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Tytuł pozycji:

Mutations linked to neurological disease enhance self-association of low-complexity protein sequences.

Tytuł:
Mutations linked to neurological disease enhance self-association of low-complexity protein sequences.
Autorzy:
Zhou X; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Sumrow L; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Tashiro K; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Sutherland L; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Liu D; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Qin T; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Kato M; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.; Institute for Quantum Life Science, National Institutes for Quantum and Radiological Science and Technology, Inage, Chiba, 263-8555, Japan.
Liszczak G; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
McKnight SL; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Źródło:
Science (New York, N.Y.) [Science] 2022 Jul; Vol. 377 (6601), pp. eabn5582. Date of Electronic Publication: 2022 Jul 01.
Typ publikacji:
Journal Article
Język:
English
Imprint Name(s):
Publication: : Washington, DC : American Association for the Advancement of Science
Original Publication: New York, N.Y. : [s.n.] 1880-
MeSH Terms:
Alzheimer Disease*/genetics
Charcot-Marie-Tooth Disease*/genetics
DNA-Binding Proteins*/chemistry
DNA-Binding Proteins*/genetics
Frontotemporal Dementia*/genetics
Cells, Cultured ; Humans ; Mutation, Missense ; Protein Domains ; Protein Folding ; Protein Stability
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Grant Information:
R35 GM130358 United States GM NIGMS NIH HHS; S10 OD021684 United States OD NIH HHS; U54 CA231649 United States CA NCI NIH HHS
Substance Nomenclature:
0 (DNA-Binding Proteins)
0 (TARDBP protein, human)
Entry Date(s):
Date Created: 20220630 Date Completed: 20220704 Latest Revision: 20230102
Update Code:
20240105
PubMed Central ID:
PMC9610444
DOI:
10.1126/science.abn5582
PMID:
35771920
Czasopismo naukowe
Protein domains of low sequence complexity do not fold into stable, three-dimensional structures. Nevertheless, proteins with these sequences assist in many aspects of cell organization, including assembly of nuclear and cytoplasmic structures not surrounded by membranes. The dynamic nature of these cellular assemblies is caused by the ability of low-complexity domains (LCDs) to transiently self-associate through labile, cross-β structures. Mechanistic studies useful for the study of LCD self-association have evolved over the past decade in the form of simple assays of phase separation. Here, we have used such assays to demonstrate that the interactions responsible for LCD self-association can be dictated by labile protein structures poised close to equilibrium between the folded and unfolded states. Furthermore, missense mutations causing Charcot-Marie-Tooth disease, frontotemporal dementia, and Alzheimer's disease manifest their pathophysiology in vitro and in cultured cell systems by enhancing the stability of otherwise labile molecular structures formed upon LCD self-association.
Comment in: Science. 2022 Jul;377(6601):31-32. (PMID: 35771902)
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