Please use this identifier to cite or link to this item: https://hdl.handle.net/10216/117913
Author(s): Francisco, T
Rodrigues, TA
Dias, AF
Barros-Barbosa, A
Bicho, D
Azevedo, JE
Title: Protein transport into peroxisomes: Knowns and unknowns
Publisher: Wiley
Issue Date: 2017
Abstract: Peroxisomal matrix proteins are synthesized on cytosolic ribosomes and rapidly transported into the organelle by a complex machinery. The data gathered in recent years suggest that this machinery operates through a syringe-like mechanism, in which the shuttling receptor PEX5 - the “plunger” - pushes a newly synthesized protein all the way through a peroxisomal transmembrane protein complex - the “barrel” - into the matrix of the organelle. Notably, insertion of cargo-loaded receptor into the “barrel” is an ATP-independent process, whereas extraction of the receptor back into the cytosol requires its monoubiquitination and the action of ATP-dependent mechanoenzymes. Here, we review the main data behind this model.
URI: https://repositorio-aberto.up.pt/handle/10216/117913
Source: BioEssays, vol.39(10)
Document Type: Artigo em Revista Científica Internacional
Rights: openAccess
License: https://creativecommons.org/licenses/by-nc/4.0/
Appears in Collections:I3S - Artigo em Revista Científica Internacional

Files in This Item:
File Description SizeFormat 
10.1002 bies.201700047.pdf590.07 kBAdobe PDFThumbnail
View/Open


This item is licensed under a Creative Commons License Creative Commons