PIP aquaporin pH-sensing is regulated by the length and charge of the C-terminal region

Autores
Scochera, Florencia Paola; Zerbetto de Palma, Gerardo Gabriel; Canessa Fortuna, Agustina; Chevriau, Jonathan; Toriano, Roxana Mabel; Soto, Gabriela Cynthia; Zeida, Ari; Alleva, Karina Edith
Año de publicación
2022
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Plant PIP aquaporins play a central role in controlling plant water status. The current structural model for PIP pH-gating states that the main pH sensor is located in loopD and that all the mobile cytosolic elements participate in a complex interaction network that ensures the closed structure. However, the precise participation of the last part of the C-terminal domain (CT) in PIP pH gating remains unknown. This last part has not been resolved in PIP crystal structures and is a key difference between PIP1 and PIP2 paralogues. Here, by a combined experimental and computational approach, we provide data about the role of CT in pH gating of Beta vulgaris PIP. We demonstrate that the length of CT and the positive charge located among its last residues modulate the pH at which the open/closed transition occurs. We also postulate a molecular-based mechanism for the differential pH sensing in PIP homo- or heterotetramers by performing atomistic molecular dynamics simulations (MDS) on complete models of PIP tetramers. Our findings show that the last part of CT can affect the environment of loopD pH sensors in the closed state. Results presented herein contribute to the understanding of how the characteristics of CT in PIP channels play a crucial role in determining the pH at which water transport through these channels is blocked, highlighting the relevance of the differentially conserved very last residues in PIP1 and PIP2 paralogues.
Fil: Scochera, Florencia Paola. Universidad Nacional de la Plata. Facultad de Ingeniería. Departamento de Fisicomatemática; Argentina
Fil: Zerbetto de Palma, Gerardo Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Canessa Fortuna, Agustina. Universidad de Buenos Aires; Argentina
Fil: Chevriau, Jonathan. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Toriano, Roxana Mabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Fisiología y Biofísica Bernardo Houssay. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Fisiología y Biofísica Bernardo Houssay; Argentina
Fil: Soto, Gabriela Cynthia. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Agrobiotecnología y Biología Molecular. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Agrobiotecnología y Biología Molecular; Argentina
Fil: Zeida, Ari. Universidad de la República; Uruguay
Fil: Alleva, Karina Edith. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Materia
C TERMINUS
HETEROTETRAMER
pH SENSING
WATER CHANNELS
HETEROTETRAMER
pH SENSING
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:11336/203560
Acceder
id CONICETDig_c0f08895ef03d4e36a247b703c1da619
oai_identifier_str oai:ri.conicet.gov.ar:11336/203560
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling PIP aquaporin pH-sensing is regulated by the length and charge of the C-terminal regionScochera, Florencia PaolaZerbetto de Palma, Gerardo GabrielCanessa Fortuna, AgustinaChevriau, JonathanToriano, Roxana MabelSoto, Gabriela CynthiaZeida, AriAlleva, Karina EdithC TERMINUSHETEROTETRAMERpH SENSINGWATER CHANNELSHETEROTETRAMERpH SENSINGhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Plant PIP aquaporins play a central role in controlling plant water status. The current structural model for PIP pH-gating states that the main pH sensor is located in loopD and that all the mobile cytosolic elements participate in a complex interaction network that ensures the closed structure. However, the precise participation of the last part of the C-terminal domain (CT) in PIP pH gating remains unknown. This last part has not been resolved in PIP crystal structures and is a key difference between PIP1 and PIP2 paralogues. Here, by a combined experimental and computational approach, we provide data about the role of CT in pH gating of Beta vulgaris PIP. We demonstrate that the length of CT and the positive charge located among its last residues modulate the pH at which the open/closed transition occurs. We also postulate a molecular-based mechanism for the differential pH sensing in PIP homo- or heterotetramers by performing atomistic molecular dynamics simulations (MDS) on complete models of PIP tetramers. Our findings show that the last part of CT can affect the environment of loopD pH sensors in the closed state. Results presented herein contribute to the understanding of how the characteristics of CT in PIP channels play a crucial role in determining the pH at which water transport through these channels is blocked, highlighting the relevance of the differentially conserved very last residues in PIP1 and PIP2 paralogues.Fil: Scochera, Florencia Paola. Universidad Nacional de la Plata. Facultad de Ingeniería. Departamento de Fisicomatemática; ArgentinaFil: Zerbetto de Palma, Gerardo Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaFil: Canessa Fortuna, Agustina. Universidad de Buenos Aires; ArgentinaFil: Chevriau, Jonathan. