The stress-responsive protein REDD1 and its pathophysiological functions
Abstract Regulated in development and DNA damage-response 1 (REDD1) is a stress-induced protein that controls various cellular functions, including metabolism, oxidative stress, autophagy, and cell fate, and contributes to the pathogenesis of metabolic and inflammatory disorders, neurodegeneration,...
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Publishing Group
2023-09-01
|
| Series: | Experimental and Molecular Medicine |
| Online Access: | https://doi.org/10.1038/s12276-023-01056-3 |
| _version_ | 1797663591928692736 |
|---|---|
| author | Ji-Yoon Kim Young-Guen Kwon Young-Myeong Kim |
| author_facet | Ji-Yoon Kim Young-Guen Kwon Young-Myeong Kim |
| author_sort | Ji-Yoon Kim |
| collection | DOAJ |
| description | Abstract Regulated in development and DNA damage-response 1 (REDD1) is a stress-induced protein that controls various cellular functions, including metabolism, oxidative stress, autophagy, and cell fate, and contributes to the pathogenesis of metabolic and inflammatory disorders, neurodegeneration, and cancer. REDD1 usually exerts deleterious effects, including tumorigenesis, metabolic inflammation, neurodegeneration, and muscle dystrophy; however, it also exhibits protective functions by regulating multiple intrinsic cell activities through either an mTORC1-dependent or -independent mechanism. REDD1 typically regulates mTORC1 signaling, NF-κB activation, and cellular pro-oxidant or antioxidant activity by interacting with 14-3-3 proteins, IκBα, and thioredoxin-interacting protein or 75 kDa glucose-regulated protein, respectively. The diverse functions of REDD1 depend on cell type, cellular context, interaction partners, and cellular localization (e.g., mitochondria, endomembrane, or cytosol). Therefore, comprehensively understanding the molecular mechanisms and biological roles of REDD1 under pathophysiological conditions is of utmost importance. In this review, based on the published literature, we highlight and discuss the molecular mechanisms underlying the REDD1 expression and its actions, biological functions, and pathophysiological roles. |
| first_indexed | 2024-03-11T19:16:53Z |
| format | Article |
| id | doaj.art-325426d181284c04b730fe8fd64ebfaf |
| institution | Directory Open Access Journal |
| issn | 2092-6413 |
| language | English |
| last_indexed | 2024-03-11T19:16:53Z |
| publishDate | 2023-09-01 |
| publisher | Nature Publishing Group |
| record_format | Article |
| series | Experimental and Molecular Medicine |
| spelling | doaj.art-325426d181284c04b730fe8fd64ebfaf2023-10-08T11:07:50ZengNature Publishing GroupExperimental and Molecular Medicine2092-64132023-09-015591933194410.1038/s12276-023-01056-3The stress-responsive protein REDD1 and its pathophysiological functionsJi-Yoon Kim0Young-Guen Kwon1Young-Myeong Kim2Department of Anesthesiology and Pain Medicine, Hanyang University HospitalDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei UniversityDepartment of Molecular and Cellular Biochemistry, School of Medicine, Kangwon National UniversityAbstract Regulated in development and DNA damage-response 1 (REDD1) is a stress-induced protein that controls various cellular functions, including metabolism, oxidative stress, autophagy, and cell fate, and contributes to the pathogenesis of metabolic and inflammatory disorders, neurodegeneration, and cancer. REDD1 usually exerts deleterious effects, including tumorigenesis, metabolic inflammation, neurodegeneration, and muscle dystrophy; however, it also exhibits protective functions by regulating multiple intrinsic cell activities through either an mTORC1-dependent or -independent mechanism. REDD1 typically regulates mTORC1 signaling, NF-κB activation, and cellular pro-oxidant or antioxidant activity by interacting with 14-3-3 proteins, IκBα, and thioredoxin-interacting protein or 75 kDa glucose-regulated protein, respectively. The diverse functions of REDD1 depend on cell type, cellular context, interaction partners, and cellular localization (e.g., mitochondria, endomembrane, or cytosol). Therefore, comprehensively understanding the molecular mechanisms and biological roles of REDD1 under pathophysiological conditions is of utmost importance. In this review, based on the published literature, we highlight and discuss the molecular mechanisms underlying the REDD1 expression and its actions, biological functions, and pathophysiological roles.https://doi.org/10.1038/s12276-023-01056-3 |
| spellingShingle | Ji-Yoon Kim Young-Guen Kwon Young-Myeong Kim The stress-responsive protein REDD1 and its pathophysiological functions Experimental and Molecular Medicine |
| title | The stress-responsive protein REDD1 and its pathophysiological functions |
| title_full | The stress-responsive protein REDD1 and its pathophysiological functions |
| title_fullStr | The stress-responsive protein REDD1 and its pathophysiological functions |
| title_full_unstemmed | The stress-responsive protein REDD1 and its pathophysiological functions |
| title_short | The stress-responsive protein REDD1 and its pathophysiological functions |
| title_sort | stress responsive protein redd1 and its pathophysiological functions |
| url | https://doi.org/10.1038/s12276-023-01056-3 |
| work_keys_str_mv | AT jiyoonkim thestressresponsiveproteinredd1anditspathophysiologicalfunctions AT youngguenkwon thestressresponsiveproteinredd1anditspathophysiologicalfunctions AT youngmyeongkim thestressresponsiveproteinredd1anditspathophysiologicalfunctions AT jiyoonkim stressresponsiveproteinredd1anditspathophysiologicalfunctions AT youngguenkwon stressresponsiveproteinredd1anditspathophysiologicalfunctions AT youngmyeongkim stressresponsiveproteinredd1anditspathophysiologicalfunctions |