The midnolin-proteasome pathway catches proteins for ubiquitination-independent degradation.
Science
; 381(6660): eadh5021, 2023 08 25.
Article
em En
| MEDLINE
| ID: mdl-37616343
ABSTRACT
Cells use ubiquitin to mark proteins for proteasomal degradation. Although the proteasome also eliminates proteins that are not ubiquitinated, how this occurs mechanistically is unclear. Here, we found that midnolin promoted the destruction of many nuclear proteins, including transcription factors encoded by the immediate-early genes. Diverse stimuli induced midnolin, and its overexpression was sufficient to cause the degradation of its targets by a mechanism that did not require ubiquitination. Instead, midnolin associated with the proteasome via an α helix, used its Catch domain to bind a region within substrates that can form a ß strand, and used a ubiquitin-like domain to promote substrate destruction. Thus, midnolin contains three regions that function in concert to target a large set of nuclear proteins to the proteasome for degradation.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Transcrição Gênica
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Proteínas Nucleares
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Genes Precoces
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Complexo de Endopeptidases do Proteassoma
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Proteólise
Idioma:
En
Ano de publicação:
2023
Tipo de documento:
Article