title: Why do peroxisomes associate with the cytoskeleton?
abstract: Attachment of peroxisomes to cytoskeleton and movement along microtubular filaments and actin cables are essential and highly regulated processes enabling metabolic efficiency, biogenesis, maintenance and inheritance of this dynamic cellular compartment. Several peroxisome-associated proteins have been identified, which mediate interaction with motor proteins, adaptor proteins or other constituents of the cytoskeleton. It appears that there is a species-specific complexity of protein-protein interactions required to control directional movement and arresting. An open question is why some proteins with a specific role in peroxisomal protein import have an additional function in the regulation of cytoskeleton binding and motility of peroxisomes.
authors.affiliation: Max-Planck-Institute of Biophysics, Frankfurt, Germany.
authors.forename: Alexander
authors.initials: A
authors.lastname: Neuhaus
authors.affiliation: MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, Headley Way, OX3 9DS Oxford, United Kingdom.
authors.forename: Christian
authors.initials: C
authors.lastname: Eggeling
authors.affiliation: Department of Systems Biochemistry, Institute of Biochemistry and Pathobiochemistry, Faculty of Medicine, Ruhr-University Bochum, Germany.
authors.forename: Ralf
authors.initials: R
authors.lastname: Erdmann
authors.affiliation: Department of Systems Biochemistry, Institute of Biochemistry and Pathobiochemistry, Faculty of Medicine, Ruhr-University Bochum, Germany. Electronic address: wolfgang.schliebs@rub.de.
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Schliebs
mesh_terms: D008841:Actin Cytoskeleton / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D001692:Biological Transport; D005786:Gene Expression Regulation; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D008870:Microtubules / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D018995:Myosin Heavy Chains / Q000235:genetics / Q000378:metabolism*; D024701:Myosin Type V / Q000235:genetics / Q000378:metabolism*; D001678:Organelle Biogenesis; D000074401:Peroxins; D020675:Peroxisomes / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D018160:Receptors, Cytoplasmic and Nuclear / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction
chemical_list: C510742:INP2 protein, S cerevisiae; C077512:MYO2 protein, S cerevisiae; D008565:Membrane Proteins; C070895:PEX3 protein, S cerevisiae; D000074401:Peroxins; D020033:Protein Isoforms; D018160:Receptors, Cytoplasmic and Nuclear; D029701:Saccharomyces cerevisiae Proteins; D024701:Myosin Type V; D018995:Myosin Heavy Chains
keywords: Actin filaments; Cytoskeleton; Microtubules; Motor proteins; Peroxins; Peroxisome motility