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Current genetics, v.66 no.4, 2020년, pp.683 - 687
Li, Jianhui , Hochstrasser, Mark
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J Biol Chem A Adachi 292 19905 2017 10.1074/jbc.M117.817510 Adachi A, Koizumi M, Ohsumi Y (2017) Autophagy induction under carbon starvation conditions is negatively regulated by carbon catabolite repression. J Biol Chem 292:19905-19918. https://doi.org/10.1074/jbc.M117.817510
J Mol Biol L Budenholzer 429 3500 2017 10.1016/j.jmb.2017.05.027 Budenholzer L, Cheng CL, Li Y, Hochstrasser M (2017) Proteasome structure and assembly. J Mol Biol 429:3500-3524. https://doi.org/10.1016/j.jmb.2017.05.027
Eur J Biochem AM Cuervo 227 792 1995 10.1111/j.1432-1033.1995.0792p.x Cuervo AM, Palmer A, Rivett AJ, Knecht E (1995) Degradation of proteasomes by lysosomes in rat liver. Eur J Biochem 227:792-800. https://doi.org/10.1111/j.1432-1033.1995.0792p.x
BBA-Mol Cell Res C Enenkel 1843 39 2014 10.1016/j.bbamcr.2013.03.023 Enenkel C (2014) Proteasome dynamics. BBA-Mol Cell Res 1843:39-46. https://doi.org/10.1016/j.bbamcr.2013.03.023
Curr Genet C Enenkel 64 137 2018 10.1007/s00294-017-0739-y Enenkel C (2018) The paradox of proteasome granules. Curr Genet 64:137-140. https://doi.org/10.1007/s00294-017-0739-y
Curr Genet D Gatica 65 847 2019 10.1007/s00294-019-00943-5 Gatica D, Klionsky DJ (2019) Towards understanding mRNA-binding protein specificity: lessons from post-transcriptional regulation of ATG mRNA during nitrogen starvation-induced autophagy. Curr Genet 65:847-849. https://doi.org/10.1007/s00294-019-00943-5
Nat Cell Biol D Gatica 20 233 2018 10.1038/s41556-018-0037-z Gatica D, Lahiri V, Klionsky DJ (2018) Cargo recognition and degradation by selective autophagy. Nat Cell Biol 20:233-242. https://doi.org/10.1038/s41556-018-0037-z
Cell Syst B Ho 6 192 2018 10.1016/j.cels.2017.12.004 Ho B, Baryshnikova A, Brown GW (2018) Unification of protein abundance datasets yields a quantitative Saccharomyces cerevisiae proteome. Cell Syst 6:192-205.e193. https://doi.org/10.1016/j.cels.2017.12.004
J Biol Chem R Iwama 294 5590 2019 10.1074/jbc.RA118.005698 Iwama R, Ohsumi Y (2019) Analysis of autophagy activated during changes in carbon source availability in yeast cells. J Biol Chem 294:5590-5603. https://doi.org/10.1074/jbc.RA118.005698
Front Mol Biosci O Karmon 2020 10.3389/fmolb.2019.00150 Karmon O, Ben Aroya S (2020) Spatial organization of proteasome aggregates in the regulation of proteasome homeostasis. Front Mol Biosci. https://doi.org/10.3389/fmolb.2019.00150
Curr Genet Z Kuang 64 807 2018 10.1007/s00294-018-0813-0 Kuang Z, Ji H, Boeke JD (2018) Stress response factors drive regrowth of quiescent cells. Curr Genet 64:807-810. https://doi.org/10.1007/s00294-018-0813-0
J Cell Biol D Laporte 181 737 2008 10.1083/jcb.200711154 Laporte D, Salin B, Daignan-Fornier B, Sagot I (2008) Reversible cytoplasmic localization of the proteasome in quiescent yeast cells. J Cell Biol 181:737-745. https://doi.org/10.1083/jcb.200711154
Cell Mol Life Sci W-W Li 69 1125 2012 10.1007/s00018-011-0865-5 Li W-W, Li J, Bao J-K (2012) Microautophagy: lesser-known self-eating. Cell Mol Life Sci 69:1125-1136. https://doi.org/10.1007/s00018-011-0865-5
PLoS Genet J Li 15 e1008387 2019 10.1371/journal.pgen.1008387 Li J, Breker M, Graham M, Schuldiner M, Hochstrasser M (2019) AMPK regulates ESCRT-dependent microautophagy of proteasomes concomitant with proteasome storage granule assembly during glucose starvation. PLoS Genet 15:e1008387. https://doi.org/10.1371/journal.pgen.1008387
ELife RS Marshall 7 e34532 2018 10.7554/eLife.34532 Marshall RS, Vierstra RD (2018) Proteasome storage granules protect proteasomes from autophagic degradation upon carbon starvation. ELife 7:e34532. https://doi.org/10.7554/eLife.34532
Mol Cell RS Marshall 58 1053 2015 10.1016/j.molcel.2015.04.023 Marshall RS, Li F, Gemperline DC, Book AJ, Vierstra RD (2015) Autophagic degradation of the 26S proteasome is mediated by the dual ATG8/ubiquitin receptor RPN10 in Arabidopsis. Mol Cell 58:1053-1066. https://doi.org/10.1016/j.molcel.2015.04.023
