The peroxisomal receptor dislocation pathway: To the exportomer and beyond

Platta, Harald W.; Hagen, Stefanie; Reidick, Christina; Erdmann, Ralf

doi:10.1016/j.biochi.2013.12.009

Cited by 56 publications

(44 citation statements)

References 202 publications

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“…This might indicate a dynamic topology throughout the peroxisomal protein import cycle, which has also been reported for the PTS1-receptor Pex5p (Kerssen et al, 2006). Receptor recycling involves monoubiquitylation of Pex5p at a conserved cysteine residue, which contributes to the ATPdependent release of the receptor from the membrane (Platta et al, 2014). This cysteine is conserved in Pex9p (Fig.…”

Section: Discussionsupporting

confidence: 60%

Pex9p is a new yeast peroxisomal import receptor for PTS1-containing proteins

Effelsberg

Cruz-Zaragoza

Schliebs

et al. 2016

Journal of Cell Science

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Peroxisomal proteins carrying a type 1 peroxisomal targeting signal (PTS1) are recognized by the well-conserved cycling import receptor Pex5p. The yeast YMR018W gene encodes a Pex5p paralog and newly identified peroxin that is involved in peroxisomal import of a subset of matrix proteins. The new peroxin was designated Pex9p, and it interacts with the docking protein Pex14p and a subclass of PTS1-containing peroxisomal matrix enzymes. Unlike Pex5p, Pex9p is not expressed in glucose-or ethanol-grown cells, but it is strongly induced by oleate. Under these conditions, Pex9p acts as a cytosolic and membrane-bound peroxisome import receptor for both malate synthase isoenzymes, Mls1p and Mls2p. The inducible Pex9p-dependent import pathway provides a mechanism for the oleate-inducible peroxisomal targeting of malate synthases. The existence of two distinct PTS1 receptors, in addition to two PTS2-dependent import routes, contributes to the adaptive metabolic capacity of peroxisomes in response to environmental changes and underlines the role of peroxisomes as multi-purpose organelles. The identification of different import routes into peroxisomes contributes to the molecular understanding of how regulated protein targeting can alter the function of organelles according to cellular needs.

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Section: Discussionsupporting

confidence: 60%

Pex9p is a new yeast peroxisomal import receptor for PTS1-containing proteins

Effelsberg

Cruz-Zaragoza

Schliebs

et al. 2016

Journal of Cell Science

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“…Yeast Pex4 is tethered to the peroxisomal membrane via interaction with an integral membrane protein Pex22, and similarly AtPEX4/ UBC21 interacts with the Arabidopsis homolog of Pex22, PEX22 (At3g21865) (Zolman et al, 2005). In yeast, three E3 ligases localized to the peroxisomal membrane are required for the monoubiquitination of Pex5, the main protein import machinery, which recycles back to the cytosol for continued import (Platta et al, 2014). Loss-of-function mutants in each of three Arabidopsis E3s with similarity to the yeast E3 proteins, PEX2/TED3 (At1g79810), PEX10 (At2g26350), PEX12 (At3g04460) are embryo lethal, indicating an essential function for these E3s and suggesting that the receptor cycling pathway is present in plants (Hu et al, 2002;Schumann et al, 2003;Sparkes et al, 2003;Fan et al, 2005).…”

