Dynamics of the translocation pore of the human peroxisomal protein import machinery.

Autor:	Ghosh M; Biochemistry Center (BZH), Heidelberg University, D-69120 Heidelberg, Germany.; Institute for Cellular Biochemistry, University Medical Center Göttingen, D-37073 Göttingen, Germany., Denkert N; Biochemistry Center (BZH), Heidelberg University, D-69120 Heidelberg, Germany.; Institute for Cellular Biochemistry, University Medical Center Göttingen, D-37073 Göttingen, Germany., Reuter M; Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, D-44780 Bochum, Germany., Klümper J; Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, D-44780 Bochum, Germany., Reglinski K; Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, D-44780 Bochum, Germany., Peschel R; Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, D-44780 Bochum, Germany., Schliebs W; Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, D-44780 Bochum, Germany., Erdmann R; Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, D-44780 Bochum, Germany., Meinecke M; Biochemistry Center (BZH), Heidelberg University, D-69120 Heidelberg, Germany.; Institute for Cellular Biochemistry, University Medical Center Göttingen, D-37073 Göttingen, Germany.
Jazyk:	angličtina
Zdroj:	Biological chemistry [Biol Chem] 2022 Aug 18; Vol. 404 (2-3), pp. 169-178. Date of Electronic Publication: 2022 Aug 18 (Print Publication: 2023).
DOI:	10.1515/hsz-2022-0170
Abstrakt:	Peroxisomal matrix proteins are synthesized on cytosolic ribosomes and imported in a posttranslational manner. Intricate protein import machineries have evolved that catalyze the different stages of translocation. In humans, PEX5L was found to be an essential component of the peroxisomal translocon. PEX5L is the main receptor for substrate proteins carrying a peroxisomal targeting signal (PTS). Substrates are bound by soluble PEX5L in the cytosol after which the cargo-receptor complex is recruited to peroxisomal membranes. Here, PEX5L interacts with the docking protein PEX14 and becomes part of an integral membrane protein complex that facilitates substrate translocation into the peroxisomal lumen in a still unknown process. In this study, we show that PEX5L containing complexes purified from human peroxisomal membranes constitute water-filled pores when reconstituted into planar-lipid membranes. Channel characteristics were highly dynamic in terms of conductance states, selectivity and voltage- and substrate-sensitivity. Our results show that a PEX5L associated pore exists in human peroxisomes, which can be activated by receptor-cargo complexes. (© 2022 Walter de Gruyter GmbH, Berlin/Boston.)
Databáze:	MEDLINE
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