Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Inherited and Sporadic Amyotrophic Lateral Sclerosis and Fronto-Temporal Lobar Degenerations arising from Pathological Condensates of Phase Separating Proteins.

Literature DB >> 31595953

Inherited and Sporadic Amyotrophic Lateral Sclerosis and Fronto-Temporal Lobar Degenerations arising from Pathological Condensates of Phase Separating Proteins.

Michael Fernandopulle¹, GuoZhen Wang¹, Jonathon Nixon-Abell¹, Seema Qamar¹, Varun Balaji², Ryuta Morihara², Peter H St George-Hyslop^1,2.

Abstract

Recent work on the biophysics of proteins with low complexity, intrinsically disordered domains that have the capacity to form biological condensates has profoundly altered the concepts about the pathogenesis of inherited and sporadic neurodegenerative disorders associated with pathological accumulation of these proteins. In the present review, we use the FUS, TDP-43 and A11 proteins as examples to illustrate how missense mutations and aberrant post-translational modifications of these proteins cause amyotrophic lateral sclerosis (ALS) and fronto-temporal lobar degeneration (FTLD).

Entities: Disease Gene

Keywords: ANXA11; Amyotrophic lateral sclerosis; FUS; TDP-43; biological condensates; fronto-temporal dementia; gelation; hydrogels; local RNA translation; neuronal transport granules; phase separation; stress granules

Mesh：

Substances：

Year: 2019 PMID： 31595953 PMCID： PMC6872449 DOI： 10.1093/hmg/ddz162

Source DB: PubMed Journal: Hum Mol Genet ISSN： 0964-6906 Impact factor: 6.150

122 in total

1. A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation.

Authors: Avinash Patel; Hyun O Lee; Louise Jawerth; Shovamayee Maharana; Marcus Jahnel; Marco Y Hein; Stoyno Stoynov; Julia Mahamid; Shambaditya Saha; Titus M Franzmann; Andrej Pozniakovski; Ina Poser; Nicola Maghelli; Loic A Royer; Martin Weigert; Eugene W Myers; Stephan Grill; David Drechsel; Anthony A Hyman; Simon Alberti
Journal: Cell Date: 2015-08-27 Impact factor: 41.582

Review 2. The epidemiology of ALS: a conspiracy of genes, environment and time.

Authors: Ammar Al-Chalabi; Orla Hardiman
Journal: Nat Rev Neurol Date: 2013-10-15 Impact factor: 42.937

3. ALS-linked mutations enlarge TDP-43-enriched neuronal RNA granules in the dendritic arbor.

Authors: Liqun Liu-Yesucevitz; Amy Y Lin; Atsushi Ebata; Joon Y Boon; Whitney Reid; Ya-Fei Xu; Kendra Kobrin; George J Murphy; Leonard Petrucelli; Benjamin Wolozin
Journal: J Neurosci Date: 2014-03-19 Impact factor: 6.167

4. Citrullination of RGG Motifs in FET Proteins by PAD4 Regulates Protein Aggregation and ALS Susceptibility.

Authors: Chizu Tanikawa; Koji Ueda; Akari Suzuki; Aritoshi Iida; Ryoichi Nakamura; Naoki Atsuta; Genki Tohnai; Gen Sobue; Naomi Saichi; Yukihide Momozawa; Yoichiro Kamatani; Michiaki Kubo; Kazuhiko Yamamoto; Yusuke Nakamura; Koichi Matsuda
Journal: Cell Rep Date: 2018-02-06 Impact factor: 9.423

5. Monomethylated and unmethylated FUS exhibit increased binding to Transportin and distinguish FTLD-FUS from ALS-FUS.

Authors: Marc Suárez-Calvet; Manuela Neumann; Thomas Arzberger; Claudia Abou-Ajram; Eva Funk; Hannelore Hartmann; Dieter Edbauer; Elisabeth Kremmer; Christoph Göbl; Moritz Resch; Benjamin Bourgeois; Tobias Madl; Stefan Reber; Daniel Jutzi; Marc-David Ruepp; Ian R A Mackenzie; Olaf Ansorge; Dorothee Dormann; Christian Haass
Journal: Acta Neuropathol Date: 2016-02-19 Impact factor: 17.088

6. TDP-43 mediates degeneration in a novel Drosophila model of disease caused by mutations in VCP/p97.

Authors: Gillian P Ritson; Sara K Custer; Brian D Freibaum; Jake B Guinto; Dyanna Geffel; Jennifer Moore; Waixing Tang; Matthew J Winton; Manuela Neumann; John Q Trojanowski; Virginia M-Y Lee; Mark S Forman; J Paul Taylor
Journal: J Neurosci Date: 2010-06-02 Impact factor: 6.167

7. ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain.

Authors: Alexander E Conicella; Gül H Zerze; Jeetain Mittal; Nicolas L Fawzi
Journal: Structure Date: 2016-08-18 Impact factor: 5.006

8. Transportin 1 colocalization with Fused in Sarcoma (FUS) inclusions is not characteristic for amyotrophic lateral sclerosis-FUS confirming disrupted nuclear import of mutant FUS and distinguishing it from frontotemporal lobar degeneration with FUS inclusions.

Authors: C Troakes; T Hortobágyi; C Vance; S Al-Sarraj; B Rogelj; C E Shaw
Journal: Neuropathol Appl Neurobiol Date: 2013-08 Impact factor: 8.090

Inherited and Sporadic Amyotrophic Lateral Sclerosis and Fronto-Temporal Lobar Degenerations arising from Pathological Condensates of Phase Separating Proteins.

1. A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation.

Review 2. The epidemiology of ALS: a conspiracy of genes, environment and time.

3. ALS-linked mutations enlarge TDP-43-enriched neuronal RNA granules in the dendritic arbor.

4. Citrullination of RGG Motifs in FET Proteins by PAD4 Regulates Protein Aggregation and ALS Susceptibility.

5. Monomethylated and unmethylated FUS exhibit increased binding to Transportin and distinguish FTLD-FUS from ALS-FUS.

6. TDP-43 mediates degeneration in a novel Drosophila model of disease caused by mutations in VCP/p97.

7. ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain.

8. Transportin 1 colocalization with Fused in Sarcoma (FUS) inclusions is not characteristic for amyotrophic lateral sclerosis-FUS confirming disrupted nuclear import of mutant FUS and distinguishing it from frontotemporal lobar degeneration with FUS inclusions.

9. The RasGAP-associated endoribonuclease G3BP assembles stress granules.

10. RNA phase transitions in repeat expansion disorders.

Review 1. FUS and TDP-43 Phases in Health and Disease.

Review 2. Post-translational Control of RNA-Binding Proteins and Disease-Related Dysregulation.

3. Structure of the ALS Mutation Target Annexin A11 Reveals a Stabilising N-Terminal Segment.