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Why Are Peroxisome Not Considered Part of the Endomembrane System

[Summary]Vesicle (biology and chemistry) Scheme of a liposome formed by phospholipids in an aqueous solution. In cell biology, a vesicle is a small structure within a cell, consisting of fluid enclosed by a lipid bilayer. Vesicles form naturally during the pr


Vesicle (biology and chemistry)

Scheme of a liposome formed by phospholipids in an aqueous solution.

In cell biology, a vesicle is a small structure within a cell, consisting of fluid enclosed by a lipid bilayer. Vesicles form naturally during the processes of secretion (exocytosis), uptake (endocytosis) and transport of materials within the cytoplasm. Alternatively, they may be prepared artificially, in which case they are called liposomes. (Not lysosomes) If there is only one phospholipid bilayer, they are called unilamellar liposome vesicles; otherwise they are called multilamellar. The membrane enclosing the vesicle is also a lamellar phase, similar to that of the plasma membrane and vesicles can fuse with the plasma membrane to release their contents outside the cell. Vesicles can also fuse with other organelles within the cell.

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A type of organelle found in both animal cells and plant cells, a peroxisome is a membrane-bound cellular organelle that contains mostly enzymes . Peroxisomes perform important functions, including lipid metabolism and chemical detoxification. They also carry out oxidation reactions that break down fatty acids and amino acids.

Frontiers | Integration of peroxisomes into an endomembrane system that governs cellular aging | Integrative Physiology


A growing body of evidence implies that, in addition to the well known roles of the peroxisome in housing fatty acid oxidation and maintaining hydrogen peroxide homeostasis (Poirier et al., 2006; Wanders and Waterham, 2006; Schlüter et al., 2010), this organelle is actively involved in organizing the processes of development, differentiation, and morphogenesis in evolutionarily distant organisms. In mammalian and plant cells, the rate of fatty acid metabolism and the efficiency of reactive oxygen species (ROS) and reactive nitrogen species (RNS) turnover within the peroxisome define the dynamics of changes in the levels of signaling lipids, ROS, and RNS outside this organelle (Desvergne and Wahli, 1999; Corpas et al., 2001; del Río et al., 2006; Nyathi and Baker, 2006). Following their release from the peroxisome, these signaling molecules bind and activate a distinct set of transcription factors that respond by causing global changes in gene expression to initiate certain developmental and differentiation programs (Kersten et al., 2000; Desikan et al., 2001; Hu et al., 2002; Ma et al., 2002; Michalik et al., 2002; Baker et al., 2006; del Río et al., 2006; Michalik and Wahli, 2006; Nyathi and Baker, 2006; Bonekamp et al., 2009; Antonenkov et al., 2010; Ivashchenko et al., 2011; Li et al., 2011; Neher et al., 2012). Thus, the peroxisome functions as an intracellular signaling compartment that can orchestrate important developmental decisions from inside the cell by modulating the extra-peroxisomal concentrations of several potent cellular messengers (Titorenko and Rachubinski, 2004; Terlecky and Titorenko, 2009; Thoms et al., 2009; Dixit et al., 2010). Furthermore, the peroxisome can operate as an organizing platform for several developmental and differentiation programs by compartmentalizing the initial steps of plasmalogen biosynthesis in mammalian and nematode cells, providing acetyl-CoA for the biosynthesis of melanin and glycerol in fungal cells, and carrying out the oxidative decomposition of very long-chain fatty acids, phytanic acid, and pristanic acid in mammalian cells (Powers and Moser, 1998; Motley et al., 2000; Thines et al., 2000; Gould et al., 2001; Kimura et al., 2001; Petriv et al., 2002; Wang et al., 2005; Asakura et al., 2006; Terlecky and Titorenko, 2009; Imazaki et al., 2010; Van Veldhoven, 2010; Goh et al., 2011; Mast et al., 2011; Bhadauria et al., 2012). Moreover, while the peroxisome-associated pools of several bifunctional proteins with dual subcellular localization operate in peroxisome biogenesis and function, their pools in other organelles organize certain processes of development, differentiation, and morphogenesis in mammalian, plant, and yeast cells (Titorenko et al., 1997; Titorenko and Rachubinski, 1998, 2004; Lin et al., 1999; Footitt et al., 2002; Gavva et al., 2002; Geuze et al., 2003; Lin et al., 2004; Slabas et al., 2004; Karnik and Trelease, 2005; Ashibe et al., 2007; Freitag et al., 2012). In addition, the peroxisome provides a template for the formation of the Woronin body, a specialized subcellular compartment that in the filamentous fungi Neurospora crassa and Aspergillus oryzae is essential for a multistep process in cell morphogenesis initiated by physical damage to hyphae (Jedd and Chua, 2000; Tenney et al., 2000; Liu et al., 2008; Escaño et al., 2009; Jedd, 2011; Liu et al., 2011). In human cells, the peroxisome can also serve as an intracellular platform for the development of the human immunodeficiency virus and rotavirus (Cohen et al., 2000; Mohan et al., 2002).

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