A family of membrane-shaping proteins at ER subdomains regulates pre-peroxisomal vesicle biogenesis

Joshi, Amit; Huang, Xiaofang; Choudhary, Vineet; Levine, Tim P.; Hu, Junjie; Prinz, William A.

doi:10.1083/jcb.201602064

Cited by 77 publications

(133 citation statements)

References 51 publications

(84 reference statements)

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“…Endoplasmic reticulum proteins implicated in the regulation of in vivo peroxisome reintroduction include the reticulon homology domain-containing proteins (RHPs) Rtn1, Rtn2, and Yop1 as well as the ER-localized peroxins Pex29, Pex30, and Pex31. The absence of RHPs speeds up peroxisome formation, pointing to a role of ER architecture in this process [43][44][45]. Conversely, reappearance of peroxisomes is slowed down by the absence of Pex30 or Pex31 [45].…”

Section: Peroxisomal Membrane Structures Do Exist In Yeast Pex3 and Pmentioning

confidence: 99%

“…The absence of RHPs speeds up peroxisome formation, pointing to a role of ER architecture in this process [43][44][45]. Conversely, reappearance of peroxisomes is slowed down by the absence of Pex30 or Pex31 [45]. In vitro vesicle budding assays using permeabilized S. cerevisiae pex19 cells revealed that in the absence of RHPs, Pex29, or Pex30, the release of Pex3 is enhanced [43].…”

Section: Peroxisomal Membrane Structures Do Exist In Yeast Pex3 and Pmentioning

confidence: 99%

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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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Section: Peroxisomal Membrane Structures Do Exist In Yeast Pex3 and Pmentioning

confidence: 99%

Section: Peroxisomal Membrane Structures Do Exist In Yeast Pex3 and Pmentioning

confidence: 99%

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

Jansen

Klei

2019

FEBS Letters

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“…In S. cerevisiae and humans, independent studies suggest that Pex3, and in yeast probably Pex13 and Pex14 as well, insert into the ER, post-translationally via the Sec61 translocon [10–12]. In the same yeast, two ER-resident peroxins, Pex30 and Pex31, contribute to the generation of the pER [13]. In Komagataella phaffii (formerly called Pichia pastoris ), two intra-ER sorting routes to the pER are described [14].…”

Section: Introductionmentioning

confidence: 99%

A New Yeast Peroxin, Pex36, a Functional Homolog of Mammalian PEX16, Functions in the ER-to-Peroxisome Traffic of Peroxisomal Membrane Proteins

Farré

Carolino

Stasyk

et al. 2017

Journal of Molecular Biology

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Peroxisomal membrane proteins (PMPs) traffic to peroxisomes by two mechanisms: direct insertion from the cytosol into the peroxisomal membrane and indirect trafficking to peroxisomes via the endoplasmic reticulum (ER). In mammals and yeast, several PMPs traffic via the ER in a Pex3- and Pex19-dependent manner. In Komagataella phaffii (formerly called Pichia pastoris) specifically, the indirect traffic of Pex2, but not of Pex11 or Pex17, depends on Pex3, but all PMPs tested for indirect trafficking require Pex19. In mammals, the indirect traffic of PMPs also requires PEX16, a protein that is absent in most yeast species. In this study, we isolated PEX36, a new gene in K. phaffii, which encodes a PMP. Pex36 is required for cell growth in conditions that require peroxisomes for the metabolism of certain carbon sources. This growth defect in cells lacking Pex36 can be rescued by the expression of human PEX16, Saccharomyces cerevisiae Pex34, or by overexpression of the endogenous K. phaffii Pex25. Pex36 is not an essential protein for peroxisome proliferation, but in the absence of the functionally redundant protein, Pex25, it becomes essential and less than 20% of these cells show import-incompetent, peroxisome-like structures (peroxisome remnants). In the absence of both proteins, peroxisome biogenesis and the intra-ER sorting of Pex2 and Pex11C are seriously impaired, likely by affecting Pex3 and Pex19 function.

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“…Our goal was to correlate changes in Inp1p's protein interactions with phenotypic changes observed in the inp1 mutant strains. Interactions of Inp1p with the following proteins were systematically queried by yeast 2‐hybrid (Y2H) analysis: Pex3p, which has previously been described as crucial for foci formation and peroxisome tethering; Atg36p, which has been implicated in peroxisome degradation; Pex30p, an integral membrane protein that also interacts with reticulons to regulate peroxisome biogenesis at the ER; Vam6p, a member of the HOPS tethering complex that has recently been implicated in mitochondria‐vacuole tethering; Pex25p, a protein involved in peroxisome division; Cdc3p, a septin that has been implicated as an interaction partner of Inp1p; and Pex17p, a member of the peroxisomal importomer complex that has recently been identified as an Inp1p‐interacting protein . A heat map depicts the strengths of interaction of wild‐type Inp1p and of 14 Inp1p point mutants with these 7 Inp1p interacting proteins in Y2H assays (Figure A).…”

Section: Resultsmentioning

confidence: 99%

Determinants of the assembly, integrity and maintenance of the endoplasmic reticulum‐peroxisome tether

Knoblach

Rachubinski

2019

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Organelle tethering and intercommunication are crucial for proper cell function. We previously described a tether between peroxisomes and the endoplasmic reticulum (ER) that acts in peroxisome population control in the yeast, Saccharomyces cerevisiae. Components of this tether are Pex3p, an integral membrane protein of both peroxisomes and the ER and Inp1p, a connector that links peroxisomes to the ER. Here, we report the analysis of random Inp1p mutants that enabled identification of regions in Inp1p required for the assembly and maintenance of the ER‐peroxisome tether. Interaction analysis between Inp1p mutants and known Inp1p‐binding proteins demonstrated that Pex3p and Inp1p do not constitute the sole components of the ER‐peroxisome tether. Deletion of these Inp1p interactors whose steady‐state localization is outside of ER‐peroxisome tethers affected peroxisome dynamics. Our findings are consistent with the presence of regulatory cues that act on ER‐peroxisome tethers and point to the existence of membrane contact sites between peroxisomes and organelles other than the ER.

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A family of membrane-shaping proteins at ER subdomains regulates pre-peroxisomal vesicle biogenesis

Abstract: Joshi et al. show that Pex30p and Pex31p contain reticulon-like ER tubulating domains. Like reticulons, they localize to the edges of ER sheets and tubules but are only present in subdomains. These subdomains are devoid of reticulons and are the sites of pre-peroxisome vesicle biogenesis.

Cited by 77 publications

References 51 publications

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

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

A New Yeast Peroxin, Pex36, a Functional Homolog of Mammalian PEX16, Functions in the ER-to-Peroxisome Traffic of Peroxisomal Membrane Proteins

Determinants of the assembly, integrity and maintenance of the endoplasmic reticulum‐peroxisome tether

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