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Compound heterozygous variants in SPG7 identified in 22 French Canadian patients with spastic ataxia.
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CACNA1A and SPG7 are major ataxia genes.
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The results of this study showed that the most frequently detected variant in this cohort was the SPG7 p.Leu78.
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A Norwegian founder mutation p.H701P is a major cause of SPG7 in Norway.
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a novel homozygous frameshift deletion in the SPG7 gene was identifies as the genetic cause of hereditary spastic paraplegia in a Greek family.
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this case shows that the spectrum of pathologies in SPG7 can include neuron loss of the dentate nucleus and the inferior olivary nucleus as well as neuritic pathology.
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Data indicates that SPG7 is essential for the mitochondrial permeability transition pore (PTP) complex formation, interacts with CypD and VDAC and determines C terminus of SPG7 and CsA-binding region of CypD as necessary for PTP formation.
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In unexplained ataxia, there was a significant number of patients with SPG7 mutations.
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The SPG7 Q866 variant is efficiently processed independent of phosphorylation of AFG3L2 at Y179, which inhibits processing of SPG7.
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Using an unbiased exome sequencing approach we identified pathogenic compound heterozygous SPG7 mutations in patients with PEO and multiple mitochondrial DNA deletions in skeletal muscle
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A Japanese patient is reported with an SPG7 mutation for a slowly progressive form of autosomal recessive cerebellar ataxia and spastic paraplegia.
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This study showed that the p.Ala510Val mutation is prevalent amongst severe hereditary spastic paraparesis patients of UK.
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Data suggest a pathogenic role for this SPG7 p.A510V variant.
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SPG7 mutations correlate with spastic paraplegia phenotypes.
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SPG7 mutations are a frequent cause of middle-aged onset of spastic gait when strict inclusion criteria are applied and should, therefore, be tested in autosomal recessive or sporadic hereditary spastic paraplegia.
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Studies indicate that both mouse and human SPG7 ESTs containing alternative first exons.
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The novel mutation is the first splice site mutation found in the SPG7 gene. It removes part of the AAA domain of paraplegin protein, probably leading to a loss-of-function of the paraplegin-AFG3L2 complex in the mitochondrial inner membrane.
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structural analysis of the ATPase domain of the human AAA+ protein paraplegin/SPG7
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mutation in spastin and paraplegin genes does not appear to cause motor neuron disease
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Adenoassociated virus-mediated intramuscular delivery of paraplegin halted the progression of neuropathological changes and rescued mitochondrial morphology in the peripheral nerves of paraplegin-deficient mice.
