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000155735 037__ $$aDZNE-2021-00903
000155735 041__ $$aEnglish
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000155735 1001_ $$0P:(DE-2719)9000764$$aSiegert, Anna$$b0$$eFirst author
000155735 245__ $$aInterplay between tau and α-synuclein liquid-liquid phase separation.
000155735 260__ $$aBethesda, Md.$$bProtein Society$$c2021
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000155735 520__ $$aIn Parkinson's disease with dementia, up to 50% of patients develop a high number of tau-containing neurofibrillary tangles. Tau-based pathologies may thus act synergistically with the α-synuclein pathology to confer a worse prognosis. A better understanding of the relationship between the two distinct pathologies is therefore required. Liquid-liquid phase separation (LLPS) of proteins has recently been shown to be important for protein aggregation involved in amyotrophic lateral sclerosis, whereas tau phase separation has been linked to Alzheimer's disease. We therefore investigated the interaction of α-synuclein with tau and its consequences on tau LLPS. We find α-synuclein to have a low propensity for both, self-coacervation and RNA-mediated LLPS at pH 7.4. However, full-length but not carboxy-terminally truncated α-synuclein efficiently partitions into tau/RNA droplets. We further demonstrate that Cdk2-phosphorylation promotes the concentration of tau into RNA-induced droplets, but at the same time decreases the amount of α-synuclein inside the droplets. NMR spectroscopy reveals that the interaction of the carboxy-terminal domain of α-synuclein with the proline-rich region P2 of tau is required for the recruitment of α-synuclein into tau droplets. The combined data suggest that the concentration of α-synuclein into tau-associated condensates can contribute to synergistic aSyn/tau pathologies.
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000155735 650_7 $$2Other$$aLLPS
000155735 650_7 $$2Other$$aphosphorylation
000155735 650_7 $$2Other$$atau
000155735 650_7 $$2Other$$atruncation
000155735 650_7 $$2Other$$aα-synuclein
000155735 650_2 $$2MeSH$$aAlzheimer Disease: metabolism
000155735 650_2 $$2MeSH$$aAmyotrophic Lateral Sclerosis: metabolism
000155735 650_2 $$2MeSH$$aHumans
000155735 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000155735 650_2 $$2MeSH$$aRecombinant Proteins: isolation & purification
000155735 650_2 $$2MeSH$$aRecombinant Proteins: metabolism
000155735 650_2 $$2MeSH$$aalpha-Synuclein: chemistry
000155735 650_2 $$2MeSH$$aalpha-Synuclein: isolation & purification
000155735 650_2 $$2MeSH$$aalpha-Synuclein: metabolism
000155735 650_2 $$2MeSH$$atau Proteins: chemistry
000155735 650_2 $$2MeSH$$atau Proteins: isolation & purification
000155735 650_2 $$2MeSH$$atau Proteins: metabolism
000155735 7001_ $$0P:(DE-2719)9001085$$aRankovic, Marija$$b1$$udzne
000155735 7001_ $$0P:(DE-2719)2811237$$aFavretto, Filippo$$b2
000155735 7001_ $$0P:(DE-2719)9000315$$aUkmar-Godec, Tina$$b3
000155735 7001_ $$0P:(DE-2719)2812850$$aStrohäker, Timo$$b4
000155735 7001_ $$aBecker, Stefan$$b5
000155735 7001_ $$0P:(DE-2719)2810591$$aZweckstetter, Markus$$b6$$eLast author
000155735 773__ $$0PERI:(DE-600)2000025-X$$a10.1002/pro.4025$$gVol. 30, no. 7, p. 1326 - 1336$$n7$$p1326 - 1336$$tProtein science$$v30$$x1469-896X$$y2021
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