Allostery Modulates Interactions between Proteasome Core Particles and Regulatory Particles
Allostery—regulation at distant sites is a key concept in biology. The proteasome exhibits multiple forms of allosteric regulation. This regulatory communication can span a distance exceeding 100 Ångstroms and can modulate interactions between the two major proteasome modules: its core particle and...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-05-01
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| Series: | Biomolecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2218-273X/12/6/764 |
| _version_ | 1827661972653473792 |
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| author | Philip Coffino Yifan Cheng |
| author_facet | Philip Coffino Yifan Cheng |
| author_sort | Philip Coffino |
| collection | DOAJ |
| description | Allostery—regulation at distant sites is a key concept in biology. The proteasome exhibits multiple forms of allosteric regulation. This regulatory communication can span a distance exceeding 100 Ångstroms and can modulate interactions between the two major proteasome modules: its core particle and regulatory complexes. Allostery can further influence the assembly of the core particle with regulatory particles. In this focused review, known and postulated interactions between these proteasome modules are described. Allostery may explain how cells build and maintain diverse populations of proteasome assemblies and can provide opportunities for therapeutic interventions. |
| first_indexed | 2024-03-10T00:18:39Z |
| format | Article |
| id | doaj.art-28c9dbcdb025453382286e26d5d3fdf2 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T00:18:39Z |
| publishDate | 2022-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-28c9dbcdb025453382286e26d5d3fdf22023-11-23T15:46:31ZengMDPI AGBiomolecules2218-273X2022-05-0112676410.3390/biom12060764Allostery Modulates Interactions between Proteasome Core Particles and Regulatory ParticlesPhilip Coffino0Yifan Cheng1Laboratory of Cellular Biophysics, Department of Molecular and Cell Biology, Rockefeller University, New York, NY 10065, USADepartment of Biochemistry and Biophysics, University of California San Francisco, San Francisco, CA 94158, USAAllostery—regulation at distant sites is a key concept in biology. The proteasome exhibits multiple forms of allosteric regulation. This regulatory communication can span a distance exceeding 100 Ångstroms and can modulate interactions between the two major proteasome modules: its core particle and regulatory complexes. Allostery can further influence the assembly of the core particle with regulatory particles. In this focused review, known and postulated interactions between these proteasome modules are described. Allostery may explain how cells build and maintain diverse populations of proteasome assemblies and can provide opportunities for therapeutic interventions.https://www.mdpi.com/2218-273X/12/6/764allosteryproteasomeassemblyAAA+ ATPaseproteolysisubiquitin |
| spellingShingle | Philip Coffino Yifan Cheng Allostery Modulates Interactions between Proteasome Core Particles and Regulatory Particles Biomolecules allostery proteasome assembly AAA+ ATPase proteolysis ubiquitin |
| title | Allostery Modulates Interactions between Proteasome Core Particles and Regulatory Particles |
| title_full | Allostery Modulates Interactions between Proteasome Core Particles and Regulatory Particles |
| title_fullStr | Allostery Modulates Interactions between Proteasome Core Particles and Regulatory Particles |
| title_full_unstemmed | Allostery Modulates Interactions between Proteasome Core Particles and Regulatory Particles |
| title_short | Allostery Modulates Interactions between Proteasome Core Particles and Regulatory Particles |
| title_sort | allostery modulates interactions between proteasome core particles and regulatory particles |
| topic | allostery proteasome assembly AAA+ ATPase proteolysis ubiquitin |
| url | https://www.mdpi.com/2218-273X/12/6/764 |
| work_keys_str_mv | AT philipcoffino allosterymodulatesinteractionsbetweenproteasomecoreparticlesandregulatoryparticles AT yifancheng allosterymodulatesinteractionsbetweenproteasomecoreparticlesandregulatoryparticles |