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Phase separation of C9orf 72 dipeptide repeats perturbs stress granule dynamics
Published on 2017-07-21660 Views
Neurodegenerative diseases are characterized by the presence of protein inclusion bodies with a different protein content depending on the type of disease. Amyotrophic lateral sclerosis (ALS) and
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Presentation
Mechanisms in C9orf72 linked ALS and FTLD00:00
Understanding the initial steps of ALS00:17
Arginine-rich DPRs perturb nucleocytoplasmic transport00:28
Stress granules in ALS00:55
Stress granules are dynamic compartments01:42
Liquid-liquid phase separation (LLPS)02:04
Arginine-rich DPRs undergo LLPS02:33
PR20 LLPS is dependent on counteranions03:13
PR30 precipitates specific cellular proteins04:13
PR30 precipitates stress granule proteins05:34
PR30 precipitates arginine-rich, disordered and aggregation-prone proteins06:04
PFA crosslinking enriches specific proteins06:43
PR induces stress granules through eIF2α07:33
PR perturbs stress granule dynamics and content09:00
PR promotes liquid-to-solid switch for other ALS proteins09:56
Conclusions10:42
Nucleator alters material state of PR granules - 111:07
Nucleator alters material state of PR granules - 211:40
Acknowledgements12:32