Stress Granule-Mediated Oxidized RNA Decay in P-Body: Hypothetical Role of ADAR1, Tudor-SN, and STAU1
Reactive oxygen species (ROS) generated under oxidative stress (OS) cause oxidative damage to RNA. Recent studies have suggested a role for oxidized RNA in several human disorders. Under the conditions of oxidative stress, mRNAs released from polysome dissociation accumulate and initiate stress gran...
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Frontiers Media S.A.
2021-06-01
|
| Series: | Frontiers in Molecular Biosciences |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/articles/10.3389/fmolb.2021.672988/full |
| _version_ | 1818822346795909120 |
|---|---|
| author | Ravi Kumar Alluri Zhongwei Li Keith R. McCrae Keith R. McCrae |
| author_facet | Ravi Kumar Alluri Zhongwei Li Keith R. McCrae Keith R. McCrae |
| author_sort | Ravi Kumar Alluri |
| collection | DOAJ |
| description | Reactive oxygen species (ROS) generated under oxidative stress (OS) cause oxidative damage to RNA. Recent studies have suggested a role for oxidized RNA in several human disorders. Under the conditions of oxidative stress, mRNAs released from polysome dissociation accumulate and initiate stress granule (SG) assembly. SGs are highly enriched in mRNAs, containing inverted repeat (IR) Alus in 3′ UTRs, AU-rich elements, and RNA-binding proteins. SGs and processing bodies (P-bodies) transiently interact through a docking mechanism to allow the exchange of RNA species. However, the types of RNA species exchanged, and the mechanisms and outcomes of exchange are still unknown. Specialized RNA-binding proteins, including adenosine deaminase acting on RNA (ADAR1-p150), with an affinity toward inverted repeat Alus, and Tudor staphylococcal nuclease (Tudor-SN) are specifically recruited to SGs under OS along with an RNA transport protein, Staufen1 (STAU1), but their precise biochemical roles in SGs and SG/P-body docking are uncertain. Here, we critically review relevant literature and propose a hypothetical mechanism for the processing and decay of oxidized-RNA in SGs/P-bodies, as well as the role of ADAR1-p150, Tudor-SN, and STAU1. |
| first_indexed | 2024-12-18T23:22:38Z |
| format | Article |
| id | doaj.art-0a3954a969574db8bf987711498f3c24 |
| institution | Directory Open Access Journal |
| issn | 2296-889X |
| language | English |
| last_indexed | 2024-12-18T23:22:38Z |
| publishDate | 2021-06-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Molecular Biosciences |
| spelling | doaj.art-0a3954a969574db8bf987711498f3c242022-12-21T20:47:53ZengFrontiers Media S.A.Frontiers in Molecular Biosciences2296-889X2021-06-01810.3389/fmolb.2021.672988672988Stress Granule-Mediated Oxidized RNA Decay in P-Body: Hypothetical Role of ADAR1, Tudor-SN, and STAU1Ravi Kumar Alluri0Zhongwei Li1Keith R. McCrae2Keith R. McCrae3Department of Cardiovascular and Metabolic Sciences, Lerner Research Institute, Cleveland Clinic, Cleveland, OH, United StatesBiomedical Science Department, College of Medicine, Florida Atlantic University, Boca Raton, FL, United StatesDepartment of Cardiovascular and Metabolic Sciences, Lerner Research Institute, Cleveland Clinic, Cleveland, OH, United StatesTaussig Cancer Institute, Cleveland Clinic, Cleveland, OH, United StatesReactive oxygen species (ROS) generated under oxidative stress (OS) cause oxidative damage to RNA. Recent studies have suggested a role for oxidized RNA in several human disorders. Under the conditions of oxidative stress, mRNAs released from polysome dissociation accumulate and initiate stress granule (SG) assembly. SGs are highly enriched in mRNAs, containing inverted repeat (IR) Alus in 3′ UTRs, AU-rich elements, and RNA-binding proteins. SGs and processing bodies (P-bodies) transiently interact through a docking mechanism to allow the exchange of RNA species. However, the types of RNA species exchanged, and the mechanisms and outcomes of exchange are still unknown. Specialized RNA-binding proteins, including adenosine deaminase acting on RNA (ADAR1-p150), with an affinity toward inverted repeat Alus, and Tudor staphylococcal nuclease (Tudor-SN) are specifically recruited to SGs under OS along with an RNA transport protein, Staufen1 (STAU1), but their precise biochemical roles in SGs and SG/P-body docking are uncertain. Here, we critically review relevant literature and propose a hypothetical mechanism for the processing and decay of oxidized-RNA in SGs/P-bodies, as well as the role of ADAR1-p150, Tudor-SN, and STAU1.https://www.frontiersin.org/articles/10.3389/fmolb.2021.672988/fulloxidative stressstress granulesP-bodiesoxidized RNA3′ UTRADAR1 |
| spellingShingle | Ravi Kumar Alluri Zhongwei Li Keith R. McCrae Keith R. McCrae Stress Granule-Mediated Oxidized RNA Decay in P-Body: Hypothetical Role of ADAR1, Tudor-SN, and STAU1 Frontiers in Molecular Biosciences oxidative stress stress granules P-bodies oxidized RNA 3′ UTR ADAR1 |
| title | Stress Granule-Mediated Oxidized RNA Decay in P-Body: Hypothetical Role of ADAR1, Tudor-SN, and STAU1 |
| title_full | Stress Granule-Mediated Oxidized RNA Decay in P-Body: Hypothetical Role of ADAR1, Tudor-SN, and STAU1 |
| title_fullStr | Stress Granule-Mediated Oxidized RNA Decay in P-Body: Hypothetical Role of ADAR1, Tudor-SN, and STAU1 |
| title_full_unstemmed | Stress Granule-Mediated Oxidized RNA Decay in P-Body: Hypothetical Role of ADAR1, Tudor-SN, and STAU1 |
| title_short | Stress Granule-Mediated Oxidized RNA Decay in P-Body: Hypothetical Role of ADAR1, Tudor-SN, and STAU1 |
| title_sort | stress granule mediated oxidized rna decay in p body hypothetical role of adar1 tudor sn and stau1 |
| topic | oxidative stress stress granules P-bodies oxidized RNA 3′ UTR ADAR1 |
| url | https://www.frontiersin.org/articles/10.3389/fmolb.2021.672988/full |
| work_keys_str_mv | AT ravikumaralluri stressgranulemediatedoxidizedrnadecayinpbodyhypotheticalroleofadar1tudorsnandstau1 AT zhongweili stressgranulemediatedoxidizedrnadecayinpbodyhypotheticalroleofadar1tudorsnandstau1 AT keithrmccrae stressgranulemediatedoxidizedrnadecayinpbodyhypotheticalroleofadar1tudorsnandstau1 AT keithrmccrae stressgranulemediatedoxidizedrnadecayinpbodyhypotheticalroleofadar1tudorsnandstau1 |