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Spinal muscular atrophy is caused by reduced levels of SMN resulting from the loss of  SMN1  and reliance on  SMN2  for the production of SMN. Loss of SMN entirely is embryonic lethal in mammals. There are several SMN missense mutations found in humans. These alleles do not show partial function in the absence of wild-type SMN and cannot rescue a null  Smn  allele in mice. However, these human SMN missense allele transgenes can rescue a null  Smn  allele when  SMN2  is present. We find that the N- and C-terminal regions constitute two independent domains of SMN that can be separated genetically and undergo intragenic complementation. These SMN protein heteromers restore snRNP assembly of Sm proteins onto snRNA and completely rescue both survival of  Smn  null mice and motor neuron electrophysiology demonstrating that the essential functional unit of SMN is the oligomer.

Intragenic complementation of amino and carboxy terminal SMN missense mutations can rescue Smn null mice