We con-dense if we want to; We can't leave AZUL outside

Thuy P Dao; Carlos A Castañeda

doi:10.1016/j.str.2023.03.006

We con-dense if we want to; We can't leave AZUL outside

Structure. 2023 Apr 6;31(4):369-371. doi: 10.1016/j.str.2023.03.006.

Authors

Thuy P Dao¹, Carlos A Castañeda²

Affiliations

¹ Departments of Biology and Chemistry, Syracuse University, Syracuse, NY 13244, USA.
² Departments of Biology and Chemistry, Syracuse University, Syracuse, NY 13244, USA; Bioinspired Institute, Syracuse University, Syracuse, NY 13244, USA; Program in Neuroscience, Syracuse University, Syracuse, NY 13244, USA. Electronic address: cacastan@syr.edu.

PMID: 37028393
DOI: 10.1016/j.str.2023.03.006

Abstract

In this issue of Structure, Buel et al. (2023) combined NMR data with AlphaFold2 to map out the interaction between the AZUL domain of ubiquitin ligase E6AP and UBQLN1/2 UBA. The authors demonstrated that this interaction enhances the self-association of the helix neighboring UBA and enables E6AP to localize to UBQLN2 droplets.

Publication types

Research Support, N.I.H., Extramural
Comment

MeSH terms

Protein Binding
Ubiquitin* / metabolism
Ubiquitin-Protein Ligases* / chemistry

Substances

Ubiquitin
Ubiquitin-Protein Ligases

Grants and funding

R01 GM136946/GM/NIGMS NIH HHS/United States