Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding

P5 is one of protein disulfide isomerase family proteins (PDIs) involved in endoplasmic reticulum (ER) protein quality control that assists oxidative folding, inhibits protein aggregation, and regulates the unfolded protein response. P5 reportedly interacts with other PDIs via intermolecular disulfi...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Motonori Matsusaki, Rina Okada, Yuya Tanikawa, Shingo Kanemura, Dai Ito, Yuxi Lin, Mai Watabe, Hiroshi Yamaguchi, Tomohide Saio, Young-Ho Lee, Kenji Inaba, Masaki Okumura
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	protein disulfide isomerase family disulfide bond endoplasmic reticulum oxidative folding molecular chaperone protein-protein interaction Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/45ecc0f3a89d47ea96fcc3025c60da76
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:45ecc0f3a89d47ea96fcc3025c60da76
record_format	dspace
spelling	oai:doaj.org-article:45ecc0f3a89d47ea96fcc3025c60da762021-11-25T16:47:06ZFunctional Interplay between P5 and PDI/ERp72 to Drive Protein Folding10.3390/biology101111122079-7737https://doaj.org/article/45ecc0f3a89d47ea96fcc3025c60da762021-10-01T00:00:00Zhttps://www.mdpi.com/2079-7737/10/11/1112https://doaj.org/toc/2079-7737P5 is one of protein disulfide isomerase family proteins (PDIs) involved in endoplasmic reticulum (ER) protein quality control that assists oxidative folding, inhibits protein aggregation, and regulates the unfolded protein response. P5 reportedly interacts with other PDIs via intermolecular disulfide bonds in cultured cells, but it remains unclear whether complex formation between P5 and other PDIs is involved in regulating enzymatic and chaperone functions. Herein, we established the far-western blot method to detect non-covalent interactions between P5 and other PDIs and found that PDI and ERp72 are partner proteins of P5. The enzymatic activity of P5-mediated oxidative folding is up-regulated by PDI, while the chaperone activity of P5 is stimulated by ERp72. These findings shed light on the mechanism by which the complex formations among PDIs drive to synergistically accelerate protein folding and prevents aggregation. This knowledge has implications for understanding misfolding-related pathology.Motonori MatsusakiRina OkadaYuya TanikawaShingo KanemuraDai ItoYuxi LinMai WatabeHiroshi YamaguchiTomohide SaioYoung-Ho LeeKenji InabaMasaki OkumuraMDPI AGarticleprotein disulfide isomerase familydisulfide bondendoplasmic reticulumoxidative foldingmolecular chaperoneprotein-protein interactionBiology (General)QH301-705.5ENBiology, Vol 10, Iss 1112, p 1112 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	protein disulfide isomerase family disulfide bond endoplasmic reticulum oxidative folding molecular chaperone protein-protein interaction Biology (General) QH301-705.5
spellingShingle	protein disulfide isomerase family disulfide bond endoplasmic reticulum oxidative folding molecular chaperone protein-protein interaction Biology (General) QH301-705.5 Motonori Matsusaki Rina Okada Yuya Tanikawa Shingo Kanemura Dai Ito Yuxi Lin Mai Watabe Hiroshi Yamaguchi Tomohide Saio Young-Ho Lee Kenji Inaba Masaki Okumura Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding
description	P5 is one of protein disulfide isomerase family proteins (PDIs) involved in endoplasmic reticulum (ER) protein quality control that assists oxidative folding, inhibits protein aggregation, and regulates the unfolded protein response. P5 reportedly interacts with other PDIs via intermolecular disulfide bonds in cultured cells, but it remains unclear whether complex formation between P5 and other PDIs is involved in regulating enzymatic and chaperone functions. Herein, we established the far-western blot method to detect non-covalent interactions between P5 and other PDIs and found that PDI and ERp72 are partner proteins of P5. The enzymatic activity of P5-mediated oxidative folding is up-regulated by PDI, while the chaperone activity of P5 is stimulated by ERp72. These findings shed light on the mechanism by which the complex formations among PDIs drive to synergistically accelerate protein folding and prevents aggregation. This knowledge has implications for understanding misfolding-related pathology.
format	article
author	Motonori Matsusaki Rina Okada Yuya Tanikawa Shingo Kanemura Dai Ito Yuxi Lin Mai Watabe Hiroshi Yamaguchi Tomohide Saio Young-Ho Lee Kenji Inaba Masaki Okumura
author_facet	Motonori Matsusaki Rina Okada Yuya Tanikawa Shingo Kanemura Dai Ito Yuxi Lin Mai Watabe Hiroshi Yamaguchi Tomohide Saio Young-Ho Lee Kenji Inaba Masaki Okumura
author_sort	Motonori Matsusaki
title	Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding
title_short	Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding
title_full	Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding
title_fullStr	Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding
title_full_unstemmed	Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding
title_sort	functional interplay between p5 and pdi/erp72 to drive protein folding
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/45ecc0f3a89d47ea96fcc3025c60da76
work_keys_str_mv	AT motonorimatsusaki functionalinterplaybetweenp5andpdierp72todriveproteinfolding AT rinaokada functionalinterplaybetweenp5andpdierp72todriveproteinfolding AT yuyatanikawa functionalinterplaybetweenp5andpdierp72todriveproteinfolding AT shingokanemura functionalinterplaybetweenp5andpdierp72todriveproteinfolding AT daiito functionalinterplaybetweenp5andpdierp72todriveproteinfolding AT yuxilin functionalinterplaybetweenp5andpdierp72todriveproteinfolding AT maiwatabe functionalinterplaybetweenp5andpdierp72todriveproteinfolding AT hiroshiyamaguchi functionalinterplaybetweenp5andpdierp72todriveproteinfolding AT tomohidesaio functionalinterplaybetweenp5andpdierp72todriveproteinfolding AT youngholee functionalinterplaybetweenp5andpdierp72todriveproteinfolding AT kenjiinaba functionalinterplaybetweenp5andpdierp72todriveproteinfolding AT masakiokumura functionalinterplaybetweenp5andpdierp72todriveproteinfolding
_version_	1718412950740402176

Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding

Ejemplares similares