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Mutations in the peroxin Pex26p responsible for peroxisome biogenesis disorders of complementation group 8 impair its stability, peroxisomal localization, and interaction with the Pex1p x Pex6p complex.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2006 Jan 20; Vol. 281 (3), pp. 1317-23. Date of Electronic Publication: 2005 Oct 27. - Publication Year :
- 2006
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Abstract
- Peroxisome biogenesis disorders (PBDs) are fatal autosomal recessive diseases and are caused by impaired peroxisome biogenesis. PBDs are genetically heterogeneous and classified into 13 complementation groups (CGs). CG8 is one of the most common groups and has three clinical phenotypes, including Zellweger syndrome (ZS), neonatal adrenoleukodystrophy, and infantile Refsum disease (IRD). We recently isolated PEX26 as the pathogenic gene for PBD of CG8. Pex26p functions in recruiting to peroxisomes the complexes of the AAA ATPase peroxins, Pex1p and Pex6p. In the present work, we identified four distinct mutations in PEX26 from five patients of CG8 PBD including 2 with ZS and 3 with IRD, in addition to 7 mutant alleles in 8 patients in the first report describing the pathogenic PEX26 gene for CG8 PBD. Phenotype-genotype analyses revealed that temperature-sensitive (ts) peroxisome assembly gave rise to a milder IRD in contrast to the non-ts phenotype of the cells from ZS patients. Furthermore, we present several lines of evidence that show that the instability, insufficient binding to Pex1p x Pex6p complexes, or mislocalization of patient-derived Pex26p mutants is most likely responsible for the CG8 PBDs.
- Subjects :
- ATPases Associated with Diverse Cellular Activities
Adrenoleukodystrophy genetics
Cell Line
Female
Genetic Complementation Test
Humans
Male
Molecular Sequence Data
Refsum Disease genetics
Zellweger Syndrome genetics
Adenosine Triphosphatases metabolism
Membrane Proteins genetics
Membrane Proteins metabolism
Mutation
Peroxisomes physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 281
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 16257970
- Full Text :
- https://doi.org/10.1074/jbc.M510044200