with the α-amylase family. The physiological relevance of this relationship remains largely unknown. Keywords: N-glycosylation; SLC3; alpha-amylase; alpha-glucosidase; ancillary protein; ectodomain; scaffold protein; structure; transporter.MDPI2021info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/184216Articles publicats en revistes (Bioquímica i Biomedicina Molecular)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésReproducció del document publicat a: https://doi.org/10.3390/molecules26206231Molecules, 2021, vol. 26, num. 20, p. 1-13https://doi.org/10.3390/molecules26206231cc-by (c) Fort i Baixeras, Joana et al., 2021https://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/1842162026-05-27T06:46:51Z
dc.title.none.fl_str_mv The Ectodomains of rBAT and 4F2hc Are Fake or Orphan α-Glucosidases
title The Ectodomains of rBAT and 4F2hc Are Fake or Orphan α-Glucosidases
spellingShingle The Ectodomains of rBAT and 4F2hc Are Fake or Orphan α-Glucosidases
Fort i Baixeras, Joana
Proteïnes portadores
Proteïnes de membrana
Carrier proteins
Membrane proteins
title_short The Ectodomains of rBAT and 4F2hc Are Fake or Orphan α-Glucosidases
title_full The Ectodomains of rBAT and 4F2hc Are Fake or Orphan α-Glucosidases
title_fullStr The Ectodomains of rBAT and 4F2hc Are Fake or Orphan α-Glucosidases
title_full_unstemmed The Ectodomains of rBAT and 4F2hc Are Fake or Orphan α-Glucosidases
title_sort The Ectodomains of rBAT and 4F2hc Are Fake or Orphan α-Glucosidases
dc.creator.none.fl_str_mv Fort i Baixeras, Joana
Nicolàs-Aragó, Adrià
Palacín Prieto, Manuel
author Fort i Baixeras, Joana
author_facet Fort i Baixeras, Joana
Nicolàs-Aragó, Adrià
Palacín Prieto, Manuel
author_role author
author2 Nicolàs-Aragó, Adrià
Palacín Prieto, Manuel
author2_role author
author
dc.subject.none.fl_str_mv Proteïnes portadores
Proteïnes de membrana
Carrier proteins
Membrane proteins
topic Proteïnes portadores
Proteïnes de membrana
Carrier proteins
Membrane proteins
description It is known that 4F2hc and rBAT are the heavy subunits of the heteromeric amino acid transporters (HATs). These heavy subunits are N-glycosylated proteins, with an N-terminal domain, one transmembrane domain and a bulky extracellular domain (ectodomain) that belongs to the α-amylase family. The heavy subunits are covalently linked to a light subunit from the SLC7 family, which is responsible for the amino acid transport activity, forming a heterodimer. The functions of 4F2hc and rBAT are related mainly to the stability and trafficking of the HATs in the plasma membrane of vertebrates, where they exert the transport activity. Moreover, 4F2hc is a modulator of integrin signaling, has a role in cell fusion and it is overexpressed in some types of cancers. On the other hand, some mutations in rBAT are found to cause the malfunctioning of the b0,+ transport system, leading to cystinuria. The ectodomains of 4F2hc and rBAT share both sequence and structure homology with α-amylase family members. Very recently, cryo-EM has revealed the structure of several HATs, including the ectodomains of rBAT and 4F2hc. Here, we analyze available data on the ectodomains of rBAT and 4Fhc and their relationship with the α-amylase family. The physiological relevance of this relationship remains largely unknown. Keywords: N-glycosylation; SLC3; alpha-amylase; alpha-glucosidase; ancillary protein; ectodomain; scaffold protein; structure; transporter.
publishDate 2021
dc.date.none.fl_str_mv 2021
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/184216
url https://hdl.handle.net/2445/184216
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.3390/molecules26206231
Molecules, 2021, vol. 26, num. 20, p. 1-13
https://doi.org/10.3390/molecules26206231
dc.rights.none.fl_str_mv cc-by (c) Fort i Baixeras, Joana et al., 2021
https://creativecommons.org/licenses/by/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by (c) Fort i Baixeras, Joana et al., 2021
https://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv Articles publicats en revistes (Bioquímica i Biomedicina Molecular)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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