The ATP13A2 gene mutations associated with KRS are truncated forms and cause protein instability with loss-of-function.[1] The truncated mutation causes mislocalization of ATP13A2 to the endoplasmic reticulum where the proteasome degrades it through the ER-associated degradation (ERAD) pathway.[9] Heterozygous and homozygous missense mutations in ATP13A2 are linked to early-onset parkinsonism.[9] Compound heterozygous and homozygous mutations in KRS subjects in families from China, Jordan, Pakistan Chile, and Afghanistan, which cause splicing variants or frameshift mutations that truncate ATP13A2.[9] Mutations in the ATP13A2 gene have also been associated with hereditary spastic paraplegia, uncomplicated early - or late-onset parkinsonism and neuronal ceroid lipofuscinosis.[12]