title: Fission and proliferation of peroxisomes.
abstract: Peroxisomes are remarkably dynamic, multifunctional organelles, which react to physiological changes in their cellular environment and adopt their morphology, number, enzyme content and metabolic functions accordingly. At the organelle level, the key molecular machinery controlling peroxisomal membrane elongation and remodeling as well as membrane fission is becoming increasingly established and defined. Key players in peroxisome division are conserved in animals, plants and fungi, and key fission components are shared with mitochondria. However, the physiological stimuli and corresponding signal transduction pathways regulating and modulating peroxisome maintenance and proliferation are, despite a few exceptions, largely unexplored. There is emerging evidence that peroxisomal dynamics and proper regulation of peroxisome number and morphology are crucial for the physiology of the cell, as well as for the pathology of the organism. Here, we discuss several key aspects of peroxisomal fission and proliferation and highlight their association with certain diseases. We address signaling and transcriptional events resulting in peroxisome proliferation, and focus on novel findings concerning the key division components and their interplay. Finally, we present an updated model of peroxisomal growth and division. This article is part of a Special Issue entitled: Metabolic Functions and Biogenesis of Peroxisomes in Health and Disease.
authors.affiliation: Department of Biology, University of Aveiro, Aveiro, Portugal. mschrader@ua.pt
authors.forename: M
authors.initials: M
authors.lastname: Schrader
authors.forename: N A
authors.initials: NA
authors.lastname: Bonekamp
authors.forename: M
authors.initials: M
authors.lastname: Islinger
mesh_terms: D000818:Animals; D034281:Dynamins; D020558:GTP Phosphohydrolases / Q000172:deficiency / Q000235:genetics; D006801:Humans; D007425:Intracellular Membranes / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000172:deficiency / Q000235:genetics; D063154:Mitochondrial Dynamics; D024101:Mitochondrial Proteins / Q000172:deficiency / Q000235:genetics; D047493:PPAR alpha / Q000502:physiology; D018901:Peroxisomal Disorders / Q000235:genetics / Q000378:metabolism; D020675:Peroxisomes / Q000378:metabolism / Q000502:physiology*; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D008565:Membrane Proteins; D008869:Microtubule-Associated Proteins; D024101:Mitochondrial Proteins; C490455:PEX11A protein, human; C490453:PEX11B protein, human; D047493:PPAR alpha; D020033:Protein Isoforms; D020558:GTP Phosphohydrolases; C110768:DNM1L protein, human; D034281:Dynamins