Proteomics

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Mapping of TDP-43 ubiquitination and acetylation sites

ABSTRACT: TAR DNA binding protein of 43 kDa (TDP-43) forms aggregates in neurodegenerative diseases, particularly certain forms of frontotemporal dementia and amyotrophic lateral sclerosis. Pathological modifications of TDP-43 include proteolytic fragmentation, phosphorylation, and ubiquitinylation. In this study, we systematically mapped TDP-42 ubiquitination as well as acetylation sites.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

DISEASE(S): Frontotemporal Dementia,Amyotrophic Lateral Sclerosis

SUBMITTER: Johannes Gloeckner  

LAB HEAD: Christian Johannes Gloeckner

PROVIDER: PXD030170 | Pride | 2022-04-01

REPOSITORIES: Pride

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Publications

Sirtuin-1 sensitive lysine-136 acetylation drives phase separation and pathological aggregation of TDP-43.

Garcia Morato Jorge J   Hans Friederike F   von Zweydorf Felix F   Feederle Regina R   Elsässer Simon J SJ   Skodras Angelos A AA   Gloeckner Christian Johannes CJ   Buratti Emanuele E   Neumann Manuela M   Kahle Philipp J PJ  

Nature communications 20220309 1

Trans-activation response DNA-binding protein of 43  kDa (TDP-43) regulates RNA processing and forms neuropathological aggregates in patients with amyotrophic lateral sclerosis and frontotemporal lobar degeneration. Investigating TDP-43 post-translational modifications, we discovered that K84 acetylation reduced nuclear import whereas K136 acetylation impaired RNA binding and splicing capabilities of TDP-43. Such failure of RNA interaction triggered TDP-43 phase separation mediated by the C-term  ...[more]

PMID: 35264561

Publication: 1/2

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