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Gene Review

PEX12  -  peroxisomal biogenesis factor 12

Homo sapiens

Synonyms: PAF-3, PAF3, PBD3A, Peroxin-12, Peroxisome assembly factor 3, ...
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High impact information on PEX12

  • PEX12 encodes an integral membrane protein of peroxisomes [1].
  • Overexpression of either PEX5 or PEX10 can suppress this PEX12 mutation, providing genetic evidence that these interactions are biologically relevant [2].
  • Using two-hybrid studies, blot overlay assays, and coimmunoprecipitation experiments, we observed that the zinc-binding domain of PEX12 binds both PEX5, the PTS1 receptor, and PEX10, another integral peroxisomal membrane protein required for peroxisomal matrix protein import [2].
  • Mutations in human PEX12 result in Zellweger syndrome, a lethal neurological disorder, and implicate the zinc ring domain in PEX12 function [2].
  • Furthermore, we identified a patient with a missense mutation in the PEX12 zinc-binding domain, S320F, and observed that this mutation reduces the binding of PEX12 to PEX5 and PEX10 [2].

Biological context of PEX12

  • However, one patient who presented relatively mild clinical and cellular phenotypes was a compound heterozygote for two seemingly severe mutations on each PEX12 allele [3].
  • Transfection studies confirmed the expression of similarly sized PEX12 proteins from the PEX12/c.26,27Delta allele [3].
  • A comparison between PEX12 genotypes and the clinical and cellular phenotypes of the corresponding PBD patients suggests a relatively straightforward relationship between genotype and phenotype in this group of the PBDs, such that the loss of PEX12 function leads to more-severe cellular and clinical phenotypes [3].
  • A stable transformant of ZP109 with the PEX12 was morphologically and biochemically restored for peroxisome biogenesis [4].
  • Two unrelated patients of this group manifesting peroxisome deficiency disorders possessed homozygous, inactivating PEX12 mutations: in one, Arg180Thr by one point mutation, and in the other, deletion of two nucleotides in codons for 291Asn and 292Ser, creating an apparently unchanged codon for Asn and a codon 292 for termination [4].

Anatomical context of PEX12

  • The N-terminal region of Pex12p, including amino acid residues at positions 17-76, was required for localization to peroxisomes, while the sequence 17-76 was not sufficient for peroxisomal targeting [5].
  • GFP fusions of T. cruzi PEX10 and L. major PEX12 also localized to glycosomes in T. brucei indicating that glycosomal membrane protein targeting is conserved across trypanosomatids [6].
  • METHODS: Measurement of beta-oxidation enzymes, peroxisomal biochemical analysis in body fluids and cultured skin fibroblasts, and DNA analysis of the PEX12 gene were performed [7].
  • PEX12, the pathogenic gene of group III Zellweger syndrome: cDNA cloning by functional complementation on a CHO cell mutant, patient analysis, and characterization of PEX12p [4].

Physical interactions of PEX12

  • The RING finger of Pex12p bound to Pex10p and the PTS1-receptor Pex5p [5].
  • PEX12 interacts with PEX5 and PEX10 and acts downstream of receptor docking in peroxisomal matrix protein import [2].

Other interactions of PEX12

  • Moreover, Pex12p was co-immunoprecipitated with Pex10p from CHO-K1 cells, where Pex5p was not associated with the Pex12p-Pex10p complex [5].
  • These and other results lead us to propose that PEX12 and PEX10 play direct roles in peroxisomal matrix protein import downstream of the receptor docking event [2].
  • Pex5p carrying the cargos, PTS1 and PTS2, docks with the initial site Pex14p in a putative import machinery, subsequently translocating to other components such as Pex13p, Pex2p, Pex10p and Pex12p, whereby the matrix proteins are imported [8].
  • The authors found that the patient had a peroxisome biogenesis disorder caused by mutations in the PEX12 gene, although all peroxisomal functions in cultured skin fibroblasts were normal [7].


  1. PEX12 encodes an integral membrane protein of peroxisomes. Okumoto, K., Fujiki, Y. Nat. Genet. (1997) [Pubmed]
  2. PEX12 interacts with PEX5 and PEX10 and acts downstream of receptor docking in peroxisomal matrix protein import. Chang, C.C., Warren, D.S., Sacksteder, K.A., Gould, S.J. J. Cell Biol. (1999) [Pubmed]
  3. Phenotype-genotype relationships in complementation group 3 of the peroxisome-biogenesis disorders. Chang, C.C., Gould, S.J. Am. J. Hum. Genet. (1998) [Pubmed]
  4. PEX12, the pathogenic gene of group III Zellweger syndrome: cDNA cloning by functional complementation on a CHO cell mutant, patient analysis, and characterization of PEX12p. Okumoto, K., Shimozawa, N., Kawai, A., Tamura, S., Tsukamoto, T., Osumi, T., Moser, H., Wanders, R.J., Suzuki, Y., Kondo, N., Fujiki, Y. Mol. Cell. Biol. (1998) [Pubmed]
  5. Molecular anatomy of the peroxin Pex12p: ring finger domain is essential for Pex12p function and interacts with the peroxisome-targeting signal type 1-receptor Pex5p and a ring peroxin, Pex10p. Okumoto, K., Abe, I., Fujiki, Y. J. Biol. Chem. (2000) [Pubmed]
  6. Characterization of glycosomal RING finger proteins of trypanosomatids. Saveria, T., Kessler, P., Jensen, B.C., Parsons, M. Exp. Parasitol. (2007) [Pubmed]
  7. Reinvestigation of trihydroxycholestanoic acidemia reveals a peroxisome biogenesis disorder. Gootjes, J., Skovby, F., Christensen, E., Wanders, R.J., Ferdinandusse, S. Neurology (2004) [Pubmed]
  8. Peroxisome biogenesis and peroxisome biogenesis disorders. Fujiki, Y. FEBS Lett. (2000) [Pubmed]
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