Interaction between the Linker, Pre-S1, and TRP Domains Determines Folding, Assembly, and Trafficking of TRPV Channels

Vista sencilla de ítem
dc.contributor.authorGarcia-Elias, Anna
dc.contributor.authorBerna-Erro, Alejandro
dc.contributor.authorRubio-Moscardo, Fanny
dc.contributor.authorPardo-Pastor, Carlos
dc.contributor.authorMrkonjić, Sanela
dc.contributor.authorSepúlveda, Romina V.
dc.contributor.authorVicente, Rubén
dc.contributor.authorGonzález-Nilo, Fernando
dc.contributor.authorValverde, Miguel A.
dc.date.accessioned2023-03-24T14:14:23Z
dc.date.available2023-03-24T14:14:23Z
dc.date.issued2015-08
dc.descriptionIndexación: Scopuses
dc.description.abstractSummary Functional transient receptor potential (TRP) channels result from the assembly of four subunits. Here, we show an interaction between the pre-S1, TRP, and the ankyrin repeat domain (ARD)-S1 linker domains of TRPV1 and TRPV4 that is essential for proper channel assembly. Neutralization of TRPV4 pre-S1 K462 resulted in protein retention in the ER, defective glycosylation and trafficking, and unresponsiveness to TRPV4-activating stimuli. Similar results were obtained with the equivalent mutation in TRPV1 pre-S1. Molecular dynamics simulations revealed that TRPV4-K462 generated an alternating hydrogen network with E745 (TRP box) and D425 (pre-S1 linker), and that K462Q mutation affected subunit folding. Consistently, single TRPV4-E745A or TRPV4-D425A mutations moderately affected TRPV4 biogenesis while double TRPV4-D425A/E745A mutation resumed the TRPV4-K462Q phenotype. Thus, the interaction between pre-S1, TRP, and linker domains is mandatory to generate a structural conformation that allows the contacts between adjacent subunits to promote correct assembly and trafficking to the plasma membrane. © 2015 Elsevier Ltd.es
dc.description.urihttps://www-sciencedirect-com.recursosbiblioteca.unab.cl/science/article/pii/S096921261500221X?via%3Dihub
dc.identifier.citationStructure Volume 23, Issue 8, Pages 1404 - 14137 August 2015 Article number 3202es
dc.identifier.doi10.1016/j.str.2015.05.018
dc.identifier.issn0969-2126
dc.identifier.urihttps://repositorio.unab.cl/xmlui/handle/ria/47852
dc.language.isoenes
dc.publisherCell Presses
dc.rights.licenseAtribución 4.0 Internacional (CC BY 4.0)
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/deed.es
dc.subjectTransient Receptor Potential Channelses
dc.subjectAnimalses
dc.subjectRN 1734es
dc.titleInteraction between the Linker, Pre-S1, and TRP Domains Determines Folding, Assembly, and Trafficking of TRPV Channelses
dc.typeArtículoes
Archivos
Bloque original
Mostrando 1 - 1 de 1
Miniatura
Nombre:
1-s2.0-S096921261500221X-main.pdf
Tamaño:
2.61 MB
Formato:
Adobe Portable Document Format
Descripción:
TEXTO EN INGLES
Descargar
Bloque de licencias
Mostrando 1 - 1 de 1
No hay miniatura disponible
Nombre:
license.txt
Tamaño:
1.71 KB
Formato:
Item-specific license agreed upon to submission
Descripción:
Descargar
Colecciones
Fac.CV - Artículos de Revista