Overexpression of Pex15p, a phosphorylated peroxisomal integral membrane protein required for peroxisome assembly in S.cerevisiae, causes proliferation of the endoplasmic reticulum membrane

Elgersma, Ype; Kwast, L.; Berg, Marlene van den; Snyder, William B.; Distel, Ben; Subramani, Suresh; Tabak, Henk F.

doi:10.1093/emboj/16.24.7326

Cited by 216 publications

(236 citation statements)

References 58 publications

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“…Membrane proliferation has been observed in cells that express high levels of certain integral ER membrane proteins such as the yeast HMG-CoA reductase isozymes, Hmg1p and Hmg2p (Wright et al, 1988;Koning et al, 1996), cytochrome P450 (Schunck et al, 1991), and various domains of the mammalian ribosome receptor, p180 (Wanker et al, 1995;Becker et al, 1999). ER-like membrane morphologies arise from the overexpression of the peroxisomal integral membrane protein, Pex15p (Elgersma et al, 1997). In addition, a yeast strain harboring a temperature-sensitive allele of the Golgi membrane protein, Yip1p, has also been shown to accumulate of ER-like membranes (Yang et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

IN02, A Positive Regulator of Lipid Biosynthesis, Is Essential for the Formation of Inducible Membranes in Yeast

Block-Alper

Webster

Zhou

et al. 2002

MBoC

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Expression of the 180-kDa canine ribosome receptor inSaccharomyces cerevisiae leads to the accumulation of ER-like membranes. Gene expression patterns in strains expressing various forms of p180, each of which gives rise to unique membrane morphologies, were surveyed by microarray analysis. Several genes whose products regulate phospholipid biosynthesis were determined by Northern blotting to be differentially expressed in all strains that undergo membrane proliferation. Of these, the INO2 gene product was found to be essential for formation of p180-inducible membranes. Expression of p180 in ino2Δ cells failed to give rise to the p180-induced membrane proliferation seen in wild-type cells, whereas p180 expression in ino4Δ cells gave rise to membranes indistinguishable from wild type. Thus, Ino2p is required for the formation of p180-induced membranes and, in this case, appears to be functional in the absence of its putative binding partner, Ino4p.

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Section: Introductionmentioning

confidence: 99%

IN02, A Positive Regulator of Lipid Biosynthesis, Is Essential for the Formation of Inducible Membranes in Yeast

Block-Alper

Webster

Zhou

et al. 2002

MBoC

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“…Different consensus sequences for peroxisomal membrane targeting have been proposed (Dyer et al, 1996;Elgersma et al, 1997). This sequence (called mPTS [membrane peroxisomal targeting signal]) seems to be on the lumenal side of membrane proteins, close to a transmembrane sequence, and consists of several positively charged amino acids (Dyer et al, 1996;Elgersma et al, 1997).…”

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confidence: 99%

Pex22p of Pichia pastoris, Essential for Peroxisomal Matrix Protein Import, Anchors the Ubiquitin-conjugating Enzyme, Pex4p, on the Peroxisomal Membrane

Koller¹

1999

The Journal of Cell Biology

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Abstract. We isolated a Pichia pastoris mutant that was unable to grow on the peroxisome-requiring media, methanol and oleate. Cloning the gene by complementation revealed that the encoded protein, Pex22p, is a new peroxin. A ⌬ pex22 strain does not grow on methanol or oleate and is unable to import peroxisomal matrix proteins. However, this strain targets peroxisomal membrane proteins to membranes, most likely peroxisomal remnants, detectable by fluorescence and electron microscopy. Pex22p, composed of 187 amino acids, is an integral peroxisomal membrane protein with its NH 2 terminus in the matrix and its COOH terminus in the cytosol. It contains a 25-amino acid peroxisome membrane-targeting signal at its NH 2 terminus. Pex22p interacts with the ubiquitin-conjugating enzyme Pex4p, a peripheral peroxisomal membrane protein, in vivo, and in a yeast two-hybrid experiment. Pex22p is required for the peroxisomal localization of Pex4p and in strains lacking Pex22p, the Pex4p is cytosolic and unstable. Therefore, Pex22p anchors Pex4p at the peroxisomal membrane. Strains that do not express Pex4p or Pex22p have similar phenotypes and lack Pex5p, suggesting that Pex4p and Pex22p act at the same step in peroxisome biogenesis. The Saccharomyces cerevisiae hypothetical protein, Yaf5p, is the functional homologue of P . pastoris Pex22p.

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“…Two basic pathways of ER proliferation appear to exist in Saccharomyces cerevisiae. Karmellae and karmellae-like membranes are assembled in response to elevated expression of S. cerevisiae Hmg1p, Hmg2p, Pex15p and Pbn1p, as well as expression of mammalian cytochrome b5 and ribosome receptor (Becker et al, 1999;Elgersma et al, 1997;Koning et al, 1996;Naik and Jones, 1998;Vergeres et al, 1993;Wright et al, 1988). ER membrane tubules, distensions or aggregates are assembled in response to elevated expression of S. cerevisiae Sec12p, the Candida maltosa alkaneinducible cytochrome P450s (P450Alk), and a mutant version of the Rhizopus niveus aspartic proteinase I (Dpro) (Nishikawa et al, 1994;Schunck et al, 1991).…”

Section: Discussionmentioning

confidence: 99%

Proliferation of the endoplasmic reticulum occurs normally in cells that lack a functional unfolded protein response

Larson

Parrish

Koning

et al. 2002

Yeast

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Increased expression of certain ER membrane proteins leads to biogenesis of novel ER membrane arrays. These structures provide models in which to explore the mechanisms by which cells control the size and organization of organelles in response to changing physiological demands. In yeast, elevated levels of HMG-CoA reductase induce ER arrays known as karmellae. Cox and co-workers (1997) discovered that karmellae assembly is toxic to ire1 mutants. These mutants are unable to initiate the unfolded protein response, which enables cells to adjust levels of ER chaperones in response to stresses. We sought to determine whether the karmellae-dependent death of ire1 mutants was due to karmellae assembly or to increased levels of HMG-CoA reductase activity. Unexpectedly, we found that ire1 cells could assemble normal levels of karmellae that were structurally identical to those of wild-type cells. In addition, karmellae assembly did not itself induce the unfolded protein response. Certain ire1 strains produced significant numbers of transformants that were unable to utilize galactose as sole carbon source. These results suggest that the karmellaedependent death of certain ire1 strains may simply reflect their inability to grow on galactose.

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Overexpression of Pex15p, a phosphorylated peroxisomal integral membrane protein required for peroxisome assembly in S.cerevisiae, causes proliferation of the endoplasmic reticulum membrane

Abstract: We have cloned PEX15 which is required for peroxisome biogenesis in Saccharomyces cerevisiae.

Cited by 216 publications

References 58 publications

IN02, A Positive Regulator of Lipid Biosynthesis, Is Essential for the Formation of Inducible Membranes in Yeast

IN02, A Positive Regulator of Lipid Biosynthesis, Is Essential for the Formation of Inducible Membranes in Yeast

Pex22p of Pichia pastoris, Essential for Peroxisomal Matrix Protein Import, Anchors the Ubiquitin-conjugating Enzyme, Pex4p, on the Peroxisomal Membrane

Proliferation of the endoplasmic reticulum occurs normally in cells that lack a functional unfolded protein response

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