PF20910

TAR DNA-binding protein 43, C-terminal

Pfam entry
Member databasePfam
Pfam typedisordered
Short nameTDP-43_C
Author Chuguransky S;0000-0002-0520-0736
Sequence Ontology0100003

Description

TDP-43 is a member of the heterogeneous nuclear ribonucleoprotein (hnRNP) family, which is involved in RNA processing and in stress granule response. It is linked to the pathogenesis of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). It is the main component of intraneuronal inclusion bodies (IBs), a pathological hallmark of ALS. This entry represents the C-terminal Gly-rich region of TAR DNA-binding protein 43 (TDP-43) [1-4], which is an intrinsically disordered prion-like domain, capable of assemble into dynamic oligomers rich in beta-sheet structures, being responsible of TDP-43 aggregation
[1]
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References

1.Strategies in the design and development of (TAR) DNA-binding protein 43 (TDP-43) binding ligands. Rao PPN, Shakeri A, Zhao Y, Calon F. Eur J Med Chem 225, 113753, (2021). PMID: 34388383

Further reading

2. Expanding the TDP-43 Proteinopathy Pathway From Neurons to Muscle: Physiological and Pathophysiological Functions. Versluys L, Ervilha Pereira P, Schuermans N, De Paepe B, De Bleecker JL, Bogaert E, Dermaut B. Front Neurosci 16, 815765, (2022). View articlePMID: 35185458

3. ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. Lim L, Wei Y, Lu Y, Song J. PLoS Biol 14, e1002338, (2016). View articlePMID: 26735904

4. Cellular model of TAR DNA-binding protein 43 (TDP-43) aggregation based on its C-terminal Gln/Asn-rich region. Budini M, Buratti E, Stuani C, Guarnaccia C, Romano V, De Conti L, Baralle FE. J Biol Chem 287, 7512-25, (2012). View articlePMID: 22235134

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