Reply: Does the polyubiquitination pathway operate inside intact chloroplasts to remove proteins?
The ubiquitin-proteasome system (UPS) is the pre-eminent proteolytic system in eukaryotic cells. Its components are abundant in the cytosol and nucleus, and it selectively targets many proteins in both of these compartments for degradation. However, its functions are not restricted to nucleocytosoli...
| Auteurs principaux: | , , , , , , |
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| Format: | Journal article |
| Langue: | English |
| Publié: |
American Society of Plant Biologists
2024
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| _version_ | 1826314473576595456 |
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| author | Jarvis, RP Li, J Lin, R Ling, Q Lyu, Y Sun, Y Yao, Z |
| author_facet | Jarvis, RP Li, J Lin, R Ling, Q Lyu, Y Sun, Y Yao, Z |
| author_sort | Jarvis, RP |
| collection | OXFORD |
| description | The ubiquitin-proteasome system (UPS) is the pre-eminent proteolytic system in eukaryotic cells. Its components are abundant in the cytosol and nucleus, and it selectively targets many proteins in both of these compartments for degradation. However, its functions are not restricted to nucleocytosolic proteins as it is now very well established that the UPS also targets proteins in organelles. For example, endoplasmic reticulum (ER) proteins are commonly degraded by the cytosolic proteasome following their extraction (or retrotranslocation) from the organelle, in a process termed ER-associated protein degradation (ERAD). In recent years, it has emerged that even proteins in endosymbiotic organelles (mitochondria and chloroplasts) are processed by ERAD-analogous systems. Ubiquitin-dependent degradation of chloroplast-resident proteins was initially described as a regulatory mechanism governing the chloroplast protein import machinery. This so called chloroplast-associated protein degradation (CHLORAD) system was assumed to act only at the surface of the organelle owing to the physical barrier presented by the double envelope membrane. However, recent results suggested that the UPS may have a more extensive role in regulating chloroplast proteins, affecting even those located internally. Though somewhat surprising, these results were not entirely unpredictable given that there are numerous historical reports suggesting ubiquitin action in chloroplasts, and there is increasing evidence that the UPS acts on internal mitochondrial proteins. We review the relevant literature, address corresponding criticisms, and present additional data supporting the possibility of UPS action inside chloroplasts. |
| first_indexed | 2024-04-23T08:26:50Z |
| format | Journal article |
| id | oxford-uuid:2a673476-0f7a-4999-bea3-d67776bda4e3 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-09-25T04:33:03Z |
| publishDate | 2024 |
| publisher | American Society of Plant Biologists |
| record_format | dspace |
| spelling | oxford-uuid:2a673476-0f7a-4999-bea3-d67776bda4e32024-09-10T10:04:53ZReply: Does the polyubiquitination pathway operate inside intact chloroplasts to remove proteins?Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:2a673476-0f7a-4999-bea3-d67776bda4e3EnglishSymplectic ElementsAmerican Society of Plant Biologists2024Jarvis, RPLi, JLin, RLing, QLyu, YSun, YYao, ZThe ubiquitin-proteasome system (UPS) is the pre-eminent proteolytic system in eukaryotic cells. Its components are abundant in the cytosol and nucleus, and it selectively targets many proteins in both of these compartments for degradation. However, its functions are not restricted to nucleocytosolic proteins as it is now very well established that the UPS also targets proteins in organelles. For example, endoplasmic reticulum (ER) proteins are commonly degraded by the cytosolic proteasome following their extraction (or retrotranslocation) from the organelle, in a process termed ER-associated protein degradation (ERAD). In recent years, it has emerged that even proteins in endosymbiotic organelles (mitochondria and chloroplasts) are processed by ERAD-analogous systems. Ubiquitin-dependent degradation of chloroplast-resident proteins was initially described as a regulatory mechanism governing the chloroplast protein import machinery. This so called chloroplast-associated protein degradation (CHLORAD) system was assumed to act only at the surface of the organelle owing to the physical barrier presented by the double envelope membrane. However, recent results suggested that the UPS may have a more extensive role in regulating chloroplast proteins, affecting even those located internally. Though somewhat surprising, these results were not entirely unpredictable given that there are numerous historical reports suggesting ubiquitin action in chloroplasts, and there is increasing evidence that the UPS acts on internal mitochondrial proteins. We review the relevant literature, address corresponding criticisms, and present additional data supporting the possibility of UPS action inside chloroplasts. |
| spellingShingle | Jarvis, RP Li, J Lin, R Ling, Q Lyu, Y Sun, Y Yao, Z Reply: Does the polyubiquitination pathway operate inside intact chloroplasts to remove proteins? |
| title | Reply: Does the polyubiquitination pathway operate inside intact chloroplasts to remove proteins? |
| title_full | Reply: Does the polyubiquitination pathway operate inside intact chloroplasts to remove proteins? |
| title_fullStr | Reply: Does the polyubiquitination pathway operate inside intact chloroplasts to remove proteins? |
| title_full_unstemmed | Reply: Does the polyubiquitination pathway operate inside intact chloroplasts to remove proteins? |
| title_short | Reply: Does the polyubiquitination pathway operate inside intact chloroplasts to remove proteins? |
| title_sort | reply does the polyubiquitination pathway operate inside intact chloroplasts to remove proteins |
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