Section: Ubiquitin Carrier Proteins (Ubiquitin Conjugating Enzymes Umentioning

confidence: 99%

The Ubiquitination Machinery of the Ubiquitin System

Callis

2014

The Arabidopsis Book

293

269

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The protein ubiquitin is a covalent modifier of proteins, including itself. The ubiquitin system encompasses the enzymes required for catalysing attachment of ubiquitin to substrates as well as proteins that bind to ubiquitinated proteins leading them to their final fate. Also included are activities that remove ubiquitin independent of, or in concert with, proteolysis of the substrate, either by the proteasome or proteases in the vacuole. In addition to ubiquitin encoded by a family of fusion proteins, there are proteins with ubiquitin-like domains, likely forming ubiquitin's β-grasp fold, but incapable of covalent modification. However, they serve as protein-protein interaction platforms within the ubiquitin system. Multi-gene families encode all of these types of activities. Within the ubiquitination machinery "half" of the ubiquitin system are redundant, partially redundant, and unique components affecting diverse developmental and environmental responses in plants. Notably, multiple aspects of biotic and abiotic stress responses require, or are modulated by, ubiquitination. Finally, aspects of the ubiquitin system have broad utility: as components to enhance gene expression or to regulate protein abundance. This review focuses on the ubiquitination machinery: ubiquitin, unique aspects about the synthesis of ubiquitin and organization of its gene family, ubiquitin activating enzymes (E1), ubiquitin conjugating enzymes (E2) and ubiquitin ligases, or E3s. Given the large number of E3s in Arabidopsis this review covers the U box, HECT and RING type E3s, with the exception of the cullin-based E3s.

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“…A comparative overview of the import mechanisms for soluble proteins into different organelles is depicted (Figure 1) and highlights the major steps of protein import. For further details of the import mechanism the readers are referred to excellent reviews that have been published elsewhere [peroxisomes (Hettema et al, 2014;Platta et al, 2014) mitochondria (Chacinska et al, 2009;Schulz et al, 2015); chloroplasts (Li and Chiu, 2010), and ER (Akopian et al, 2013;Johnson et al, 2013b)]. …”

Section: Mechanisms Of Protein Import From the Cytosol Into Endomembrmentioning

confidence: 99%

“…Ubiquitination is exerted by specific machinery involving an ubiquitin conjugating enzyme (UBC, type E2) and a ubiquitin ligase (type E3). In yeast the UBC activity is exerted by Pex4 (Wiebel and Kunau, 1992;Platta et al, 2007) attached to the outer side of the peroxisomal membrane and the ubiquitin ligase activity is performed by the peroxisomal membrane proteins Pex10 and Pex12 (Platta et al, 2009(Platta et al, , 2014. In mammals three homologous cytosolic proteins (UbcH5a-c) exert the UBC activity (Grou et al, 2008), whereas the ubiquitin ligase activity requires the peroxisomal proteins Pex2, Pex10, and Pex12, which might cooperatively exert the ligase activity .…”

Section: Subramanimentioning

confidence: 99%

“…In mammals three homologous cytosolic proteins (UbcH5a-c) exert the UBC activity (Grou et al, 2008), whereas the ubiquitin ligase activity requires the peroxisomal proteins Pex2, Pex10, and Pex12, which might cooperatively exert the ligase activity . The extraction of the mono-ubiquitinated Pex5 is exerted by the receptor extraction module (REM) consisting of a peroxisomal transmembrane protein (Pex26/Pex15) and two members of the AAA-ATPase family (Pex1 and Pex6), which utilize the energy of ATP hydrolysis to extract Pex5 from the membrane (Costa-Rodrigues et al, 2004;Platta et al, 2005) ( Figure 1A) (for review see, Francisco et al, 2014;Platta et al, 2014). Deubiquitination of Pex5 is exerted by deubiquitinating enzymes (Usp9x/Ubp15) (Debelyy et al, 2011;Grou et al, 2012).…”

Section: Subramanimentioning

confidence: 99%

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Molecular Mechanisms and Physiological Significance of Organelle Interactions and Cooperation

2017

Frontiers Research Topics

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The peroxisomal receptor dislocation pathway: To the exportomer and beyond

Cited by 56 publications

References 202 publications

Pex9p is a new yeast peroxisomal import receptor for PTS1-containing proteins

Pex9p is a new yeast peroxisomal import receptor for PTS1-containing proteins

The Ubiquitination Machinery of the Ubiquitin System

Molecular Mechanisms and Physiological Significance of Organelle Interactions and Cooperation

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