Linear Ubiquitin Chain-Binding Domains

Authors

Lilian Fennell, Vienna BioCenter
Simin Rahighi, Chapman UniversityFollow
Fumiyo Ikeda, Vienna BioCenter

Document Type

Article

Publication Date

4-30-2018

Abstract

Ubiquitin modification (ubiquitination) of target proteins can vary with respect to chain lengths, linkage type, and chain forms, such as homologous, mixed, and branched ubiquitin chains. Thus, ubiquitination can generate multiple unique surfaces on a target protein substrate. Ubiquitin‐binding domains (UBDs) recognize ubiquitinated substrates, by specifically binding to these unique surfaces, modulate the formation of cellular signaling complexes and regulate downstream signaling cascades. Among the eight different homotypic chain types, Met1‐linked (also termed linear) chains are the only chains in which linkage occurs on a non‐Lys residue of ubiquitin. Linear ubiquitin chains have been implicated in immune responses, cell death and autophagy, and several UBDs ‐ specific for linear ubiquitin chains ‐ have been identified. In this review, we describe the main principles of ubiquitin recognition by UBDs, focusing on linear ubiquitin chains and their roles in biology.

Comments

This article was originally published in FEBS Journal in 2018. DOI: 10.1111/febs.14478

Recommended Citation

Fennell L, Rahighi S, Ikeda F. Linear ubiquitin chain-binding domains. FEBS J. 2018. doi: 10.1111/febs.14478

Copyright

Wiley

Creative Commons License

This work is licensed under a Creative Commons Attribution 4.0 License.