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Title: The intrinsically disordered nature of the peroxisomal protein translocation machinery

Journal Article · · Federation of European Biochemical Societies (FEBS) Journal
DOI: https://doi.org/10.1111/febs.14704 · OSTI ID:1484307
 [1];  [1];  [1];  [1];  [1];  [1];  [1]
  1. Instituto de Investigação e Inovação em Saúde (i3S) Universidade do Porto Portugal, Instituto de Biologia Molecular e Celular (IBMC) Universidade do Porto Portugal, Instituto de Ciências Biomédicas de Abel Salazar (ICBAS) Universidade do Porto Portugal

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.

Sponsoring Organization:
USDOE
OSTI ID:
1484307
Journal Information:
Federation of European Biochemical Societies (FEBS) Journal, Journal Name: Federation of European Biochemical Societies (FEBS) Journal Journal Issue: 1 Vol. 286; ISSN 1742-464X
Publisher:
Wiley-BlackwellCopyright Statement
Country of Publication:
United Kingdom
Language:
English

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