Protein Misfolding and Disease

Volume 232 of the series Methods in Molecular Biology™ pp 165-173

Study of Mutant Proteins With Folding Defects in Cultured Patient Cells

  • Gabriele DodtAffiliated withPhysiologisch-Chemisches Institut, Eberhard Karls Universität Tübingen
  • , Claudia WalterAffiliated withInstitut für Physiologische Chemie, Ruhr-Universität Bochum

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The example used in this chapter concerns the group of autosomal recessive inherited peroxisome biogenesis disorders (PBDs). These disorders are genetically heterogeneous with at least 12 different complementation groups (CGs). CG 1 is the largest characterized by mutations in HsPEX1, a gene encoding a 143 kD AAA protein (ATPases associated with diverse cellular activities) (13). About 65% of the PBD patients suffering from peroxisome biogenesis disorders harbor mutations in PEX1 (46). Although the function of PEX1 is not defined yet, it is likely that PEX1 plays a significant role in the import of peroxisomal matrix proteins from the cytosol—where they are translated—into the peroxisomes (1,2,7,8).