title: Interaction between chaperone and protease functions of LON2, and autophagy during the functional transition of peroxisomes.
abstract: Functional transition of glyoxysomes to leaf peroxisomes is observed in greening cotyledons. Glyoxysomal proteins are rapidly degraded and leaf-peroxisomal proteins are transported into peroxisomes after cotyledons are exposed to light, but the molecular mechanisms underlying these processes remain unclear. We recently discovered that two degradation pathways are involved in the functional transition of peroxisomes using Arabidopsis thaliana. Lon protease 2 (LON2) is responsible for the degradation of glyoxysomal proteins inside peroxisomes, and, in parallel, autophagy eliminates damaged or obsolete peroxisomes. A double mutant defective in both the LON2- and autophagy-dependent degradation pathways accumulated glyoxysomal proteins after the cotyledons became green. Our study also demonstrated that the LON2- and autophagy-dependent pathways are interdependent, with the chaperone function of LON2 suppressing autophagic peroxisome degradation. Moreover, the peptidase domain of LON2 interferes with the suppression of autophagy, indicating that autophagy is regulated by intramolecular modulation between the proteolysis and chaperone functions of LON2.
authors.affiliation: Department of Cell Biology; National Institute for Basic Biology; Okazaki, Japan.
authors.forename: Shino
authors.initials: S
authors.lastname: Goto-Yamada
authors.affiliation: Department of Cell Biology; National Institute for Basic Biology; Okazaki, Japan; Department of Basic Biology; School of Life Science; The Graduate University for Advanced Studies; Okazaki, Japan.
authors.forename: Shoji
authors.initials: S
authors.lastname: Mano
authors.affiliation: Department of Applied Biological Chemistry; Niigata University; Niigata, Japan.
authors.forename: Kazusato
authors.initials: K
authors.lastname: Oikawa
authors.affiliation: Department of Cell Biology; National Institute for Basic Biology; Okazaki, Japan; Department of Basic Biology; School of Life Science; The Graduate University for Advanced Studies; Okazaki, Japan.
authors.forename: Michitaro
authors.initials: M
authors.lastname: Shibata
authors.affiliation: Department of Cell Biology; National Institute for Basic Biology; Okazaki, Japan; Department of Basic Biology; School of Life Science; The Graduate University for Advanced Studies; Okazaki, Japan.
authors.forename: Mikio
authors.initials: M
authors.lastname: Nishimura
mesh_terms: D017360:Arabidopsis / Q000201:enzymology*; D029681:Arabidopsis Proteins / Q000378:metabolism*; D001343:Autophagy; D020676:Glyoxysomes / Q000378:metabolism; D053858:Metabolic Networks and Pathways; D008954:Models, Biological; D018832:Molecular Chaperones / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D020675:Peroxisomes / Q000378:metabolism*
chemical_list: D029681:Arabidopsis Proteins; D018832:Molecular Chaperones; D010447:Peptide Hydrolases
keywords: Arabidopsis thaliana; Lon protease; autophagy; chaperone; functional transition; peroxisome
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