ABSTRACT
Glycine-rich regions form intrinsically unstructured domains within RNA-binding proteins. Although they lack a defined structure when alone in solution, these domains can form more defined structural elements when interacting with other proteins or with RNA. TDP-43 and FUS are RN A binding proteins with glycine-rich domains that form abnormal aggregates in amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD ). The vast majority o f mutations in familial A LS occur within the glycine-rich domain o f TDP-43 as do about a third o f FUS mutations. This chapter will review the various functions o f some o f the best characterised glycine-rich domains in RNA-binding proteins. Furthermore, the chapter will discuss how these findings inform on the possible functions o f glycine-rich domains in TDP-43 and FUS.
