Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 117, Issue 52, Pages 33216-33224Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.2009502117
Keywords
peroxisomal import; peroxin; docking complex; peroxisomal translocon; cryoEM
Categories
Funding
- Max Planck Society
- Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) [FOR1905]
- DFG [278002225, RTG 2202, 403222702, SFB 1381, EXC-2189, 390939984]
- Excellence Initiative of the German federal and state governments (BIOSS) [EXC 294]
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Import of yeast peroxisomal matrix proteins is initiated by cytosolic receptors, which specifically recognize and bind the respective cargo proteins. At the peroxisomal membrane, the cargo-loaded receptor interacts with the docking protein Pex14p that is tightly associated with Pex17p. Previous data suggest that this interaction triggers the formation of an import pore for further translocation of the cargo. The mechanistic principles, however, are unclear, mainly because structures of higher-order assemblies are still lacking. Here, using an integrative approach, we provide the structural characterization of the major components of the peroxisomal docking complex Pex14p/Pex17p, in a native bilayer environment, and reveal its subunit organization. Our data show that three copies of Pex14p and a single copy of Pex17p assemble to form a 20-nm rod-like particle. The different subunits are arranged in a parallel manner, showing interactions along their complete sequences and providing receptor binding sites on both membrane sides. The long rod facing the cytosol is mainly formed by the predicted coiled-coil domains of Pex14p and Pex17p, possibly providing the necessary structural support for the formation of the import pore. Further implications of Pex14p/Pex17p for formation of the peroxisomal translocon are discussed.
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