The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation

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...

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Autores principales:	Annette Aichem, Samira Anders, Nicola Catone, Philip Rößler, Sophie Stotz, Andrej Berg, Ricarda Schwab, Sophia Scheuermann, Johanna Bialas, Mira C. Schütz-Stoffregen, Gunter Schmidtke, Christine Peter, Marcus Groettrup, Silke Wiesner
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/8af997f790444de5b901c153993949d5
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spelling	oai:doaj.org-article:8af997f790444de5b901c153993949d52021-12-02T17:31:46ZThe structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation10.1038/s41467-018-05776-32041-1723https://doaj.org/article/8af997f790444de5b901c153993949d52018-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-05776-3https://doaj.org/toc/2041-1723The 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.Annette AichemSamira AndersNicola CatonePhilip RößlerSophie StotzAndrej BergRicarda SchwabSophia ScheuermannJohanna BialasMira C. Schütz-StoffregenGunter SchmidtkeChristine PeterMarcus GroettrupSilke WiesnerNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Annette Aichem Samira Anders Nicola Catone Philip Rößler Sophie Stotz Andrej Berg Ricarda Schwab Sophia Scheuermann Johanna Bialas Mira C. Schütz-Stoffregen Gunter Schmidtke Christine Peter Marcus Groettrup Silke Wiesner The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation
description	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.
format	article
author	Annette Aichem Samira Anders Nicola Catone Philip Rößler Sophie Stotz Andrej Berg Ricarda Schwab Sophia Scheuermann Johanna Bialas Mira C. Schütz-Stoffregen Gunter Schmidtke Christine Peter Marcus Groettrup Silke Wiesner
author_facet	Annette Aichem Samira Anders Nicola Catone Philip Rößler Sophie Stotz Andrej Berg Ricarda Schwab Sophia Scheuermann Johanna Bialas Mira C. Schütz-Stoffregen Gunter Schmidtke Christine Peter Marcus Groettrup Silke Wiesner
author_sort	Annette Aichem
title	The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation
title_short	The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation
title_full	The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation
title_fullStr	The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation
title_full_unstemmed	The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation
title_sort	structure of the ubiquitin-like modifier fat10 reveals an alternative targeting mechanism for proteasomal degradation
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/8af997f790444de5b901c153993949d5
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The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation

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