期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 288, 期 40, 页码 29151-29159出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M113.487140
关键词
Peroxisomes; Protein Sorting; Protein Translocation; Subcellular Organelles; Ubiquitination; PEX5; PTS1 Protein; In Vitro Import Assays
资金
- Fundo Europeu de Desenvolvimento Regional (FEDER) through the Operational Competitiveness Programme (COMPETE)
- Fundacao para a Ciencia e a Tecnologia (FCT) [FCOMP-01-0124-FEDER-022718 (PEst-C/SAU/LA0002/2011), FCOMP-01-0124-FEDER-007044 (PTDC/BIA-BCM/64771/2006), FCOMP-01-0124-FEDER-019731 (PTDC/BIA-BCM/118577/2010)]
- Fundacao para a Ciencia e a Tecnologia
- Programa Operacional Potencial Humano do Quadro de Referencia Estrategica Nacional (QREN)
- Fundo Social Europeu
- Programa Ciencia
- Programa Operacional Potencial Humano do QREN
- Tipologia 4.2
- Promocao do Emprego Cientifico
- Ministerio da Ciencia, Tecnologia e Ensino Superior
Peroxisomal matrix proteins are synthesized on cytosolic ribosomes and post-translationally targeted to the organelle by PEX5, the peroxisomal shuttling receptor. The pathway followed by PEX5 during this process is known with reasonable detail. After recognizing cargo proteins in the cytosol, the receptor interacts with the peroxisomal docking/translocation machinery, where it gets inserted; PEX5 is then monoubiquitinated, extracted back to the cytosol and, finally, deubiquitinated. However, despite this information, the exact step of this pathway where cargo proteins are translocated across the organelle membrane is still ill-defined. In this work, we used an in vitro import system to characterize the translocation mechanism of a matrix protein possessing a type 1 targeting signal. Our results suggest that translocation of proteins across the organelle membrane occurs downstream of a reversible docking step and upstream of the first cytosolic ATP-dependent step (i.e. before ubiquitination of PEX5), concomitantly with the insertion of the receptor into the docking/translocation machinery.
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