The cytosolic peroxisome-targeting signal (PTS)-receptors, Pex7p and Pex5pL, are sufficient to transport PTS2 proteins to peroxisomes.


Journal

Biochimica et biophysica acta. Molecular cell research
ISSN: 1879-2596
Titre abrégé: Biochim Biophys Acta Mol Cell Res
Pays: Netherlands
ID NLM: 101731731

Informations de publication

Date de publication:
03 2019
Historique:
received: 15 06 2018
revised: 14 09 2018
accepted: 02 10 2018
pubmed: 9 10 2018
medline: 11 9 2019
entrez: 9 10 2018
Statut: ppublish

Résumé

Proteins harboring peroxisome-targeting signal type-2 (PTS2) are recognized in the cytosol by mobile PTS2 receptor Pex7p and associate with a longer isoform Pex5pL of the PTS1 receptor. Trimeric PTS2 protein-Pex7p-Pex5pL complexes are translocated to peroxisomes in mammalian cells. However, it remains unclear whether Pex5pL and Pex7p are sufficient cytosolic components in transporting of PTS2 proteins to peroxisomes. Here, we construct a semi-intact cell import system to define the cytosolic components required for the peroxisomal PTS2 protein import and show that the PTS2 pre-import complexes comprising Pex7p, Pex5p, and Hsc70 isolated from the cytosol of pex14 Chinese hamster ovary cell mutant ZP161 is import-competent. PTS2 reporter proteins are transported to peroxisomes by recombinant Pex7p and Pex5pL in semi-intact cells devoid of the cytosol. Furthermore, PTS2 proteins are translocated to peroxisomes in the presence of a non-hydrolyzable ATP analogue, adenylyl imidodiphosphate, and N-ethylmaleimide, suggesting that ATP-dependent chaperones including Hsc70 are dispensable for PTS2 protein import. Taken together, we suggest that Pex7p and Pex5pL are the minimal cytosolic factors in the transport of PTS2 proteins to peroxisomes.

Identifiants

pubmed: 30296498
pii: S0167-4889(18)30432-4
doi: 10.1016/j.bbamcr.2018.10.006
pii:
doi:

Substances chimiques

Membrane Proteins 0
Molecular Chaperones 0
PEX5 protein, human 0
Peroxisomal Targeting Signal 2 Receptor 0
Peroxisomal Targeting Signals 0
Peroxisome-Targeting Signal 1 Receptor 0
Protein Isoforms 0
Receptors, Cytoplasmic and Nuclear 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

441-449

Informations de copyright

Copyright © 2018 Elsevier B.V. All rights reserved.

Auteurs

Satoru Mukai (S)

Department of Biology, Faculty of Sciences, Kyushu University, 744 Motooka Nishi-ku, Fukuoka 819-0395, Japan.

Takashi Matsuzaki (T)

Department of Biology, Faculty of Sciences, Kyushu University, 744 Motooka Nishi-ku, Fukuoka 819-0395, Japan.

Yukio Fujiki (Y)

Division of Organelle Homeostasis, Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan. Electronic address: yfujiki@kyudai.jp.

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Classifications MeSH