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaFil: Toriano, Roxana Mabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Fisiología y Biofísica Bernardo Houssay. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Fisiología y Biofísica Bernardo Houssay; ArgentinaFil: Soto, Gabriela Cynthia. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Agrobiotecnología y Biología Molecular. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Agrobiotecnología y Biología Molecular; ArgentinaFil: Zeida, Ari. Universidad de la República; UruguayFil: Alleva, Karina Edith. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaWiley Blackwell Publishing, Inc2022-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/203560Scochera, Florencia Paola; Zerbetto de Palma, Gerardo Gabriel; Canessa Fortuna, Agustina; Chevriau, Jonathan; Toriano, Roxana Mabel; et al.; PIP aquaporin pH-sensing is regulated by the length and charge of the C-terminal region; Wiley Blackwell Publishing, Inc; Febs Journal; 289; 1; 1-2022; 246-2611742-464XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1111/febs.16134info:eu-repo/semantics/altIdentifier/url/https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.16134info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:07:54Zoai:ri.conicet.gov.ar:11336/203560instacron: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:34982025-10-22 12:07:55.185CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv PIP aquaporin pH-sensing is regulated by the length and charge of the C-terminal region
title PIP aquaporin pH-sensing is regulated by the length and charge of the C-terminal region
spellingShingle PIP aquaporin pH-sensing is regulated by the length and charge of the C-terminal region
Scochera, Florencia Paola
C TERMINUS
HETEROTETRAMER
pH SENSING
WATER CHANNELS
HETEROTETRAMER
pH SENSING
title_short PIP aquaporin pH-sensing is regulated by the length and charge of the C-terminal region
title_full PIP aquaporin pH-sensing is regulated by the length and charge of the C-terminal region
title_fullStr PIP aquaporin pH-sensing is regulated by the length and charge of the C-terminal region
title_full_unstemmed PIP aquaporin pH-sensing is regulated by the length and charge of the C-terminal region
title_sort PIP aquaporin pH-sensing is regulated by the length and charge of the C-terminal region
dc.creator.none.fl_str_mv Scochera, Florencia Paola
Zerbetto de Palma, Gerardo Gabriel
Canessa Fortuna, Agustina
Chevriau, Jonathan
Toriano, Roxana Mabel
Soto, Gabriela Cynthia
Zeida, Ari
Alleva, Karina Edith
author Scochera, Florencia Paola
author_facet Scochera, Florencia Paola
Zerbetto de Palma, Gerardo Gabriel
Canessa Fortuna, Agustina
Chevriau, Jonathan
Toriano, Roxana Mabel
Soto, Gabriela Cynthia
Zeida, Ari
Alleva, Karina Edith
author_role author
author2 Zerbetto de Palma, Gerardo Gabriel
Canessa Fortuna, Agustina
Chevriau, Jonathan
Toriano, Roxana Mabel
Soto, Gabriela Cynthia
Zeida, Ari
Alleva, Karina Edith
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv C TERMINUS
HETEROTETRAMER
pH SENSING
WATER CHANNELS
HETEROTETRAMER
pH SENSING
topic C TERMINUS
HETEROTETRAMER
pH SENSING
WATER CHANNELS
HETEROTETRAMER
pH SENSING
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Plant PIP aquaporins play a central role in controlling plant water status. The current structural model for PIP pH-gating states that the main pH sensor is located in loopD and that all the mobile cytosolic elements participate in a complex interaction network that ensures the closed structure. However, the precise participation of the last part of the C-terminal domain (CT) in PIP pH gating remains unknown. This last part has not been resolved in PIP crystal structures and is a key difference between PIP1 and PIP2 paralogues. Here, by a combined experimental and computational approach, we provide data about the role of CT in pH gating of Beta vulgaris PIP. We demonstrate that the length of CT and the positive charge located among its last residues modulate the pH at which the open/closed transition occurs. We also postulate a molecular-based mechanism for the differential pH sensing in PIP homo- or heterotetramers by performing atomistic molecular dynamics simulations (MDS) on complete models of PIP tetramers. Our findings show that the last part of CT can affect the environment of loopD pH sensors in the closed state. Results presented herein contribute to the understanding of how the characteristics of CT in PIP channels play a crucial role in determining the pH at which water transport through these channels is blocked, highlighting the relevance of the differentially conserved very last residues in PIP1 and PIP2 paralogues.
