FAT10ylation as a signal for proteasomal degradation

Schmidtke, Gunter; Aichem, Annette; Gröttrup, Marcus

FAT10ylation as a signal for proteasomal degradation

Dateien

Schmidtke_219830.pdfGröße: 282.51 KBDownloads: 321

Datum

2014

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 2014, 1843(1), pp. 97-102. ISSN 0167-4889. eISSN 0006-3002. Available under: doi: 10.1016/j.bbamcr.2013.01.009

Zusammenfassung

The Nobel prize has been awarded for the discovery of ubiquitin as a transferable signal for the degradation of proteins by the 26S proteasome. While isopeptide linkage of a protein with a single ubiquitin does not serve as a degradation signal for the proteasome, poly-ubiquitylation via several different lysine residues within ubiquitin leads to efficient proteasomal degradation. Ubiquitin-like modifiers have not been shown to directly mediate proteasomal degradation except for the cytokine inducible modifier HLA-F adjacent transcript 10 (FAT10), which consists of two ubiquitin-like domains. FAT10 ends with a free diglycine motif at its C-terminus which is required for isopeptide linkage to hundreds of different substrates. In contrast to ubiquitin, a single FAT10 suffices to bind to the 26S proteasome and to efficiently mediate proteasomal degradation in a ubiquitin-independent manner. Here we review the data on ubiquitin-independent degradation by FAT10, on how FAT10 is conjugated to its substrates, how FAT10 binds to the 26S proteasome, and how the ubiquitin-like (UBL)-ubiquitin-associated (UBA) protein NUB1L accelerates FAT10 mediated proteolysis. Finally, with a glimpse on recently identified substrates, we will discuss the currently emerging knowledge about the biological functions of FAT10. This article is part of a Special Issue entitled: Ubiquitin-Proteasome System.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Schlagwörter

Ubiquitin, Proteasome, FAT10, Degradation, NUB1L

Zitieren

ISO 690

SCHMIDTKE, Gunter, Annette AICHEM, Marcus GRÖTTRUP, 2014. FAT10ylation as a signal for proteasomal degradation. In: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 2014, 1843(1), pp. 97-102. ISSN 0167-4889. eISSN 0006-3002. Available under: doi: 10.1016/j.bbamcr.2013.01.009

BibTex

@article{Schmidtke2014-01FAT10-21983,
  year={2014},
  doi={10.1016/j.bbamcr.2013.01.009},
  title={FAT10ylation as a signal for proteasomal degradation},
  number={1},
  volume={1843},
  issn={0167-4889},
  journal={Biochimica et Biophysica Acta (BBA) - Molecular Cell Research},
  pages={97--102},
  author={Schmidtke, Gunter and Aichem, Annette and Gröttrup, Marcus}
}

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