气候变化领域集成服务门户(CCPortal): Towards the molecular architecture of the peroxisomal receptor docking complex

CCPortal

DOI	10.1073/PNAS.2009502117
	Towards the molecular architecture of the peroxisomal receptor docking complex
	Lill P.; Hansen T.; Wendscheck D.; Klink B.U.; Jeziorek T.; Vismpas D.; Miehling J.; Bender J.; Schummer A.; Drepper F.; Girzalsky W.; Warscheid B.; Erdmann R.; Gatsogiannis C.
发表日期	2021
ISSN	00278424
起始页码	33216
结束页码	33224
卷号	117 期号:52
英文摘要	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. © 2020 National Academy of Sciences. All rights reserved.
英文关键词	CryoEM; Docking complex; Peroxin; Peroxisomal import; Peroxisomal translocon
语种	英语
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/179609
作者单位	Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, 44227, Germany; Institute of Biochemistry and Pathobiochemistry, Faculty of Medicine, System Biochemistry, Ruhr University Bochum, Bochum, 44801, Germany; Biochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology, University of Freiburg, Freiburg, 79104, Germany; Signalling Research Centres BIOSS and CIBSS, University of Freiburg, Freiburg, 79104, Germany; Institute for Medical Physics and Biophysics, Center for Soft Nanoscience, Westfälische Wilhelms Universität Münster, Münster, 48149, Germany; Interdisciplinary Research Center HALOmem, Institute for Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Halle (Saale), 06120, Germany; Protagen Protein Services GmbH, Heilbronn, 74076, Germany
推荐引用方式 GB/T 7714	Lill P.,Hansen T.,Wendscheck D.,et al. Towards the molecular architecture of the peroxisomal receptor docking complex[J],2021,117(52).
APA	Lill P..,Hansen T..,Wendscheck D..,Klink B.U..,Jeziorek T..,...&Gatsogiannis C..(2021).Towards the molecular architecture of the peroxisomal receptor docking complex.Proceedings of the National Academy of Sciences of the United States of America,117(52).
MLA	Lill P.,et al."Towards the molecular architecture of the peroxisomal receptor docking complex".Proceedings of the National Academy of Sciences of the United States of America 117.52(2021).