Fil: Scochera, Florencia Paola. Universidad Nacional de la Plata. Facultad de Ingeniería. Departamento de Fisicomatemática; Argentina
Fil: Zerbetto de Palma, Gerardo Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Canessa Fortuna, Agustina. Universidad de Buenos Aires; Argentina
Fil: Chevriau, Jonathan. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Toriano, Roxana Mabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Fisiología y Biofísica Bernardo Houssay. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Fisiología y Biofísica Bernardo Houssay; Argentina
Fil: Soto, Gabriela Cynthia. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Agrobiotecnología y Biología Molecular. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Agrobiotecnología y Biología Molecular; Argentina
Fil: Zeida, Ari. Universidad de la República; Uruguay
Fil: Alleva, Karina Edith. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
description Plant PIP aquaporins play a central role in controlling plant water status. The current structural model for PIP pH-gating states that the main pH sensor is located in loopD and that all the mobile cytosolic elements participate in a complex interaction network that ensures the closed structure. However, the precise participation of the last part of the C-terminal domain (CT) in PIP pH gating remains unknown. This last part has not been resolved in PIP crystal structures and is a key difference between PIP1 and PIP2 paralogues. Here, by a combined experimental and computational approach, we provide data about the role of CT in pH gating of Beta vulgaris PIP. We demonstrate that the length of CT and the positive charge located among its last residues modulate the pH at which the open/closed transition occurs. We also postulate a molecular-based mechanism for the differential pH sensing in PIP homo- or heterotetramers by performing atomistic molecular dynamics simulations (MDS) on complete models of PIP tetramers. Our findings show that the last part of CT can affect the environment of loopD pH sensors in the closed state. Results presented herein contribute to the understanding of how the characteristics of CT in PIP channels play a crucial role in determining the pH at which water transport through these channels is blocked, highlighting the relevance of the differentially conserved very last residues in PIP1 and PIP2 paralogues.
publishDate 2022
dc.date.none.fl_str_mv 2022-01
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/11336/203560
Scochera, Florencia Paola; Zerbetto de Palma, Gerardo Gabriel; Canessa Fortuna, Agustina; Chevriau, Jonathan; Toriano, Roxana Mabel; et al.; PIP aquaporin pH-sensing is regulated by the length and charge of the C-terminal region; Wiley Blackwell Publishing, Inc; Febs Journal; 289; 1; 1-2022; 246-261
1742-464X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/203560
identifier_str_mv Scochera, Florencia Paola; Zerbetto de Palma, Gerardo Gabriel; Canessa Fortuna, Agustina; Chevriau, Jonathan; Toriano, Roxana Mabel; et al.; PIP aquaporin pH-sensing is regulated by the length and charge of the C-terminal region; Wiley Blackwell Publishing, Inc; Febs Journal; 289; 1; 1-2022; 246-261
1742-464X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1111/febs.16134
info:eu-repo/semantics/altIdentifier/url/https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.16134
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
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
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_ 1846782446877540352
score 12.982451

Publicaciones similares