4.6 Article

The intrinsically disordered nature of the peroxisomal protein translocation machinery

Journal

FEBS JOURNAL
Volume 286, Issue 1, Pages 24-38

Publisher

WILEY
DOI: 10.1111/febs.14704

Keywords

docking/translocation module; intrinsic disorder; matrix protein import; peroxins; peroxisomes

Funding

  1. FEDER (Fundo Europeu de Desenvolvimento Regional) funds through the COMPETE 2020 - Operacional Programme for Competitiveness and Internationalization (POCI), Portugal 2020
  2. Portuguese funds through FCT (Fundacao para a Ciencia e Tecnologia)/Ministerio da Ciencia, Tecnologia e Inovacao [POCI-01-0145-FEDER-007274, PTDC/BEX-BCM/2311/2014]
  3. Norte Portugal Regional Operational Programme (NORTE 2020), under the PORTUGAL 2020 Partnership Agreement, through the European Regional Development Fund (FEDER) [NORTE-01-0145-FEDER-000008]
  4. Fundacao para a Ciencia e Tecnologia
  5. Programa Operacional Potencial Humano do QREN
  6. Fundo Social Europeu
  7. Fundação para a Ciência e a Tecnologia [PTDC/BEX-BCM/2311/2014] Funding Source: FCT

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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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