The type-2 peroxisomal targeting signal

Kunze, Markus

doi:10.1016/j.bbamcr.2019.118609

Cited by 46 publications

(47 citation statements)

References 203 publications

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“…In contrast, in many fungi the PEX7 co-receptor is a separate PEX protein, namely PEX18, PEX20 or PEX21 (see for more detailed reviews e.g. (Kunze, 2020, Schliebs & Kunau, 2006)). Duplication of the ancestral PEX20 in S. cerevisiae (see figure S4 ), resulted in the partially redundant paralogs PEX18 and PEX21 that perform the same function (Purdue et al, 1998).…”

Section: Resultsmentioning

confidence: 99%

Comparative genomics of peroxisome biogenesis proteins: making sense of the PEX mess

Jansen

Molina

Noort

et al. 2020

Preprint

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PEX genes encode proteins involved in peroxisome biogenesis and proliferation. Using a comparative genomics approach, we clarify the evolutionary relationships between the 37 known PEX proteins in a representative set of eukaryotes, including all common model organisms, pathogenic unicellular eukaryotes and human. A large number of previously unknown PEX orthologs were identified. We analysed all PEX proteins, their conservation and domain architecture and defined the minimum set of PEX proteins that is required to make a peroxisome. The molecular processes in peroxisome biogenesis in different organisms were put into context, showing that peroxisomes are not static organelles in eukaryotic evolution. Organisms that lack peroxisomes still contain a few PEX proteins, which probably play a role in alternative processes. Finally, the relationships between PEX proteins of two large families, the Pex11 and Pex23 families, were clarified, thereby contributing to the understanding of their complicated and sometimes incorrect nomenclature. We provide an exhaustive overview of this important eukaryotic organelle.

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Section: Resultsmentioning

confidence: 99%

Comparative genomics of peroxisome biogenesis proteins: making sense of the PEX mess

Jansen

Molina

Noort

et al. 2020

Preprint

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“…In humans, congenital deficiency in ether lipid biosynthesis evokes the rare, often fatal disease rhizomelic chondrodysplasia punctata (RCDP) ( Berger et al, 2016 ). Genetically, most cases are caused by mutations in peroxin (PEX) 7 (RCDP type 1), coding for a receptor enabling the peroxisomal import of proteins, like ADHAPS, containing a peroxisome targeting signal 2 (PTS2) ( Kunze, 2020 ). Other RCDP subtypes are assigned to mutations in GNPAT (RCDP type 2), AGPS (RCDP type 3), FAR1 (RCDP type 4) or PEX5 (RCDP type 5) affecting the long isoform of PEX5, a protein assisting in PEX7-mediated import.…”

Section: Introductionmentioning

confidence: 99%

Plasmalogens, platelet-activating factor and beyond – Ether lipids in signaling and neurodegeneration

Dorninger

Forss‐Petter

Wimmer

et al. 2020

Neurobiology of Disease

107

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“…A recent study in vivo has shown that differences in affinity for different PTS1 cargos play a critical role in cargo sorting and targeting priority to the peroxisomal matrix 20 . The PTS2 motif is more degenerate and is usually located close to the N‐terminus, but other localizations have also been observed 21,22 . Several cases have been reported where hidden PTS1 and PTS2 motifs may become exposed by splicing or translational read‐through, which provides crucial additional mechanisms of regulated cargo transport and sorting and leads to distributed targeting to peroxisomes and mitochondria or, alternatively, the protein remaining in the cytosol 23‐26 …”

Section: Introductionmentioning

confidence: 99%

“…This review aims to integrate the available data that provide mechanistic insight into the first part of the overall cyclic process—recognition, docking, translocation—and to draw generally applicable conclusions where possible. For further details on the subsequent recycling steps, we refer to recent reviews 2,13,15,18,21,27 …”

Section: Introductionmentioning

confidence: 99%

Versatile allosteric properties in Pex5‐like tetratricopeptide repeat proteins to induce diverse downstream function

Bürgi

Ekal

Wilmanns

2021

Traffic

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Proteins composed of tetratricopeptide repeat (TPR) arrays belong to the α‐solenoid tandem‐repeat family that have unique properties in terms of their overall conformational flexibility and ability to bind to multiple protein ligands. The peroxisomal matrix protein import receptor Pex5 comprises two TPR triplets that recognize protein cargos with a specific C‐terminal Peroxisomal Targeting Signal (PTS) 1 motif. Import of PTS1‐containing protein cargos into peroxisomes through a transient pore is mainly driven by allosteric binding, coupling and release mechanisms, without a need for external energy. A very similar TPR architecture is found in the functionally unrelated TRIP8b, a regulator of the hyperpolarization‐activated cyclic nucleotide‐gated (HCN) ion channel. TRIP8b binds to the HCN ion channel via a C‐terminal sequence motif that is nearly identical to the PTS1 motif of Pex5 receptor cargos. Pex5, Pex5‐related Pex9, and TRIP8b also share a less conserved N‐terminal domain. This domain provides a second protein cargo‐binding site and plays a distinct role in allosteric coupling of initial cargo loading by PTS1 motif‐mediated interactions and different downstream functional readouts. The data reviewed here highlight the overarching role of molecular allostery in driving the diverse functions of TPR array proteins, which could form a model for other α‐solenoid tandem‐repeat proteins involved in translocation processes across membranes.

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The type-2 peroxisomal targeting signal

Cited by 46 publications

References 203 publications

Comparative genomics of peroxisome biogenesis proteins: making sense of the PEX mess

Comparative genomics of peroxisome biogenesis proteins: making sense of the PEX mess

Plasmalogens, platelet-activating factor and beyond – Ether lipids in signaling and neurodegeneration

Versatile allosteric properties in Pex5‐like tetratricopeptide repeat proteins to induce diverse downstream function

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