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TXNIP/TBP-2: A Master Regulator for Glucose Homeostasis

Identification of thioredoxin binding protein-2 (TBP-2), which is currently known as thioredoxin interacting protein (TXNIP), as an important binding partner for thioredoxin (TRX) revealed that an evolutionarily conserved reduction-oxidation (redox) signal complex plays an important role for pathoph...

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Autor principal: Yoshihara, Eiji
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7464905/
https://www.ncbi.nlm.nih.gov/pubmed/32824669
http://dx.doi.org/10.3390/antiox9080765
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author Yoshihara, Eiji
author_facet Yoshihara, Eiji
author_sort Yoshihara, Eiji
collection PubMed
description Identification of thioredoxin binding protein-2 (TBP-2), which is currently known as thioredoxin interacting protein (TXNIP), as an important binding partner for thioredoxin (TRX) revealed that an evolutionarily conserved reduction-oxidation (redox) signal complex plays an important role for pathophysiology. Due to the reducing activity of TRX, the TRX/TXNIP signal complex has been shown to be an important regulator for redox-related signal transduction in many types of cells in various species. In addition to its role in redox-dependent regulation, TXNIP has cellular functions that are performed in a redox-independent manner, which largely rely on their scaffolding function as an ancestral α-Arrestin family. Both the redox-dependent and -independent TXNIP functions serve as regulatory pathways in glucose metabolism. This review highlights the key advances in understanding TXNIP function as a master regulator for whole-body glucose homeostasis. The potential for therapeutic advantages of targeting TXNIP in diabetes and the future direction of the study are also discussed.
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spelling pubmed-74649052020-09-04 TXNIP/TBP-2: A Master Regulator for Glucose Homeostasis Yoshihara, Eiji Antioxidants (Basel) Review Identification of thioredoxin binding protein-2 (TBP-2), which is currently known as thioredoxin interacting protein (TXNIP), as an important binding partner for thioredoxin (TRX) revealed that an evolutionarily conserved reduction-oxidation (redox) signal complex plays an important role for pathophysiology. Due to the reducing activity of TRX, the TRX/TXNIP signal complex has been shown to be an important regulator for redox-related signal transduction in many types of cells in various species. In addition to its role in redox-dependent regulation, TXNIP has cellular functions that are performed in a redox-independent manner, which largely rely on their scaffolding function as an ancestral α-Arrestin family. Both the redox-dependent and -independent TXNIP functions serve as regulatory pathways in glucose metabolism. This review highlights the key advances in understanding TXNIP function as a master regulator for whole-body glucose homeostasis. The potential for therapeutic advantages of targeting TXNIP in diabetes and the future direction of the study are also discussed. MDPI 2020-08-18 /pmc/articles/PMC7464905/ /pubmed/32824669 http://dx.doi.org/10.3390/antiox9080765 Text en © 2020 by the author. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Yoshihara, Eiji
TXNIP/TBP-2: A Master Regulator for Glucose Homeostasis
title TXNIP/TBP-2: A Master Regulator for Glucose Homeostasis
title_full TXNIP/TBP-2: A Master Regulator for Glucose Homeostasis
title_fullStr TXNIP/TBP-2: A Master Regulator for Glucose Homeostasis
title_full_unstemmed TXNIP/TBP-2: A Master Regulator for Glucose Homeostasis
title_short TXNIP/TBP-2: A Master Regulator for Glucose Homeostasis
title_sort txnip/tbp-2: a master regulator for glucose homeostasis
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7464905/
https://www.ncbi.nlm.nih.gov/pubmed/32824669
http://dx.doi.org/10.3390/antiox9080765
work_keys_str_mv AT yoshiharaeiji txniptbp2amasterregulatorforglucosehomeostasis