Table 1.

Mutations and SG phenotypes for RBPs associated with neurological disorders

Protein	Mutations	Domain	SG phenotype	References
TDP-43	A90V	NLS	Cytoplasmic mis-localization to SGs	[193, 194]
	D169G	RRM1	Decrease Ubiquitination in cytoplasmic and nuclear inclusions	[195, 196]
	K263E	RRM2
	A315T, G335D, M337V, Q343R N345K and R361S	Glycine rich LCD	Promote phase separation; more fibrillar granules	[197–199]
FUS	G156E	PrLD	Increased self-templating capacity, defective RNA binding	[200]
	R244C	Glycine rich LCD	Defective RNA binding	[200]
	R495X	RGG	Increased targeting to SGs	[201]
	H517Q, R521G/C, R522G and P525L	NLS	Cytoplasmic mis-localization and increased accumulation in perinuclear SGs	[201–203]
HNRNPA1	D262V/N, D314V and N267S	PrLD	Increased self-templating capacity	[95, 204, 205]
	F273L, M276L and F281L	NLS (or TPNO-1 binding) domain	Cytoplasmic mis-localization and increased targeting to SGs	[118]
HNRNPA2/B1	D290V	PrLD	Increased amyloidogenic cytoplasmic inclusions	[95]
EWSR1	P522L and G511A	RGG	Increased cytoplasmic localization, Increased self-aggregation	[206, 207]
TAF15	M368T, G391E, R408C and G473E	RGG	Cytoplasmic mis-colalization, increased targeting to SGs	[207, 208]
TIA-1/R	P362L, A381T and E384K	LCD	Increased targeting to SGs	[94]
C9orf72	(G4C2) hexanucleotide expansions in intron 1	N/A	G2C2-RNA repeats and arginine-rich dipeptide repeats promote phase separation and maturation of SGs to amyloid-like inclusions	[59, 164]