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anti-Human AFG3L2 Antibodies:
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Data report here co-occurrence of a heterozygous de novo AFG3L2 missense mutation (p.R468C) and a maternally inherited heterozygous intragenic deletion of SPG7 in a patient with a complex ataxic and extrapyramidal phenotype with early-onset optic atrophy. Functional analysis in yeast demonstrated the pathogenic role of AFG3L2 p.R468C mutation shedding light on its pathogenic mechanism.
Created are solubilized forms of AFG3L2 to examine the enzyme's substrate specificity mechanisms. The study shows that conserved residues within the presequence of the mitochondrial ribosomal protein, MrpL32, target the subunit to the protease for processing into a mature form. Moreover, these residues can act as a degron, delivering diverse model proteins to AFG3L2 for degradation.
Deletion of AFG3L2 associated with spinocerebellar ataxia type 28 in the context of multiple genomic anomalies.
AOA2 with myoclonus associated with mutations in SETX and AFG3L2
This study that AFG3L2 mutations are another important cause, albeit rare, of a late-onset ataxic PEO phenotype due to a disturbance of mtDNA maintenance.
StAR proteolysis is executed by at least 2 mitochondrial proteases, the matrix LON protease and the inner membrane complexes of the metalloproteases AFG3L2 and AFG3L2:SPG7/paraplegin.
Here, we report on a novel AFG3L2 mutation in a patient with slowly progressive ataxia and a positive family history.
Identification of a partial AFG3L2 deletion and subsequent functional studies reveal loss of function as the most likely disease mechanism.
Both full-length and truncated COX1 proteins physically interact with AFG3L2.
These findings expand the phenotype associated with AFG3L2 mutations and suggest that AFG3L2-related disease should be considered in the differential diagnosis of spastic ataxias.
The mutations of SCA28 are associated with amino acid changes in evolutionarily conserved residues of the alleged SCA28 gene, and indicate SCA28 as the sixth recognized SCA genotype caused by point mutations.
We further confirm both the involvement of AFG3L2 gene in Spinocerebellar ataxia type 28 (SCA28) and the presence of a mutational hotspot in exons 15-16.
in spinocerebellar ataxia type 28 patients study found novel missense mutation at an evolutionarily conserved amino-acid position; amino-acid exchange p.E700K was detected in a 4-generation family and was not observed in chromosomes of controls
work identifies AFG3L2 as a novel cause of dominant neurodegenerative disease and indicates a previously unknown role for this component of the mitochondrial protein quality control machinery in protecting the human cerebellum against neurodegeneration.
An intersubunit signaling network coordinates ATP hydrolysis by m-AAA protease AGG3L2.
total ablation of the m-AAA protease, by deleting both Afg3l2 and its paralogue Afg3l1, triggers progressive motor dysfunction and demyelination, owing to rapid oligodendrocyte cell death
AFG3L2 is critical to the surveillance mechanism that acts as a sensor to couple the synthesis of mitochondrial proteins with organelle fitness, thus ensuring coordinated assembly of the oxidative phosphorylation complexes from two sets of ribosomes.
Reactive oxygen species signaling leads to cytoskeletal modifications that impair mitochondrial transport in neurons lacking AFGL.
defective mitochondrial protein synthesis, leading to early-onset fragmentation of the mitochondrial network, is a central causative factor in AFG3L2-related neurodegeneration.
These findings shed new light in the molecular mechanisms underlining neurodegeneration caused by AFG3L2 mutations.
Data show that Afg3l1 or Afg3l2 are required for maturation of newly imported paraplegin subunits after their cleavage by MPP.
AFG3L2 mutant mouse models display a marked impairment of axonal development with delayed myelination and poor axonal growth.
Spg7 and Afg3l2 double mutants show an early-onset ataxic phenotype, indicating a role of the m-AAA proteases in cerebellar degeneration.
demonstrate that cerebellum is the neuronal tissue with the highest susceptibility to reduced Afg3l2 dosage; propose that the Afg3l2 heterozygous mouse is an excellent model to unravel the pathological cascade leading to spinocerebellar ataxia type 28
This gene encodes a protein localized in mitochondria and closely related to paraplegin. The paraplegin gene is responsible for an autosomal recessive form of hereditary spastic paraplegia. This gene is a candidate gene for other hereditary spastic paraplegias or neurodegenerative disorders.
AFG3 ATPase family gene 3-like 2 (S. cerevisiae)
, AFG3 ATPase family gene 3-like 2
, AFG3 ATPase family gene 3-like 2-like
, AFG3-like protein 2-like
, AFG3-like protein 2
, AFG3-like protein 2 (Paraplegin-like protein)
, ATPase family gene 3, yeast
, paraplegin-like protein