4.5 Article

Isoform-specific domain organization determines conformation and function of the peroxisomal biogenesis factor PEX26

期刊

出版社

ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2018.10.013

关键词

PEX26; Oligomerization; Heptad repeat; Bioluminescence resonance energy transfer (BRET); Peroxisomal biogenesis; Peroxisomal function; Peroxisomal biogenesis disorders (PBD); Zellweger syndrome

资金

  1. Bavarian Genome Research Network
  2. LMUexcellent grant [42595-6]
  3. German Federal Ministry of Education and Research [01EA1307]
  4. Fritz Thyssen Stiftung scholarship

向作者/读者索取更多资源

Peroxisomal biogenesis factor PEX26 is a membrane anchor for the multi-subunit PEX1-PEX6 protein complex that controls ubiquitination and dislocation of PEX5 cargo receptors for peroxisomal matrix protein import. PEX26 associates with the peroxisomal translocation pore via PEX14 and a splice variant (PEX26 Delta ex5) of unknown function has been reported. Here, we demonstrate PEX26 homooligomerization mediated by two heptad repeat domains adjacent to the transmembrane domain. We show that isoform-specific domain organization determines PEX26 oligomerization and impacts peroxisomal beta-oxidation and proliferation. PEX26 and PEX26 Delta ex5 displayed different patterns of interaction with PEX2-PEX10 or PEX13-PEX14 complexes, which relate to distinct pre-peroxisomes in the de novo synthesis pathway. Our data support an alternative PEX14-dependent mechanism of peroxisomal membrane association for the splice variant, which lacks a transmembrane domain. Structure-function relationships of PEX26 isoforms explain an extended function in peroxisomal homeostasis and these findings may improve our understanding of the broad phenotype of PEX26-associated human disorders.

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