The intrinsically disordered nature of the peroxisomal protein translocation machinery

• Published in: The FEBS journal Vol. 286; no. 1; pp. 24 - 38
• Main Authors: Barros‐Barbosa, Aurora, Rodrigues, Tony A., Ferreira, Maria J., Pedrosa, Ana G., Teixeira, Nélson R., Francisco, Tânia, Azevedo, Jorge E.
• Format: Journal Article
• Language: English
• Published: England Blackwell Publishing Ltd 01.01.2019
• Subjects: docking/translocation module; Domains; intrinsic disorder; Machinery and equipment; matrix protein import; Membrane proteins; Metabolites; peroxins; Peroxisomes; Protein transport; Proteins; Translocation; peroxisomes; docking/translocation module; matrix protein import; intrinsic disorder; peroxins
• ISSN: 1742-464X; 1742-4658
• DOI: 10.1111/febs.14704

Despite having a membrane that is impermeable to all but the smallest of metabolites, peroxisomes acquire their newly synthesized (cytosolic) matrix proteins in an already folded conformation. In some cases, even oligomeric proteins have been reported to translocate the organelle membrane. The protein sorting machinery that accomplishes this feat must be rather flexible and, unsurprisingly, several of its key components have large intrinsically disordered domains. Here, we provide an overview on these domains and their interactions trying to infer their functional roles in this protein sorting pathway. In order to translocate a wide range of already folded proteins, the peroxisomal matrix protein import machinery must be flexible. Unsurprisingly, several of its key components have large intrinsically disordered domains. In this review, we provide an overview on these domains and their interactions, trying to infer their functional roles in this protein sorting pathway.