Abstract
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.
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Barros-Barbosa, A., Rodrigues, T. A., Ferreira, M. J., Pedrosa, A. G., Teixeira, N. R., Francisco, T., & Azevedo, J. E. (2019). The intrinsically disordered nature of the peroxisomal protein translocation machinery. FEBS Journal, 286(1), 24–38. https://doi.org/10.1111/febs.14704
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