A New Phase in ALS Research.
In this issue of Structure, Conicella et al. (2016) present evidence that the low complexity C-terminal region of TDP-43 undergoes liquid-liquid phase separation. ALS-associated mutations alter this phase separation process, providing a possible mechanism for the pathology caused by these TDP-43 mutations. The work is strongly supportive of toxic loss of RNA processing function in ALS.
Program in Molecular Structure and Function, Hospital for Sick Children, Toronto, ON M5G 1X8, Canada.
P Andrew
PA
Chong
Program in Molecular Structure and Function, Hospital for Sick Children, Toronto, ON M5G 1X8, Canada; Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada. Electronic address: forman@sickkids.ca.
Julie D
JD
Forman-Kay
D000690:Amyotrophic Lateral Sclerosis / Q000235:genetics*; D004268:DNA-Binding Proteins / Q000737:chemistry*; D009154:Mutation
D004268:DNA-Binding Proteins