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Question: Which are the main features of CREST and other ALS-linked proteins?

Context: Similar to several proteins implicated in ALS, CREST contains a prion-like domain and was reported to be a component of paraspeckles.
Like several other ALS-associated proteins, CREST is recruited to induced stress granules.
CREST and certain other ALS-linked proteins share several features implicated in ALS pathogenesis, namely the ability to aggregate, be recruited to stress granules and alter paraspeckle integrity.
Similar to several proteins implicated in ALS, CREST contains a prion-like domain and was reported to be a component of paraspeckles
Like several other ALS-associated proteins, CREST is recruited to induced stress granules
Our data indicate that CREST and certain other ALS-linked proteins share several features implicated in ALS pathogenesis, namely the ability to aggregate, be recruited to stress granules and alter paraspeckle integrity.
Similar to several proteins implicated in ALS, CREST contains a prion-like domain and was reported to be a component of paraspeckles
Our data indicate that CREST and certain other ALS-linked proteins share several features implicated in ALS pathogenesis, namely the ability to aggregate, be recruited to stress granules and alter paraspeckle integrity. A change in CREST levels in neurons which might occur under pathological conditions would have a profound negative effect on neuronal homeostasis.
Calcium-responsive transactivator (CREST) protein shares a set of structural and functional traits with other proteins associated with amyotrophic lateral sclerosis.
calcium-responsive transactivator (CREST) encoding gene have been recently linked to ALS.
A de novo mutation in the SS18L1 (also known as CREST or KIAA0693) gene encoding the calcium-responsive transactivator and/or neuronal chromatin remodeling complex subunit has recently been identified by exome sequencing of 47 sporadic ALS trios.
Here we report that profilin 1 and related protein profilin 2 are novel stress granule-associated proteins in mouse primary cortical neurons and in human cell lines and that ALS-linked mutations in profilin 1 alter stress granule dynamics, providing further evidence for the potential role of stress granules in ALS pathogenesis
Aggregation of ALS-linked FUS mutant sequesters RNA binding proteins and impairs RNA granules formation
In the present study, we examined the effects of ALS-linked FUS mutants on ALS-associated RNA binding proteins and RNA granules
Aggregation of ALS-linked FUS mutant sequesters RNA binding proteins and impairs RNA granules formation.
CREST and certain other ALS-linked proteins share several features implicated in ALS pathogenesis, namely the ability to aggregate, be recruited to stress granules and alter paraspeckle integrity. Similar to several proteins implicated in ALS, CREST contains a prion-like domain and was reported to be a component of paraspeckles. Like several other ALS-associated proteins, CREST is recruited to induced stress granules. Our data indicate that CREST and certain other ALS-linked proteins share several features implicated in ALS pathogenesis, namely the ability to aggregate, be recruited to stress granules and alter paraspeckle integrity. Like several other ALS-associated proteins, CREST is recruited to induced stress granules.