Author Correction: The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation
| Autor: | Johanna Bialas, Andrej Berg, Gunter Schmidtke, Nicola Catone, Philip Rößler, Sophie Stotz, Christine Peter, Samira Anders, Sophia Scheuermann, Silke Wiesner, Ricarda Schwab, Annette Aichem, Mira C. Schütz-Stoffregen, Marcus Groettrup |
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| Rok vydání: | 2018 |
| Předmět: |
Structure (mathematical logic)
Multidisciplinary biology Computer science Mechanism (biology) Science InformationSystems_INFORMATIONSTORAGEANDRETRIEVAL General Physics and Astronomy ComputerApplications_COMPUTERSINOTHERSYSTEMS General Chemistry Computational biology General Biochemistry Genetics and Molecular Biology Article Ubiquitin biology.protein ComputingMilieux_COMPUTERSANDEDUCATION ComputingMethodologies_DOCUMENTANDTEXTPROCESSING ComputingMilieux_COMPUTERSANDSOCIETY lcsh:Q lcsh:Science |
| Zdroj: | Nature Communications Nature Communications, Vol 9, Iss 1, Pp 1-1 (2018) |
| ISSN: | 2041-1723 |
| Popis: | FAT10 is a ubiquitin-like modifier that directly targets proteins for proteasomal degradation. Here, we report the high-resolution structures of the two individual ubiquitin-like domains (UBD) of FAT10 that are joined by a flexible linker. While the UBDs of FAT10 show the typical ubiquitin-fold, their surfaces are entirely different from each other and from ubiquitin explaining their unique binding specificities. Deletion of the linker abrogates FAT10-conjugation while its mutation blocks auto-FAT10ylation of the FAT10-conjugating enzyme USE1 but not bulk conjugate formation. FAT10- but not ubiquitin-mediated degradation is independent of the segregase VCP/p97 in the presence but not the absence of FAT10’s unstructured N-terminal heptapeptide. Stabilization of the FAT10 UBDs strongly decelerates degradation suggesting that the intrinsic instability of FAT10 together with its disordered N-terminus enables the rapid, joint degradation of FAT10 and its substrates without the need for FAT10 de-conjugation and partial substrate unfolding. The ubiquitin-like modifier FAT10 is composed of two ubiquitin-like domains (UBDs). Here the authors present the FAT10 UBD structures and show that the unstructured FAT10 N-terminal heptapeptide together with the poor stability of FAT10 facilitate the rapid proteasomal targeting of FAT10 along with its substrates. |
| Databáze: | OpenAIRE |
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