The Different Faces of the TDP-43 Low-Complexity Domain: The Formation of Liquid Droplets and Amyloid Fibrils.
TAR-DNA binding protein 43
amyloid fibrils
amyotrophic lateral sclerosis
liquid droplet
low-complexity domain
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
30 Jul 2021
30 Jul 2021
Historique:
received:
25
06
2021
revised:
22
07
2021
accepted:
27
07
2021
entrez:
7
8
2021
pubmed:
8
8
2021
medline:
9
9
2021
Statut:
epublish
Résumé
Transactive response DNA-binding protein 43 (TDP-43) is a nucleic acid-binding protein that is involved in transcription and translation regulation, non-coding RNA processing, and stress granule assembly. Aside from its multiple functions, it is also known as the signature protein in the hallmark inclusions of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD) patients. TDP-43 is built of four domains, but its low-complexity domain (LCD) has become an intense research focus that brings to light its possible role in TDP-43 functions and involvement in the pathogenesis of these neurodegenerative diseases. Recent endeavors have further uncovered the distinct biophysical properties of TDP-43 under various circumstances. In this review, we summarize the multiple structural and biochemical properties of LCD in either promoting the liquid droplets or inducing fibrillar aggregates. We also revisit the roles of the LCD in paraspeckles, stress granules, and cytoplasmic inclusions to date.
Identifiants
pubmed: 34360978
pii: ijms22158213
doi: 10.3390/ijms22158213
pmc: PMC8348237
pii:
doi:
Substances chimiques
Amyloid
0
DNA-Binding Proteins
0
TARDBP protein, human
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Ministry of Science and Technology, Taiwan
ID : MOST-110-2113-M-001-055
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