Protein aggregates into neurons and glial cells are common features of amyotrophic lateral sclerosis (ALS) pathology, and have a key role in ALS initiation and progression: TDP43 proteinopathy is a hallmark of >95% of sporadic/nonmutated ALS.[1,2] Protein degradation machinery and autophagy have a crucial role in dealing with misfolded aggregated proteins.[3] In ALS several genes (UBQLN2, SQSTM1, OPTN, VCP, TBK1) have strong links with protein degradation pathways as their products contribute to recruitment of ubiquitinated proteins to the autophagosome. This evidence concerns the gene SQSTM1 and amyotrophic lateral sclerosis.