title: Identification and functional analysis of Joka2, a tobacco member of the family of selective autophagy cargo receptors.
abstract: Two main mechanisms of protein turnover exist in eukaryotic cells: the ubiquitin-proteasome system and the autophagy-lysosomal pathway. Autophagy is an emerging important constituent of many physiological and pathological processes, such as response to nutrient deficiency, programmed cell death and innate immune response. In mammalian cells the selectivity of autophagy is ensured by the presence of cargo receptors, such as p62/SQSTM1 and NBR1, responsible for sequestration of the ubiquitinated proteins. In plants no selective cargo receptors have been identified yet. The present report indicates that structural and functional homologs of p62 and NBR1 proteins exist in plants. The tobacco protein, named Joka2, has been identified in yeast two-hybrid search as a binding partner of a small coiled-coil protein, a member of UP9/LSU family of unknown function, encoded by the UP9C gene strongly and specifically induced during sulfur deficiency. The typical domains of p62 and NBR1 are conserved in Joka2. Similarly to p62, Joka2-YFP has dual localization (cytosolic speckles and the nucleus); it forms homodimers and interacts with a member of the ATG8 family. Increased expression of Joka2 and ATG8f was observed in roots of tobacco plants grown for two days in nutrient-deficient conditions. Constitutive ectopic expression of Joka2-YFP in tobacco resulted in attenuated response (manifested by lesser yellowing of the leaves) to nutrient deficiency. In conclusion, Joka2, and presumably the process of selective autophagy, might constitute an important part of plant response to environmental stresses.
authors.affiliation: Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
authors.forename: Katarzyna
authors.initials: K
authors.lastname: Zientara-Rytter
authors.forename: Jolanta
authors.initials: J
authors.lastname: Lukomska
authors.forename: Grzegorz
authors.initials: G
authors.lastname: Moniuszko
authors.forename: Rafał
authors.initials: R
authors.lastname: Gwozdecki
authors.forename: Przemysław
authors.initials: P
authors.lastname: Surowiecki
authors.forename: Małgorzata
authors.initials: M
authors.lastname: Lewandowska
authors.forename: Frantz
authors.initials: F
authors.lastname: Liszewska
authors.forename: Anna
authors.initials: A
authors.lastname: Wawrzyńska
authors.forename: Agnieszka
authors.initials: A
authors.lastname: Sirko
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000378:metabolism*; D001343:Autophagy; D000071190:Autophagy-Related Protein 8 Family; D002352:Carrier Proteins / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism; D004777:Environment; D018506:Gene Expression Regulation, Plant; D006801:Humans; D008840:Microfilament Proteins / Q000378:metabolism*; D008856:Microscopy, Fluorescence / Q000379:methods; D009584:Nitrogen / Q000737:chemistry; D018515:Plant Leaves / Q000378:metabolism; D017434:Protein Structure, Tertiary; D018160:Receptors, Cytoplasmic and Nuclear / Q000235:genetics* / Q000502:physiology; D000071456:Sequestosome-1 Protein; D013455:Sulfur / Q000737:chemistry; D014026:Nicotiana / Q000378:metabolism*
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D029681:Arabidopsis Proteins; D000071190:Autophagy-Related Protein 8 Family; D002352:Carrier Proteins; C498698:GABARAPL2 protein, human; D008840:Microfilament Proteins; C568852:NBR1 protein, Arabidopsis; D018160:Receptors, Cytoplasmic and Nuclear; C099718:SQSTM1 protein, human; D000071456:Sequestosome-1 Protein; D013455:Sulfur; D009584:Nitrogen