Pex8p: An Intraperoxisomal Organizer of the Peroxisomal Import Machinery

Agne, Birgit; Meindl, Nadja M; Niederhoff, Karsten; Einwächter, Henrik; Rehling, Peter; Sickmann, Albert; Meyer, Helmut E.; Girzalsky, Wolfgang; Kunau, Wolf‐H.

doi:10.1016/s1097-2765(03)00062-5

Cited by 223 publications

(276 citation statements)

References 55 publications

(4 reference statements)

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“…2). Also, Pex8 may play a role in the formation of these supercomplexes (Agne et al,2003). Data from Hazra et al (2002) indicate that Pex3 connects these two sub-complexes.…”

Section: Mechanism Of Peroxisome Targeting For Degradationmentioning

confidence: 99%

Autophagy in organelle homeostasis: Peroxisome turnover

Monastyrska

Klionsky

2006

Molecular Aspects of Medicine

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When cells are confronted with an insufficient supply of nutrients in their extracellular fluid, they may begin to cannibalize some of their internal proteins as well as whole organelles for reuse in the synthesis of new components. This process is termed autophagy and it involves the formation of a double-membrane structure within the cell, which encloses the material to be degraded into a vesicle called an autophagosome. The autophagosome subsequently fuses with a lysosome/vacuole whose hydrolytic enzymes degrade the sequestered organelle. Degradation of peroxisomes is a specific type of autophagy, which occurs in a selective manner and has been mostly studied in yeast. Recently, it was reported that a similar selective process of autophagy occurs in mammalian cells with proliferated peroxisomes. Here we discuss characteristics of the autophagy of peroxisomes in mammalian cells and present a comprehensive model of their likely mechanism of degradation on the basis of known and common elements from other systems.

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“…2). Also, Pex8 may play a role in the formation of these supercomplexes (Agne et al,2003). Data from Hazra et al (2002) indicate that Pex3 connects these two sub-complexes.…”

Section: Mechanism Of Peroxisome Targeting For Degradationmentioning

confidence: 99%

Autophagy in organelle homeostasis: Peroxisome turnover

Monastyrska

Klionsky

2006

Molecular Aspects of Medicine

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“…12 peroxins that make up the translocon required for peroxisomal matrix protein import. These peroxins are collectively known as the importomer (Agne et al, 2003;Rayapuram and Subramani, 2006). Import of the matrix proteins can be divided into four stages: initial binding of the receptor to the cargo, docking of the receptor-cargo complex at the peroxisome membrane, membrane translocation of the cargo or receptor-cargo complex with cargo release and, finally, receptor recycling (Brown and Baker, 2008).…”

Section: Import Of Matrix Proteinsmentioning

confidence: 99%

“…The membrane docking complex is comprised of a group of PMPs (peroxisomal membrane proteins); Pex13p and Pex14p (and Pex17p in yeasts) (Agne et al, 2003). The docking complex has been shown to receive the receptor-cargo complex in both PTS1 and PTS2 pathways, thus representing a point of convergence for the two pathways (Rayapuram and Subramani, 2006).…”

Section: Docking Complexmentioning

confidence: 99%

“…These three membrane proteins expose their RING-finger domains to the cis side of the membrane, and mammalian PEX10 and PEX12 have been show to bind to PEX5 by various methods (Chang et al, 1999). The docking complex and the RING-finger subcomplex are linked by Pex3p in P. pastoris (Hazra et al, 2002) or Pex8p in S. cerevisiae (Agne et al, 2003).…”

Section: Receptor Release and Recyclingmentioning

confidence: 99%

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Getting a camel through the eye of a needle: the import of folded proteins by peroxisomes

Lanyon‐Hogg

Warriner

Baker

2010

Biology of the Cell

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Peroxisomes are a family of organelles which have many unusual features. They can arise de novo from the endoplasmic reticulum by a still poorly characterized process, yet possess a unique machinery for the import of their matrix proteins. As peroxisomes lack DNA, their function, which is highly variable and dependent on developmental and/or environmental conditions, is determined by the post-translational import of specific metabolic enzymes in folded or oligomeric states. The two classes of matrix targeting signals for peroxisomal proteins [PTS1 (peroxisomal targeting signal 1) and PTS2] are recognized by cytosolic receptors [PEX5 (peroxin 5) and PEX7 respectively] which escort their cargo proteins to, or possibly across, the peroxisome membrane. Although the membrane translocation mechanism remains unclear, it appears to be driven by thermodynamically favourable binding interactions. Recycling of the receptors from the peroxisome membrane requires ATP hydrolysis for two linked processes: ubiquitination of PEX5 (and the PEX7 co-receptors in yeast) and the function of two peroxisome-associated AAA (ATPase associated with various cellular activities) ATPases, which play a role in recycling or turnover of the ubiquitinated receptors. This review summarizes and integrates recent findings on peroxisome matrix protein import from yeast, plant and mammalian model systems, and discusses some of the gaps in our understanding of this remarkable protein transport system.

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“…We established a new procedure for isolation of subcomplexes from the human peroxisomal membrane for mass spectrometric analyses. For this purpose, we generated stable human cell lines expressing genomically tagged peroxins that are functional and suitable for affinity purification of protein complexes of the peroxisomal protein import machinery, a strategy which has been used successfully for yeast (Agne et al, 2003). Analysis of PEX14-associated proteins revealed tubulin as a major interacting partner of PEX14.…”

Section: Introductionmentioning

confidence: 99%

PEX14 is required for microtubule-based peroxisome motility in human cells

Bharti

Schliebs

Schievelbusch

et al. 2011

Journal of Cell Science

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SummaryWe have established a procedure for isolating native peroxisomal membrane protein complexes from cultured human cells. Protein-A-tagged peroxin 14 (PEX14), a central component of the peroxisomal protein translocation machinery was genomically expressed in Flp-In-293 cells and purified from digitonin-solubilized membranes. Size-exclusion chromatography revealed the existence of distinct multimeric PEX14 assemblies at the peroxisomal membrane. Using mass spectrometric analysis, almost all known human peroxins involved in protein import were identified as constituents of the PEX14 complexes. Unexpectedly, tubulin was discovered to be the major PEX14-associated protein, and direct binding of the proteins was demonstrated. Accordingly, peroxisomal remnants in PEX14-deficient cells have lost their ability to move along microtubules. In vivo and in vitro analyses indicate that the physical binding to tubulin is mediated by the conserved N-terminal domain of PEX14. Thus, human PEX14 is a multi-tasking protein that not only facilitates peroxisomal protein import but is also required for peroxisome motility by serving as membrane anchor for microtubules.

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Pex8p: An Intraperoxisomal Organizer of the Peroxisomal Import Machinery

Cited by 223 publications

References 55 publications

Autophagy in organelle homeostasis: Peroxisome turnover

Autophagy in organelle homeostasis: Peroxisome turnover

Getting a camel through the eye of a needle: the import of folded proteins by peroxisomes

PEX14 is required for microtubule-based peroxisome motility in human cells

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