Biochemically Distinct Vesicles from the Endoplasmic Reticulum Fuse to Form Peroxisomes

Zand, Adabella van der; Gent, Jürgen; Braakman, Ineke; Tabak, Henk F.

doi:10.1016/j.cell.2012.01.054

Cited by 175 publications

(208 citation statements)

References 54 publications

(58 reference statements)

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“…Past results show that both vesicular and nonvesicular transport of lipids and proteins from the ER are required for proper peroxisomal formation and maintenance (Raychaudhuri and Prinz 2008;Lam et al 2010;Agrawal et al 2011;van der Zand et al 2012). In vitro ER-peroxisome lipid transfer assays also show nonvesicular transport between the membrane compartments; however, the proteins mediating this process remain to be identified (Raychaudhuri and Prinz 2008).…”

Section: Er and Peroxisomesmentioning

confidence: 99%

“…In vitro ER-peroxisome lipid transfer assays also show nonvesicular transport between the membrane compartments; however, the proteins mediating this process remain to be identified (Raychaudhuri and Prinz 2008). Recent live cell image analysis and in vitro cell-free ER budding assays identified a distinct pool of vesicles rich in peroxisomal membrane proteins budding from the ER at peroxisomal ER exit sites, these vesicles then underwent heterotypic fusion with other ER-derived peroxisomal membrane protein vesicles to form a new peroxisome compartment (Agrawal et al 2011;van der Zand et al 2012). The ER-derived peroxisome remains a striking example of the ER's ability to generate an organelle distinct from itself in both morphology and function.…”

Section: Er and Peroxisomesmentioning

confidence: 99%

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Endoplasmic Reticulum Structure and Interconnections with Other Organelles

English

Voeltz

2013

Cold Spring Harbor Perspectives in Biology

286

220

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The endoplasmic reticulum (ER) is a large, continuous membrane-bound organelle comprised of functionally and structurally distinct domains including the nuclear envelope, peripheral tubular ER, peripheral cisternae, and numerous membrane contact sites at the plasma membrane, mitochondria, Golgi, endosomes, and peroxisomes. These domains are required for multiple cellular processes, including synthesis of proteins and lipids, calcium level regulation, and exchange of macromolecules with various organelles at ER-membrane contact sites. The ER maintains its unique overall structure regardless of dynamics or transfer at ER-organelle contacts. In this review, we describe the numerous factors that contribute to the structure of the ER.T he endoplasmic reticulum (ER) is a dynamic organelle responsible for many cellular functions, including the synthesis of proteins and lipids, and regulation of intracellular calcium levels. This review focuses on the distinct and complex morphology of the ER. The structure of the ER is complex because of the numerous distinct domains that exist within one continuous membrane bilayer. These domains are shaped by interactions with the cytoskeleton, by proteins that stabilize membrane shape, and by a homotypic fusion machinery that allows the ER membrane to maintain its continuity and identity. The ER also contains domains that contact the plasma membrane (PM) and other organelles including the Golgi, endosomes, mitochondria, lipid droplets, and peroxisomes. ER contact sites with other organelles and the PM are both abundant and dispersed throughout the cytoplasm, suggesting that they too could influence the overall architecture of the ER. As we will discuss here, ER shape and distribution are regulated by many intrinsic and extrinsic forces. ER STRUCTURE AND FORMATION Domains of the ER Are Stabilized by Membrane-Shaping ProteinsThe endoplasmic reticulum (ER) is a large membrane-bound compartment spread throughout the cytoplasm of eukaryotic cells. It is divided into three major morphologies that include the nuclear envelope (NE), peripheral ER cisternae, and an interconnected tubular network

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Section: Er and Peroxisomesmentioning

confidence: 99%

Section: Er and Peroxisomesmentioning

confidence: 99%

Endoplasmic Reticulum Structure and Interconnections with Other Organelles

English

Voeltz

2013

Cold Spring Harbor Perspectives in Biology

286

220

View full text Add to dashboard Cite

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“…Peroxisomes are generated by two different mechanisms: They can form de novo from the endoplasmic reticulum or by growth and division from pre-existing peroxisomes. The contribution of the two pathways to peroxisome biogenesis is a matter of intensive debate [3][4][5].…”

Section: Introductionmentioning

confidence: 99%

Charcot‐Marie‐Tooth disease‐associated mutants of GDAP1 dissociate its roles in peroxisomal and mitochondrial fission

et al. 2013

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Mitochondria and peroxisomes can be fragmented by the process of fission. The fission machineries of both organelles share a set of proteins. GDAP1 is a tail-anchored protein of mitochondria and induces mitochondrial fragmentation. Mutations in GDAP1 lead to Charcot-Marie-Tooth disease (CMT), an inherited peripheral neuropathy, and affect mitochondrial dynamics. Here, we show that GDAP1 is also targeted to peroxisomes mediated by the import receptor Pex19. Knockdown of GDAP1 leads to peroxisomal elongation that can be rescued by re-expressing GDAP1 and by missense mutated forms found in CMT patients. GDAP1-induced peroxisomal fission is dependent on the integrity of its hydrophobic domain 1, and on Drp1 and Mff, as is mitochondrial fission. Thus, GDAP1 regulates mitochondrial and peroxisomal fission by a similar mechanism. However, our results reveal also a more critical role of the amino-terminal GDAP1 domains, carrying most CMT-causing mutations, in the regulation of mitochondrial compared to peroxisomal fission.

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“…To underscore this notion, a subset of ER resident proteins have emerged as constituents of maturing phagosomes giving rise to a mechanistic basis for antigen cross presentation in innate immunity (Gagnon et al 2002;Houde et al 2003;Cebrian et al 2011;Campbell-Valois et al 2012). The ER also generates peroxisomes (Titorenko et al 1997;Titorenko and Rachubinski 1998;van der Zand et al 2012), and a further specialized subset of ER is found beneath the cell membrane of many cells (English et al 2009). The Golgi apparatus, on the other hand, contributes part of its machinery to lipid droplet biogenesis, revealing a mechanistic link previously thought to be exclusive to that of the ER.…”

Section: Conclusion and Outlooksmentioning

confidence: 99%