The shape of the transmembrane domain is a novel endocytosis signal for single-spanning membrane proteins

Autores
González Montoro, María Ayelén; Bigliani, Gonzalo Yamil; Valdez, Javier Esteban
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Endocytosis is crucial for all cells as it allows them to incorporate material from the extracellular space and control the availability of transmembrane proteins at the plasma membrane. In yeast, endocytosis followed by recycling to the plasma membrane results in a polarised distribution of membrane proteins by a kinetic mechanism. Here, we report that increasing the volume of residues that constitute the exoplasmic half of the transmembrane domain (TMD) in the yeast SNARE Sso1, a type II membrane protein, results in its polarised distribution at the plasma membrane. Expression of this chimera in strains affected in either endocytosis or recycling revealed that this polarisation is achieved by endocytic cycling. A bioinformatics search of the Saccharomyces cerevisiae proteome identified several proteins with high-volume exoplasmic hemi-TMDs. Our experiments indicate that TMDs from these proteins can confer a polarised distribution to the Sso1 cytoplasmic domain, indicating that the shape of the TMD can act as a novel endocytosis and polarity signal in yeast. Additionally, a high-volume exoplasmic hemi-TMD can act as an endocytosis signal in a mammalian cell line.
Fil: González Montoro, María Ayelén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Bigliani, Gonzalo Yamil. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Valdez, Javier Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Materia
ENDOCYTOSIS
POLARITY
SNARES
TRANSMEMBRANE DOMAIN
YEAST
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:11336/64299
Acceder
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network_name_str CONICET Digital (CONICET)
spelling The shape of the transmembrane domain is a novel endocytosis signal for single-spanning membrane proteinsGonzález Montoro, María AyelénBigliani, Gonzalo YamilValdez, Javier EstebanENDOCYTOSISPOLARITYSNARESTRANSMEMBRANE DOMAINYEASThttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Endocytosis is crucial for all cells as it allows them to incorporate material from the extracellular space and control the availability of transmembrane proteins at the plasma membrane. In yeast, endocytosis followed by recycling to the plasma membrane results in a polarised distribution of membrane proteins by a kinetic mechanism. Here, we report that increasing the volume of residues that constitute the exoplasmic half of the transmembrane domain (TMD) in the yeast SNARE Sso1, a type II membrane protein, results in its polarised distribution at the plasma membrane. Expression of this chimera in strains affected in either endocytosis or recycling revealed that this polarisation is achieved by endocytic cycling. A bioinformatics search of the Saccharomyces cerevisiae proteome identified several proteins with high-volume exoplasmic hemi-TMDs. Our experiments indicate that TMDs from these proteins can confer a polarised distribution to the Sso1 cytoplasmic domain, indicating that the shape of the TMD can act as a novel endocytosis and polarity signal in yeast. Additionally, a high-volume exoplasmic hemi-TMD can act as an endocytosis signal in a mammalian cell line.Fil: González Montoro, María Ayelén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Bigliani, Gonzalo Yamil. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Valdez, Javier Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaCompany of Biologists2017-11-15info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/64299González Montoro, María Ayelén; Bigliani, Gonzalo Yamil; Valdez, Javier Esteban; The shape of the transmembrane domain is a novel endocytosis signal for single-spanning membrane proteins; Company of Biologists; Journal of Cell Science; 130; 22; 15-11-2017; 3829-38380021-9533CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1242/jcs.202937info:eu-repo/semantics/altIdentifier/url/http://jcs.biologists.org/content/130/22/3829info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:42:08Zoai:ri.conicet.gov.ar:11336/64299instacron: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:34982025-09-29 09:42:08.971CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The shape of the transmembrane domain is a novel endocytosis signal for single-spanning membrane proteins
title The shape of the transmembrane domain is a novel endocytosis signal for single-spanning membrane proteins
spellingShingle The shape of the transmembrane domain is a novel endocytosis signal for single-spanning membrane proteins
González Montoro, María Ayelén
ENDOCYTOSIS
POLARITY
SNARES
TRANSMEMBRANE DOMAIN
YEAST
title_short The shape of the transmembrane domain is a novel endocytosis signal for single-spanning membrane proteins
