Regulation of peroxisomal matrix protein import by ubiquitination

Platta, Harald W.; Brinkmeier, Rebecca; Reidick, Christina; Galiani, Silvia; Clausen, Mathias P.; Eggeling, Christian

doi:10.1016/j.bbamcr.2015.09.010

Cited by 50 publications

(42 citation statements)

References 184 publications

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“…They form a subcomplex within the DTM, as shown by biochemical and genetic studies in yeasts . Also, the RING domains of all three peroxins display ubiquitin‐ligase activity in in vitro assays .…”

Section: The Receptor Recycling Machinerymentioning

confidence: 89%

Protein transport into peroxisomes: Knowns and unknowns

et al. 2017

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Peroxisomal matrix proteins are synthesized on cytosolic ribosomes and rapidly transported into the organelle by a complex machinery. The data gathered in recent years suggest that this machinery operates through a syringe-like mechanism, in which the shuttling receptor PEX5 - the "plunger" - pushes a newly synthesized protein all the way through a peroxisomal transmembrane protein complex - the "barrel" - into the matrix of the organelle. Notably, insertion of cargo-loaded receptor into the "barrel" is an ATP-independent process, whereas extraction of the receptor back into the cytosol requires its monoubiquitination and the action of ATP-dependent mechanoenzymes. Here, we review the main data behind this model.

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Section: The Receptor Recycling Machinerymentioning

confidence: 89%

Protein transport into peroxisomes: Knowns and unknowns

et al. 2017

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“…The machinery that transports these proteins to the peroxisome matrix comprises many different components [4][5][6][7]. Most are exclusively dedicated to this taskthese belong to the so-called peroxin family [8].…”

Section: Introductionmentioning

confidence: 99%

Membrane topologies of PEX13 and PEX14 provide new insights on the mechanism of protein import into peroxisomes

et al. 2018

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PEX13 and PEX14 are two core components of the so‐called peroxisomal docking/translocation module, the transmembrane hydrophilic channel through which newly synthesized peroxisomal proteins are translocated into the organelle matrix. The two proteins interact with each other and with PEX5, the peroxisomal matrix protein shuttling receptor, through relatively well characterized domains. However, the topologies of these membrane proteins are still poorly defined. Here, we subjected proteoliposomes containing PEX13 or PEX14 and purified rat liver peroxisomes to protease‐protection assays and analyzed the protected protein fragments by mass spectrometry, Edman degradation and western blotting using antibodies directed to specific domains of the proteins. Our results indicate that PEX14 is a bona fide intrinsic membrane protein with a Nin‐Cout topology, and that PEX13 adopts a Nout‐Cin topology, thus exposing its carboxy‐terminal Src homology 3 [SH3] domain into the organelle matrix. These results reconcile several enigmatic findings previously reported on PEX13 and PEX14 and provide new insights into the organization of the peroxisomal protein import machinery. Enzymes Trypsin, http://www.chem.qmul.ac.uk/iubmb/enzyme/EC3/4/21/4.html; Proteinase K, http://www.chem.qmul.ac.uk/iubmb/enzyme/EC3/4/21/64.html; Tobacco etch virus protease, http://www.chem.qmul.ac.uk/iubmb/enzyme/EC3/4/22/44.html.

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“…Their specific sorting to this compartment is mediated by a complex machinery comprising a core of 10 evolutionary conserved peroxins (peroxins are proteins specifically involved in peroxisomal biogenesis) plus a set of additional proteins most of which are involved in ubiquitin conjugation and deconjugation ( [8][9][10][11][12][13]; see also Table I in ref. [14], this issue).…”

Section: Introductionmentioning

confidence: 89%

The first minutes in the life of a peroxisomal matrix protein

Dias

Francisco

Rodrigues

et al. 2016

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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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.

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Regulation of peroxisomal matrix protein import by ubiquitination

Cited by 50 publications

References 184 publications

Protein transport into peroxisomes: Knowns and unknowns

Protein transport into peroxisomes: Knowns and unknowns

Membrane topologies of PEX13 and PEX14 provide new insights on the mechanism of protein import into peroxisomes

The first minutes in the life of a peroxisomal matrix protein

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