Identification of core components of peroxisomal membrane translocator

2014 Fiscal Year Final Research Report

• Project/Area Number: 24570134
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Structural biochemistry
• Research Institution: Kyushu University
• Principal Investigator: TAMURA Shigehiko 九州大学, 基幹教育院, 教授 (90236753)
• Co-Investigator(Kenkyū-buntansha): FUJIKI Yukio 九州大学, カーボンニュートラル・エネルギー国際研究所, 教授 (70261237)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: ペルオキシソーム / 膜タンパク質複合体 / オルガネラ形成

Outline of Final Research Achievements

The aim of this study is to investigate the molecular mechanism of peroxisome biogenesis. Pex1p and Pex6p are required for the relocation of the import receptor Pex5p from the peroxisomal membrane to the cytosol. We show that mammalian Pex26p directly binds to Pex14p, the initial docking receptor of Pex5p, and interacts with Pex5p via Pex14p. The binding affinity of Pex26p to Pex14p is altered by Pex5p. Further evidence suggests that the N-terminal region in Pex26p acts as a scaffold protein to recruit Pex14p-Pex5p complex together with Pex1p-Pex6p complexes on peroxisomes. Pex26p binding to Pex14p was suppressed by overexpression of Pex1p and Pex6p in an ATP-dependent manner. These results suggested that peroxisome biogenesis requires Pex1p- and Pex6p-regulated dissociation of Pex14p from Pex26p. Taken together, in the peroxisomal protein import, AAA peroxins modulate the interaction between Pex26p and Pex14p on peroxisome membrane.

Free Research Field

分子細胞生物学