期刊
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
卷 1863, 期 5, 页码 814-820出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2015.09.025
关键词
Protein translocation; Peroxisome; PEX5; PEX7; PTS1; PTS2
资金
- FCT - Fundacao para a Ciencia e a Tecnologia/MEC - Ministerio da Educacao e Ciencia
- FEDER funds [4293]
- national funds through FCT [FCOMP-01-0124-FEDER-019731 (PTDC/BIABCM/118577/2010)]
- Fundo Europeu de Desenvolvimento Regional (FEDER) through the Operational Competitiveness Programme (COMPETE)
- FCT
- Programa Operational Potential Humano (POPH) do Quadro de Referencia Estrategico Nacional (QREN)
- Fundo Social Europeu (FSE)
- Fundação para a Ciência e a Tecnologia [PTDC/BIA-BCM/118577/2010] Funding Source: FCT
In the field of intracellular protein sorting, peroxisomes are most famous by their capacity to import oligomeric proteins. The data supporting this remarkable property are abundant and, understandably, have inspired a variety of hypothetical models on how newly synthesized (cytosolic) proteins reach the peroxisome matrix. However, there is also accumulating evidence suggesting that many peroxisomal oligomeric proteins actually arrive at the peroxisome still as monomers. In support of this idea, recent data suggest that PEX5, the shuttling receptor for peroxisomal matrix proteins, is also a chaperone/holdase, binding newly synthesized peroxisomal proteins in the cytosol and blocking their oligomerization. Here we review the data behind these two different perspectives and discuss their mechanistic implications on this protein sorting pathway. This article is part of a Special Issue entitled: Peroxisomes edited by Ralf Erdmann. (C) 2015 Elsevier B.V. All rights reserved.
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