AAA peroxins and their recruiter Pex26p modulate the interactions of peroxins involved in peroxisomal protein import.

Abstract

Pex1p and Pex6p are required for the relocation of the import receptor Pex5p from the peroxisomal membrane to the cytosol. We herein 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, whereas Pex14p was not competed out by Pex1p and Pex6p from Pex26p mutant defective in peroxisomal matrix protein import. These results suggested that peroxisome biogenesis requires Pex1p- and Pex6p-regulated dissociation of Pex14p from Pex26p. Pex1p homo-oligomer directly binds to Pex5p as assessed by a surface plasmon resonance-based assay. Moreover, cytosolic Pex1p is likely to maintain the functional oligomer of Pex5p. Taken together, in the peroxisomal protein import, AAA peroxins modulate the interaction between Pex26p and Pex14p on peroxisome membrane as well as Pex5p oligomer in the cytosol.

DOI: 10.1074/jbc.M114.588038
01020201520162017
Citations per Year

Citation Velocity: 7

Averaging 7 citations per year over the last 3 years.

Learn more about how we calculate this metric in our FAQ.

Cite this paper

@article{Tamura2014AAAPA, title={AAA peroxins and their recruiter Pex26p modulate the interactions of peroxins involved in peroxisomal protein import.}, author={Shigehiko Tamura and Naomi Matsumoto and Ryota Takeba and Yukio Fujiki}, journal={The Journal of biological chemistry}, year={2014}, volume={289 35}, pages={24336-46} }