Ubiquitin-binding domains

  title={Ubiquitin-binding domains},
  author={Linda A Hicke and Heidi L. Schubert and Christopher P. Hill},
  journal={Nature Reviews Molecular Cell Biology},
Ubiquitin-binding domains (UBDs) are a collection of modular protein domains that non-covalently bind to ubiquitin. These recently discovered motifs interpret and transmit information conferred by protein ubiquitylation to control various cellular events. Detailed molecular structures are known for a number of UBDs, but to understand their mechanism of action, we also need to know how binding specificity is determined, how ubiquitin binding is regulated, and the function of UBDs in the context… 

Ubiquitin-binding domains — from structures to functions

New structure-based insights provide strategies for controlling cellular processes by targeting ubiquitin–UBD interfaces with implications for drug design and cell reprograming.

A new side to ubiquitin.

Ubiquitin binding domains – from structure to application

  • Ruofan Yang
  • Biology
    IOP Conference Series: Materials Science and Engineering
  • 2020
Some recent work on UBDs characterization and application is summarized, finding that UBD’s are good tools pool for material design such as ubiquitin pathway inhibitor, ubiquit in enrichment material and manufactural specific ubiquitIn chain antibody.

Delivery of ubiquitinated substrates to protein-unfolding machines

The intimate interplay between the proteasome and Cdc48, mediated in part by loosely associated ubiquitin receptors, has important functions in cellular regulation.

Ubiquitin‐binding domains: Mechanisms of ubiquitin recognition and use as tools to investigate ubiquitin‐modified proteomes

This work focuses on the use of UBDs to directly purify or detect (poly)ubiquitin‐modified proteins and more broadly for the targeted manipulation of ubiquitIn‐mediated processes, highlighting insights into ubiquitin signalling that have been provided.

Structural mechanisms underlying posttranslational modification by ubiquitin-like proteins.

Structures are now available for many protein complexes in E1-E2-E3 cascades, revealing a series of modular building blocks and providing mechanistic insights into their functions.

Characterization of ubiquitin-binding domain in C1orf124 protein

It is showed that C1orf124 protein binds monoubiquitin and polyubiquit in chains, and interaction is achieved through hydrophobic patch surrounding Ile44 on ubiquitIn and Asp residue in-between second Zn-binding dyad of UBZ4 domain.



Proteins containing the UBA domain are able to bind to multi-ubiquitin chains

It is shown that the UBA domain is responsible for this activity, and two other proteins containing this motif, the fission-yeast homologues of Rad23 and Dsk2, are also shown to bind multi-ubiquitin chains via their UBA domains.

Ubiquitin: structures, functions, mechanisms.

Structure and Ubiquitin Binding of the Ubiquitin-interacting Motif*

It is found that UIM peptides from several proteins involved in endocytosis and vacuolar protein sorting including Hrs, Vps27p, Stam1, and Eps15 bound specifically, but with modest affinity, to free ubiquitin.

Specificity of the Interaction between Ubiquitin-associated Domains and Ubiquitin*

The results suggest that UBA domains may interact with Ub as well as other proteins in more than one way while utilizing the same binding surface.

Mechanism of Ubiquitin Recognition by the CUE Domain of Vps9p

A 26 S protease subunit that binds ubiquitin conjugates.

The novel functions of ubiquitination in signaling.

Analysis of the Role of Ubiquitin-interacting Motifs in Ubiquitin Binding and Ubiquitylation*[boxs]

This study found that many, but not all, UIM-containing proteins were ubiquitylated, and revealed specific amino acids that are important for both polyubiquitin binding and ubiquitin conjugation.

Binding of polyubiquitin chains to ubiquitin-associated (UBA) domains of HHR23A.