Curvature sensing amphipathic helix in the C-terminus of RTNLB13 is conserved in all endoplasmic reticulum shaping reticulons in Arabidopsis thaliana

Abstract The reticulon family of integral membrane proteins are conserved across all eukaryotes and typically localize to the endoplasmic reticulum (ER), where they are involved in generating highly-curved tubules. We recently demonstrated that Reticulon-like protein B13 (RTNLB13) from Arabidopsis t...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Rhiannon L. Brooks, Chandni S. Mistry, Ann M. Dixon
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/afcfddedfe5e4b1d92fd994784aab3c2
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:afcfddedfe5e4b1d92fd994784aab3c2
record_format	dspace
spelling	oai:doaj.org-article:afcfddedfe5e4b1d92fd994784aab3c22021-12-02T17:05:11ZCurvature sensing amphipathic helix in the C-terminus of RTNLB13 is conserved in all endoplasmic reticulum shaping reticulons in Arabidopsis thaliana10.1038/s41598-021-85866-32045-2322https://doaj.org/article/afcfddedfe5e4b1d92fd994784aab3c22021-03-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-85866-3https://doaj.org/toc/2045-2322Abstract The reticulon family of integral membrane proteins are conserved across all eukaryotes and typically localize to the endoplasmic reticulum (ER), where they are involved in generating highly-curved tubules. We recently demonstrated that Reticulon-like protein B13 (RTNLB13) from Arabidopsis thaliana contains a curvature-responsive amphipathic helix (APH) important for the proteins’ ability to induce curvature in the ER membrane, but incapable of generating curvature by itself. We suggested it acts as a feedback element, only folding/binding once a sufficient degree of curvature has been achieved, and stabilizes curvature without disrupting the bilayer. However, it remains unclear whether this is unique to RTNLB13 or is conserved across all reticulons—to date, experimental evidence has only been reported for two reticulons. Here we used biophysical methods to characterize a minimal library of putative APH peptides from across the 21 A. thaliana isoforms. We found that reticulons with the closest evolutionary relationship to RTNLB13 contain curvature-sensing APHs in the same location with sequence conservation. Our data reveal that a more distantly-related branch of reticulons developed a ~ 20-residue linker between the transmembrane domain and APH. This may facilitate functional flexibility as previous studies have linked these isoforms not only to ER remodeling but other cellular activities.Rhiannon L. BrooksChandni S. MistryAnn M. DixonNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Rhiannon L. Brooks Chandni S. Mistry Ann M. Dixon Curvature sensing amphipathic helix in the C-terminus of RTNLB13 is conserved in all endoplasmic reticulum shaping reticulons in Arabidopsis thaliana
description	Abstract The reticulon family of integral membrane proteins are conserved across all eukaryotes and typically localize to the endoplasmic reticulum (ER), where they are involved in generating highly-curved tubules. We recently demonstrated that Reticulon-like protein B13 (RTNLB13) from Arabidopsis thaliana contains a curvature-responsive amphipathic helix (APH) important for the proteins’ ability to induce curvature in the ER membrane, but incapable of generating curvature by itself. We suggested it acts as a feedback element, only folding/binding once a sufficient degree of curvature has been achieved, and stabilizes curvature without disrupting the bilayer. However, it remains unclear whether this is unique to RTNLB13 or is conserved across all reticulons—to date, experimental evidence has only been reported for two reticulons. Here we used biophysical methods to characterize a minimal library of putative APH peptides from across the 21 A. thaliana isoforms. We found that reticulons with the closest evolutionary relationship to RTNLB13 contain curvature-sensing APHs in the same location with sequence conservation. Our data reveal that a more distantly-related branch of reticulons developed a ~ 20-residue linker between the transmembrane domain and APH. This may facilitate functional flexibility as previous studies have linked these isoforms not only to ER remodeling but other cellular activities.
format	article
author	Rhiannon L. Brooks Chandni S. Mistry Ann M. Dixon
author_facet	Rhiannon L. Brooks Chandni S. Mistry Ann M. Dixon
author_sort	Rhiannon L. Brooks
title	Curvature sensing amphipathic helix in the C-terminus of RTNLB13 is conserved in all endoplasmic reticulum shaping reticulons in Arabidopsis thaliana
title_short	Curvature sensing amphipathic helix in the C-terminus of RTNLB13 is conserved in all endoplasmic reticulum shaping reticulons in Arabidopsis thaliana
title_full	Curvature sensing amphipathic helix in the C-terminus of RTNLB13 is conserved in all endoplasmic reticulum shaping reticulons in Arabidopsis thaliana
title_fullStr	Curvature sensing amphipathic helix in the C-terminus of RTNLB13 is conserved in all endoplasmic reticulum shaping reticulons in Arabidopsis thaliana
title_full_unstemmed	Curvature sensing amphipathic helix in the C-terminus of RTNLB13 is conserved in all endoplasmic reticulum shaping reticulons in Arabidopsis thaliana
title_sort	curvature sensing amphipathic helix in the c-terminus of rtnlb13 is conserved in all endoplasmic reticulum shaping reticulons in arabidopsis thaliana
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/afcfddedfe5e4b1d92fd994784aab3c2
work_keys_str_mv	AT rhiannonlbrooks curvaturesensingamphipathichelixinthecterminusofrtnlb13isconservedinallendoplasmicreticulumshapingreticulonsinarabidopsisthaliana AT chandnismistry curvaturesensingamphipathichelixinthecterminusofrtnlb13isconservedinallendoplasmicreticulumshapingreticulonsinarabidopsisthaliana AT annmdixon curvaturesensingamphipathichelixinthecterminusofrtnlb13isconservedinallendoplasmicreticulumshapingreticulonsinarabidopsisthaliana
_version_	1718381808558538752

Curvature sensing amphipathic helix in the C-terminus of RTNLB13 is conserved in all endoplasmic reticulum shaping reticulons in Arabidopsis thaliana

Ejemplares similares