Peroxisome Biogenesis Occurs in an Unsynchronized Manner in Close Association with the Endoplasmic Reticulum in Temperature-sensitive<i>Yarrowia lipolytica</i>Pex3p Mutants

Bascom, R.A.; Chan, Honey; Rachubinski, Richard A.

doi:10.1091/mbc.e02-10-0633

Cited by 51 publications

(30 citation statements)

References 46 publications

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“…N.S., not significant; **P,0.01. pex3D cells of Y. lipolytica failed to assemble functional peroxisomes and showed a general mislocalization of peroxisomal matrix proteins to the cytosol (Bascom et al, 2003). We speculate that the elongated fluorescent structures observed in pex11D and pex3D cells expressing genomically integrated POT1-GFP are an artifact of oligomerization of Pot1p-GFP that is mislocalized to the cytosol.…”

Section: Y Lipolytica Pex11 Protein Family Members Are Peroxisomal Imentioning

confidence: 86%

“…The functions of the peroxins Pex3p and Pex19p in these processes are well documented in different eukaryotes (Smith and Aitchison, 2013;Tabak et al, 2013). In Y. lipolytica, pex3D cells lack any peroxisomal structures (Bascom et al, 2003) and pex19D cells, although they do contain morphologically identifiable peroxisomes, mislocalize peroxisomal matrix proteins to the cytosol (Lambkin and Rachubinski, 2001). We assessed the localization of Pex11p-mC, Pex11Cp-mC and Pex11/25p-mC in pex3D and pex19D cells by confocal microscopy.…”

Section: Y Lipolytica Pex11 Protein Family Members Are Peroxisomal Imentioning

confidence: 99%

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An ancestral role in peroxisome assembly is retained by the divisional peroxin Pex11 in the yeast Yarrowia lipolytica

Chang

Klute

Tower

et al. 2015

Journal of Cell Science

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The peroxin Pex11 has a recognized role in peroxisome division. Pex11p remodels and elongates peroxisomal membranes prior to the recruitment of dynamin-related GTPases that act in membrane scission to divide peroxisomes. We performed a comprehensive comparative genomics survey to understand the significance of the evolution of the Pex11 protein family in yeast and other eukaryotes. Pex11p is highly conserved and ancestral, and has undergone numerous lineage-specific duplications, whereas other Pex11 protein family members are fungal-specific innovations. Functional characterization of the in-silico-predicted Pex11 protein family members of the yeast Yarrowia lipolytica, i.e. Pex11p, Pex11Cp and Pex11/25p, demonstrated that Pex11Cp and Pex11/25p have a role in the regulation of peroxisome size and number characteristic of Pex11 protein family members. Unexpectedly, deletion of PEX11 in Y. lipolytica produces cells that lack morphologically identifiable peroxisomes, mislocalize peroxisomal matrix proteins and preferentially degrade peroxisomal membrane proteins, i.e. they exhibit the classical pex mutant phenotype, which has not been observed previously in cells deleted for the PEX11 gene. Our results are consistent with an unprecedented role for Pex11p in de novo peroxisome assembly.

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Section: Y Lipolytica Pex11 Protein Family Members Are Peroxisomal Imentioning

confidence: 86%

Section: Y Lipolytica Pex11 Protein Family Members Are Peroxisomal Imentioning

confidence: 99%

An ancestral role in peroxisome assembly is retained by the divisional peroxin Pex11 in the yeast Yarrowia lipolytica

Chang

Klute

Tower

et al. 2015

Journal of Cell Science

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“…There is certainly increasing data to suggest that there are subdomains of the ER such as specific regions that are continuous with a peroxisomal reticulum from which a major source of peroxisomes can originate (Bascom et al, 2003;Hoepfner et al, 2005), as well as ER subdomains that give rise to lipid droplets (Ozeki et al, 2005;Robenek et al, 2004). In addition there is now increasing evidence to suggest that there are regions of the ER that are in direct contact with the plasma membrane as well as in intimate association with mitochondria (Levine and Rabouille, 2005).…”

Section: Discussionmentioning

confidence: 99%

Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER

Browman

Resek

Zajchowski

et al. 2006

Journal of Cell Science

205

204

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Our laboratory was interested in characterizing the molecular composition of non-caveolar lipid rafts. Thus, we generated monoclonal antibodies to lipid raft proteins of human myelomonocytic cells. Two of these proteins, KE04p and C8orf2, were found to be highly enriched in the detergent-insoluble, buoyant fraction of sucrose gradients in a cholesterol-dependent manner. They contain an evolutionarily conserved domain placing them in the prohibitin family of proteins. In contrast to other family members, these two proteins localized to the ER. Furthermore, the extreme N-termini of KE04p and C8orf2 were found to be sufficient for heterologous targeting of GFP to the ER in the absence of classical ER retrieval motifs. We also demonstrate that all prohibitin family members rely on sequences in their extreme N-termini for their distinctive subcellular distributions including the mitochondria, plasma membrane and Golgi vesicles. Owing to their subcellular localization and their presence in lipid rafts, we have named KE04p and C8orf2, ER lipid raft protein (erlin)-1 and erlin-2, respectively. Interestingly, the ER contains relatively low levels of cholesterol and sphingolipids compared with other organelles. Thus, our data support the existence of lipid-raft-like domains within the membranes of the ER.

