Lou Gehrig's Disease (ALS): UBQLN2 Mutations Strike Out of Phase

Nicole Higgins; Brian Lin; Mervyn J Monteiro

doi:10.1016/j.str.2019.05.006

Lou Gehrig's Disease (ALS): UBQLN2 Mutations Strike Out of Phase

Structure. 2019 Jun 4;27(6):879-881. doi: 10.1016/j.str.2019.05.006.

Authors

Nicole Higgins¹, Brian Lin¹, Mervyn J Monteiro²

Affiliations

¹ The Center for Biomedical Engineering and Technology, Department of Anatomy and Neurobiology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
² The Center for Biomedical Engineering and Technology, Department of Anatomy and Neurobiology, University of Maryland School of Medicine, Baltimore, MD 21201, USA. Electronic address: monteiro@som.umaryland.edu.

Abstract

In this issue of Structure, Dao et al. (2019) report that ALS-linked mutations in the Pxx domain of Ubiquilin 2 (UBQLN2) differentially influence the protein's phase separation abilities. The affect is by reducing the temperature and UBQLN2 concentration necessary for liquid-liquid phase separation droplet formation and by modulating UBQLN2 oligomerization.

Publication types

Research Support, Non-U.S. Gov't
Comment

MeSH terms

Adaptor Proteins, Signal Transducing
Amino Acids
Amyotrophic Lateral Sclerosis*
Autophagy-Related Proteins
Cell Cycle Proteins / genetics
Humans
Mutation
Ubiquitins / genetics

Substances

Adaptor Proteins, Signal Transducing
Amino Acids
Autophagy-Related Proteins
Cell Cycle Proteins
UBQLN2 protein, human
Ubiquitins

Supplementary concepts

Amyotrophic Lateral Sclerosis 2, Juvenile

Abstract

Publication types

MeSH terms

Substances

Supplementary concepts

Grants and funding