The peroxisomal receptor Pex19p forms a helical mPTS recognition domain

Schueller, Nicole; Holton, Simon J.; Fodor, Krisztián; Milewski, M.; Konarev, Petr V.; Stanley, Will A.; Wolf, Janina; Erdmann, Ralf; Schliebs, Wolfgang; Song, Young Ho; Wilmanns, Matthias

doi:10.1038/emboj.2010.115

Cited by 52 publications

(77 citation statements)

References 41 publications

(71 reference statements)

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“…Similar to PTS1 or PTS2, which target peroxisomal matrix proteins, mPTS is known to target peroxisomal membrane proteins. This mPTS is generally located on one or two TMDs, which correspond to the PEX19 binding site (Halbach et al, 2006;Schueller et al, 2010). Because PEX19 is involved in peroxisomal membrane protein transport, it is considered to act as a receptor or chaperone for peroxisomal membrane proteins (Rottensteiner et al, 2004;Shibata et al, 2004;Schueller et al, 2010).…”

Section: Apem9 Is Localized To the Peroxisomal Membranementioning

confidence: 99%

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ArabidopsisABERRANT PEROXISOME MORPHOLOGY9 Is a Peroxin That Recruits the PEX1-PEX6 Complex to Peroxisomes

et al. 2011

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Peroxisomes have pivotal roles in several metabolic processes, such as the detoxification of H 2 O 2 and b-oxidation of fatty acids, and their functions are tightly regulated by multiple factors involved in peroxisome biogenesis, including protein transport. This study describes the isolation of an embryonic lethal Arabidopsis thaliana mutant, aberrant peroxisome morphology9 (apem9), which is compromised in protein transport into peroxisomes. The APEM9 gene was found to encode an unknown protein. Compared with apem9 having the nucleotide substitution, the knockdown mutants showed severe defects in peroxisomal functions and plant growth. We showed that expression of APEM9 altered PEROXIN6 (PEX6) subcellular localization from the cytosol to peroxisomes. In addition, we showed that PEX1 and PEX6 comprise a heterooligomer and that this complex was recruited to peroxisomal membranes via protein-protein interactions of APEM9 with PEX6. These findings show that APEM9 functions as an anchoring protein, similar to Pex26 in mammals and Pex15p in yeast. Interestingly, however, the identities of amino acids among these anchoring proteins are quite low. These results indicate that although the association of the PEX1-PEX6 complex with peroxisomal membranes is essential for peroxisomal functions, the protein that anchors this complex evolved uniquely in plants.

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Section: Apem9 Is Localized To the Peroxisomal Membranementioning

confidence: 99%

“…Pex19 is reported to be required for targeting of peroxisomal membrane protein transport (Rottensteiner et al, 2004;Shibata et al, 2004;Schueller et al, 2010). In Figure 5K, nYFP-PEX19-1 and cYFP-APEM9 were introduced with a peroxisomal marker, mRFP1-PTS1.…”

Section: Protein-protein Interactions Among Apem9 Pex6 and Pex1mentioning

confidence: 99%

ArabidopsisABERRANT PEROXISOME MORPHOLOGY9 Is a Peroxin That Recruits the PEX1-PEX6 Complex to Peroxisomes

et al. 2011

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“…Interestingly, a helix projecting from the globular C-terminal mPTS-binding domain of human PEX19 (alpha-1 according to ref. 43) also conforms to this pattern ( Fig. 3b-d).…”

Section: Tmd-pex26 Insertion Occurs In the Absence Of Er Membranesmentioning

confidence: 85%

“…1c). The human PEX19 C-terminal domain (amino acids 161-283) is capable of binding immobilized mPTS sequences 43 . We produced the analogous fragment of Neurospora PEX19 (CTD: amino acids 208-327) and found that this domain is also sufficient for chaperone activity (Fig.…”

Section: Resultsmentioning

confidence: 99%

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Hydrophobic handoff for direct delivery of peroxisome tail-anchored proteins

et al. 2014

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Tail-anchored (TA) proteins are inserted into membranes post-translationally through a C-terminal transmembrane domain (TMD). The PEX19 protein binds peroxisome TA proteins in the cytoplasm and delivers them to the membrane through the PEX3 receptor protein. An amphipathic segment in PEX19 promotes docking on PEX3. However, how this leads to substrate insertion is unknown. Here we reconstitute peroxisome TA protein biogenesis into two sequential steps of substrate TMD engagement and membrane insertion. We identify a series of previously uncharacterized amphipathic segments in PEX19 and identify one whose hydrophobicity is required for membrane insertion, but not TMD chaperone activity or PEX3 binding. A membrane-proximal hydrophobic surface of PEX3 promotes an unconventional form of membrane intercalation, and is also required for TMD insertion. Together, these data support a mechanism in which hydrophobic moieties in the TMD chaperone and its membrane-associated receptor act in a concerted manner to prompt TMD release and membrane insertion.

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The peroxisome biogenesis factors Pex3 and Pex19: multitasking proteins with disputed functions

Jansen

Klei

2019

FEBS Letters

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The peroxisomal membrane protein (PMP) Pex3 and its cytosolic interaction partner Pex19 have been implicated in peroxisomal membrane biogenesis. Although these peroxins have been extensively studied, no consensus has been reached yet on how they operate. Here, we discuss two major models of their function, namely, in direct insertion of proteins into the peroxisomal membrane or in formation of PMP‐containing vesicles from the endoplasmic reticulum (ER). Pex3 can also recruit other proteins to the peroxisomal membrane (e.g., Inp1, Atg30, Atg36), thereby fulfilling roles in other processes such as autophagy and organelle retention. Recent studies indicate that Pex3 and Pex19 can also facilitate sorting of certain membrane proteins to other cellular organelles, including the ER, lipid droplets, and mitochondria.

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The peroxisomal receptor Pex19p forms a helical mPTS recognition domain

Cited by 52 publications

References 41 publications

ArabidopsisABERRANT PEROXISOME MORPHOLOGY9 Is a Peroxin That Recruits the PEX1-PEX6 Complex to Peroxisomes

ArabidopsisABERRANT PEROXISOME MORPHOLOGY9 Is a Peroxin That Recruits the PEX1-PEX6 Complex to Peroxisomes

Hydrophobic handoff for direct delivery of peroxisome tail-anchored proteins

The peroxisome biogenesis factors Pex3 and Pex19: multitasking proteins with disputed functions

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