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000269004 1001_ $$0P:(DE-2719)2811855$$aGarcía Morato, Jorge$$b0$$eFirst author$$udzne
000269004 245__ $$aProteomics elucidating physiological and pathological functions of TDP‐43
000269004 260__ $$aWeinheim$$bWiley VCH$$c2023
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000269004 520__ $$aTrans-activation response DNA binding protein of 43 kDa (TDP-43) regulates a great variety of cellular processes in the nucleus and cytosol. In addition, a defined subset of neurodegenerative diseases is characterized by nuclear depletion of TDP-43 as well as cytosolic mislocalization and aggregation. To perform its diverse functions TDP-43 can associate with different ribonucleoprotein complexes. Combined with transcriptomics, MS interactome studies have unveiled associations between TDP-43 and the spliceosome machinery, polysomes and RNA granules. Moreover, the highly dynamic, low-valency interactions regulated by its low-complexity domain calls for innovative proximity labeling methodologies. In addition to protein partners, the analysis of post-translational modifications showed that they may play a role in the nucleocytoplasmic shuttling, RNA binding, liquid-liquid phase separation and protein aggregation of TDP-43. Here we review the various TDP-43 ribonucleoprotein complexes characterized so far, how they contribute to the diverse functions of TDP-43, and roles of post-translational modifications. Further understanding of the fluid dynamic properties of TDP-43 in ribonucleoprotein complexes, RNA granules, and self-assemblies will advance the understanding of RNA processing in cells and perhaps help to develop novel therapeutic approaches for TDPopathies.
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000269004 650_2 $$2MeSH$$aProteomics
000269004 650_2 $$2MeSH$$aProtein Aggregates
000269004 650_2 $$2MeSH$$aDNA-Binding Proteins: genetics
000269004 650_2 $$2MeSH$$aRibonucleoproteins
000269004 7001_ $$0P:(DE-2719)2811291$$aGloeckner, Christian Johannes$$b1$$udzne
000269004 7001_ $$0P:(DE-2719)2810803$$aKahle, Philipp$$b2$$eLast author$$udzne
000269004 773__ $$0PERI:(DE-600)2037674-1$$a10.1002/pmic.202200410$$gVol. 23, no. 23-24, p. 2200410$$n23-24$$p2200410$$tProteomics$$v23$$x1615-9853$$y2023
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