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“…In the yeast Yarrowia lipolytica, the peroxisomal membrane proteins Pex2p and Pex16p were shown to traffic through the ER and to acquire core N-linked glycosylation (7). Findings supporting de novo peroxisome biogenesis in close association with the ER were obtained in cells of Y. lipolytica temperature-sensitive for Pex3p function (8), and studies in the plant Arabidopsis showed that peroxisomal ascorbate peroxidase localized to a subdomain of rough ER that could serve as a compartment for posttranslational sorting to peroxisomes (9). In mouse dendritic cells, the peroxisomal membrane proteins Pex13p and PMP70 were found in subdomains of the ER that extended to a peroxisomal reticulum from which mature peroxisome arose (10).…”

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confidence: 95%

Pex3p Initiates the Formation of a Preperoxisomal Compartment from a Subdomain of the Endoplasmic Reticulum in Saccharomyces cerevisiae

Tam¹,

Fagarasanu

et al. 2005

Journal of Biological Chemistry

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151

172

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Peroxisomes are dynamic organelles that often proliferate in response to compounds that they metabolize. Peroxisomes can proliferate by two apparent mechanisms, division of preexisting peroxisomes and de novo synthesis of peroxisomes. Evidence for de novo peroxisome synthesis comes from studies of cells lacking the peroxisomal integral membrane peroxin Pex3p. These cells lack peroxisomes, but peroxisomes can assemble upon reintroduction of Pex3p. The source of these peroxisomes has been the subject of debate. Here, we show that the amino-terminal 46 amino acids of Pex3p of Saccharomyces cerevisiae target to a subdomain of the endoplasmic reticulum and initiate the formation of a preperoxisomal compartment for de novo peroxisome synthesis. In vivo video microscopy showed that this preperoxisomal compartment can import both peroxisomal matrix and membrane proteins leading to the formation of bona fide peroxisomes through the continued activity of full-length Pex3p. Peroxisome formation from the preperoxisomal compartment depends on the activity of the genes PEX14 and PEX19, which are required for the targeting of peroxisomal matrix and membrane proteins, respectively. Our findings support a direct role for the endoplasmic reticulum in de novo peroxisome formation.A characteristic of eukaryotic cells is the presence of seemingly distinct subcellular compartments or organelles possessing specific sets of proteins required for specialized cellular functions. However, organelles do not exist in isolation, and interorganellar communication through the movement and exchange of different molecules is required for normal cell function. This interdependence of organelles extends beyond their biochemical and metabolic roles and necessitates that their biogenesis and turnover also be coordinated.The peroxisome has long been considered an autonomous organelle that proliferates by the growth and division of preexisting peroxisomes (1) and is inherited as a functional organelle at cell division. But what of the concept of de novo peroxisome biogenesis? From an evolutionary point of view, peroxisome proliferation and inheritance could have evolved as a response to a slow and perhaps unreliable mechanism of de novo peroxisome biogenesis. However, de novo peroxisome biogenesis, when combined with peroxisome growth, division, and inheritance, would provide the cell with a fail-safe system for peroxisome maintenance and ultimately for its survival.Evidence implicating the endoplasmic reticulum (ER) 3 in peroxisome biogenesis has accumulated in recent years (reviewed in Refs. 2-4). The amino-terminal 16 amino acids of the peroxisomal integral membrane protein Pex3p of Hansenula polymorpha were shown to be sufficient to target a reporter protein to the ER (5), whereas treatment of cells of this yeast with brefeldin A led to the accumulation of newly synthesized peroxisomal membrane and matrix proteins at the ER (6). In the yeast Yarrowia lipolytica, the peroxisomal membrane proteins Pex2p and Pex16p were shown to traffic through the E...

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Peroxisome Biogenesis Occurs in an Unsynchronized Manner in Close Association with the Endoplasmic Reticulum in Temperature-sensitiveYarrowia lipolyticaPex3p Mutants

Cited by 51 publications

References 46 publications

An ancestral role in peroxisome assembly is retained by the divisional peroxin Pex11 in the yeast Yarrowia lipolytica

An ancestral role in peroxisome assembly is retained by the divisional peroxin Pex11 in the yeast Yarrowia lipolytica

Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER

Pex3p Initiates the Formation of a Preperoxisomal Compartment from a Subdomain of the Endoplasmic Reticulum in Saccharomyces cerevisiae

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