Biological and Pathological Implications of an Alternative ATP-Powered Proteasomal Assembly With Cdc48 and the 20S Peptidase
The ATP-powered protein degradation machinery plays essential roles in maintaining protein homeostasis in all organisms. Robust proteolytic activities are typically sequestered within protein complexes to avoid the fatal removal of essential proteins. Because the openings of proteolytic chambers are...
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Frontiers Media S.A.
2018-06-01
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| Series: | Frontiers in Molecular Biosciences |
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| Online Access: | https://www.frontiersin.org/article/10.3389/fmolb.2018.00056/full |
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| author | Masatoshi Esaki Masatoshi Esaki Ai Johjima-Murata Ai Johjima-Murata Md. Tanvir Islam Md. Tanvir Islam Teru Ogura Teru Ogura Teru Ogura |
| author_facet | Masatoshi Esaki Masatoshi Esaki Ai Johjima-Murata Ai Johjima-Murata Md. Tanvir Islam Md. Tanvir Islam Teru Ogura Teru Ogura Teru Ogura |
| author_sort | Masatoshi Esaki |
| collection | DOAJ |
| description | The ATP-powered protein degradation machinery plays essential roles in maintaining protein homeostasis in all organisms. Robust proteolytic activities are typically sequestered within protein complexes to avoid the fatal removal of essential proteins. Because the openings of proteolytic chambers are narrow, substrate proteins must undergo unfolding. AAA superfamily proteins (ATPases associated with diverse cellular activities) are mostly located at these openings and regulate protein degradation appropriately. The 26S proteasome, comprising 20S peptidase and 19S regulatory particles, is the major ATP-powered protein degradation machinery in eukaryotes. The 19S particles are composed of six AAA proteins and 13 regulatory proteins, and bind to both ends of a barrel-shaped proteolytic chamber formed by the 20S peptidase. Several recent studies have reported that another AAA protein, Cdc48, can replace the 19S particles to form an alternative ATP-powered proteasomal complex, i.e., the Cdc48-20S proteasome. This review focuses on our current knowledge of this alternative proteasome and its possible linkage to amyotrophic lateral sclerosis. |
| first_indexed | 2024-12-23T19:37:11Z |
| format | Article |
| id | doaj.art-dafc4761ade54f2881b92dfae214b66e |
| institution | Directory Open Access Journal |
| issn | 2296-889X |
| language | English |
| last_indexed | 2024-12-23T19:37:11Z |
| publishDate | 2018-06-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Molecular Biosciences |
| spelling | doaj.art-dafc4761ade54f2881b92dfae214b66e2022-12-21T17:33:46ZengFrontiers Media S.A.Frontiers in Molecular Biosciences2296-889X2018-06-01510.3389/fmolb.2018.00056384176Biological and Pathological Implications of an Alternative ATP-Powered Proteasomal Assembly With Cdc48 and the 20S PeptidaseMasatoshi Esaki0Masatoshi Esaki1Ai Johjima-Murata2Ai Johjima-Murata3Md. Tanvir Islam4Md. Tanvir Islam5Teru Ogura6Teru Ogura7Teru Ogura8Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto, JapanCore Research for Evolutional Science and Technology, Japan Science and Technology Agency, Saitama, JapanDepartment of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto, JapanCore Research for Evolutional Science and Technology, Japan Science and Technology Agency, Saitama, JapanDepartment of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto, JapanProgram for Leading Graduate Schools “HIGO Program, ” Kumamoto University, Kumamoto, JapanDepartment of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto, JapanCore Research for Evolutional Science and Technology, Japan Science and Technology Agency, Saitama, JapanProgram for Leading Graduate Schools “HIGO Program, ” Kumamoto University, Kumamoto, JapanThe ATP-powered protein degradation machinery plays essential roles in maintaining protein homeostasis in all organisms. Robust proteolytic activities are typically sequestered within protein complexes to avoid the fatal removal of essential proteins. Because the openings of proteolytic chambers are narrow, substrate proteins must undergo unfolding. AAA superfamily proteins (ATPases associated with diverse cellular activities) are mostly located at these openings and regulate protein degradation appropriately. The 26S proteasome, comprising 20S peptidase and 19S regulatory particles, is the major ATP-powered protein degradation machinery in eukaryotes. The 19S particles are composed of six AAA proteins and 13 regulatory proteins, and bind to both ends of a barrel-shaped proteolytic chamber formed by the 20S peptidase. Several recent studies have reported that another AAA protein, Cdc48, can replace the 19S particles to form an alternative ATP-powered proteasomal complex, i.e., the Cdc48-20S proteasome. This review focuses on our current knowledge of this alternative proteasome and its possible linkage to amyotrophic lateral sclerosis.https://www.frontiersin.org/article/10.3389/fmolb.2018.00056/fullAAA ATPaseCdc48/p97/VCPproteasomeproteolysisSod1ALS |
| spellingShingle | Masatoshi Esaki Masatoshi Esaki Ai Johjima-Murata Ai Johjima-Murata Md. Tanvir Islam Md. Tanvir Islam Teru Ogura Teru Ogura Teru Ogura Biological and Pathological Implications of an Alternative ATP-Powered Proteasomal Assembly With Cdc48 and the 20S Peptidase Frontiers in Molecular Biosciences AAA ATPase Cdc48/p97/VCP proteasome proteolysis Sod1 ALS |
| title | Biological and Pathological Implications of an Alternative ATP-Powered Proteasomal Assembly With Cdc48 and the 20S Peptidase |
| title_full | Biological and Pathological Implications of an Alternative ATP-Powered Proteasomal Assembly With Cdc48 and the 20S Peptidase |
| title_fullStr | Biological and Pathological Implications of an Alternative ATP-Powered Proteasomal Assembly With Cdc48 and the 20S Peptidase |
| title_full_unstemmed | Biological and Pathological Implications of an Alternative ATP-Powered Proteasomal Assembly With Cdc48 and the 20S Peptidase |
| title_short | Biological and Pathological Implications of an Alternative ATP-Powered Proteasomal Assembly With Cdc48 and the 20S Peptidase |
| title_sort | biological and pathological implications of an alternative atp powered proteasomal assembly with cdc48 and the 20s peptidase |
| topic | AAA ATPase Cdc48/p97/VCP proteasome proteolysis Sod1 ALS |
| url | https://www.frontiersin.org/article/10.3389/fmolb.2018.00056/full |
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