title_full The shape of the transmembrane domain is a novel endocytosis signal for single-spanning membrane proteins
title_fullStr The shape of the transmembrane domain is a novel endocytosis signal for single-spanning membrane proteins
title_full_unstemmed The shape of the transmembrane domain is a novel endocytosis signal for single-spanning membrane proteins
title_sort The shape of the transmembrane domain is a novel endocytosis signal for single-spanning membrane proteins
dc.creator.none.fl_str_mv González Montoro, María Ayelén
Bigliani, Gonzalo Yamil
Valdez, Javier Esteban
author González Montoro, María Ayelén
author_facet González Montoro, María Ayelén
Bigliani, Gonzalo Yamil
Valdez, Javier Esteban
author_role author
author2 Bigliani, Gonzalo Yamil
Valdez, Javier Esteban
author2_role author
author
dc.subject.none.fl_str_mv ENDOCYTOSIS
POLARITY
SNARES
TRANSMEMBRANE DOMAIN
YEAST
topic ENDOCYTOSIS
POLARITY
SNARES
TRANSMEMBRANE DOMAIN
YEAST
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Endocytosis is crucial for all cells as it allows them to incorporate material from the extracellular space and control the availability of transmembrane proteins at the plasma membrane. In yeast, endocytosis followed by recycling to the plasma membrane results in a polarised distribution of membrane proteins by a kinetic mechanism. Here, we report that increasing the volume of residues that constitute the exoplasmic half of the transmembrane domain (TMD) in the yeast SNARE Sso1, a type II membrane protein, results in its polarised distribution at the plasma membrane. Expression of this chimera in strains affected in either endocytosis or recycling revealed that this polarisation is achieved by endocytic cycling. A bioinformatics search of the Saccharomyces cerevisiae proteome identified several proteins with high-volume exoplasmic hemi-TMDs. Our experiments indicate that TMDs from these proteins can confer a polarised distribution to the Sso1 cytoplasmic domain, indicating that the shape of the TMD can act as a novel endocytosis and polarity signal in yeast. Additionally, a high-volume exoplasmic hemi-TMD can act as an endocytosis signal in a mammalian cell line.
Fil: González Montoro, María Ayelén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Bigliani, Gonzalo Yamil. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Valdez, Javier Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
description Endocytosis is crucial for all cells as it allows them to incorporate material from the extracellular space and control the availability of transmembrane proteins at the plasma membrane. In yeast, endocytosis followed by recycling to the plasma membrane results in a polarised distribution of membrane proteins by a kinetic mechanism. Here, we report that increasing the volume of residues that constitute the exoplasmic half of the transmembrane domain (TMD) in the yeast SNARE Sso1, a type II membrane protein, results in its polarised distribution at the plasma membrane. Expression of this chimera in strains affected in either endocytosis or recycling revealed that this polarisation is achieved by endocytic cycling. A bioinformatics search of the Saccharomyces cerevisiae proteome identified several proteins with high-volume exoplasmic hemi-TMDs. Our experiments indicate that TMDs from these proteins can confer a polarised distribution to the Sso1 cytoplasmic domain, indicating that the shape of the TMD can act as a novel endocytosis and polarity signal in yeast. Additionally, a high-volume exoplasmic hemi-TMD can act as an endocytosis signal in a mammalian cell line.
publishDate 2017
dc.date.none.fl_str_mv 2017-11-15
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/11336/64299
González Montoro, María Ayelén; Bigliani, Gonzalo Yamil; Valdez, Javier Esteban; The shape of the transmembrane domain is a novel endocytosis signal for single-spanning membrane proteins; Company of Biologists; Journal of Cell Science; 130; 22; 15-11-2017; 3829-3838
0021-9533
CONICET Digital
CONICET
url http://hdl.handle.net/11336/64299
identifier_str_mv González Montoro, María Ayelén; Bigliani, Gonzalo Yamil; Valdez, Javier Esteban; The shape of the transmembrane domain is a novel endocytosis signal for single-spanning membrane proteins; Company of Biologists; Journal of Cell Science; 130; 22; 15-11-2017; 3829-3838
0021-9533
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1242/jcs.202937
info:eu-repo/semantics/altIdentifier/url/http://jcs.biologists.org/content/130/22/3829
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 Company of Biologists
publisher.none.fl_str_mv Company of Biologists
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
_version_ 1844613328388751360
score 13.070432

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