Cell Rep RS Marshall 16 1717 2016 10.1016/j.celrep.2016.07.015 Marshall RS, McLoughlin F, Vierstra RD (2016) Autophagic turnover of inactive 26S proteasomes in yeast is directed by the ubiquitin receptor Cue5 and the Hsp42 chaperone. Cell Rep 16:1717-1732. https://doi.org/10.1016/j.celrep.2016.07.015
J Biol Chem AA Nemec 292 21466 2017 10.1074/jbc.M117.817999 Nemec AA, Howell LA, Peterson AK, Murray MA, Tomko RJ (2017) Autophagic clearance of proteasomes in yeast requires the conserved sorting nexin Snx4. J Biol Chem 292:21466-21480. https://doi.org/10.1074/jbc.M117.817999
BioEssays M Oku 40 1800008 2018 10.1002/bies.201800008 Oku M, Sakai Y (2018) Three distinct types of microautophagy based on membrane dynamics and molecular machineries. BioEssays 40:1800008. https://doi.org/10.1002/bies.201800008
J Cell Biol M Oku 216 3263 2017 10.1083/jcb.201611029 Oku M, Maeda Y, Kagohashi Y, Kondo T, Yamada M, Fujimoto T, Sakai Y (2017) Evidence for ESCRT- and clathrin-dependent microautophagy. J Cell Biol 216:3263-3274. https://doi.org/10.1083/jcb.201611029
J Cell Biol LZ Peters 201 663 2013 10.1083/jcb.201211146 Peters LZ, Hazan R, Breker M, Schuldiner M, Ben-Aroya S (2013) Formation and dissociation of proteasome storage granules are regulated by cytosolic pH. J Cell Biol 201:663-671. https://doi.org/10.1083/jcb.201211146
J Cell Sci LZ Peters 129 1190 2016 10.1242/jcs.179648 Peters LZ, Karmon O, Miodownik S, Ben-Aroya S (2016) Proteasome storage granules are transiently associated with the insoluble protein deposit in Saccharomyces cerevisiae. J Cell Sci 129:1190-1197. https://doi.org/10.1242/jcs.179648
PLoS ONE R Saunier 8 e70357 2013 10.1371/journal.pone.0070357 Saunier R, Esposito M, Dassa EP, Delahodde A (2013) Integrity of the Saccharomyces cerevisiae Rpn11 protein is critical for formation of proteasome storage granules (PSG) and survival in stationary phase. PLoS ONE 8:e70357. https://doi.org/10.1371/journal.pone.0070357
EMBO J JA Schäfer 39 e102586 2020 10.15252/embj.2019102586 Schäfer JA, Schessner JP, Bircham PW, Tsuji T, Funaya C, Pajonk O, Schaeff K, Ruffini G, Papagiannidis D, Knop M, Fujimoto T, Schuck S (2020) ESCRT machinery mediates selective microautophagy of endoplasmic reticulum in yeast. EMBO J 39:e102586. https://doi.org/10.15252/embj.2019102586
Curr Genet K Simpson-Lavy 64 785 2018 10.1007/s00294-018-0805-0 Simpson-Lavy K, Kupiec M (2018) A reversible liquid drop aggregation controls glucose response in yeast. Curr Genet 64:785-788. https://doi.org/10.1007/s00294-018-0805-0
J Biol Chem K Tekirdag 293 5414 2018 10.1074/jbc.R117.818237 Tekirdag K, Cuervo AM (2018) Chaperone-mediated autophagy and endosomal microautophagy: jointed by a chaperone. J Biol Chem 293:5414-5424. https://doi.org/10.1074/jbc.R117.818237
Annu Rev Biochem RJ Tomko 82 415 2013 10.1146/annurev-biochem-060410-150257 Tomko RJ, Hochstrasser M (2013) Molecular architecture and assembly of the eukaryotic proteasome. Annu Rev Biochem 82:415-445. https://doi.org/10.1146/annurev-biochem-060410-150257
J Cell Sci S van Deventer 128 109 2015 10.1242/jcs.157354 van Deventer S, Menendez-Benito V, van Leeuwen F, Neefjes J (2015) N-terminal acetylation and replicative age affect proteasome localization and cell fitness during aging. J Cell Sci 128:109-117. https://doi.org/10.1242/jcs.157354
J Biol Chem KA Waite 291 3239 2016 10.1074/jbc.M115.699124 Waite KA, Mota-Peynado AD-L, Vontz G, Roelofs J (2016) Starvation induces proteasome autophagy with different pathways for core and regulatory particles. J Biol Chem 291:3239-3253. https://doi.org/10.1074/jbc.M115.699124
EMBO J MH Weberruss 32 2697 2013 10.1038/emboj.2013.192 Weberruss MH, Savulescu AF, Jando J, Bissinger T, Harel A, Glickman MH, Enenkel C (2013) Blm10 facilitates nuclear import of proteasome core particles. EMBO J 32:2697-2707. https://doi.org/10.1038/emboj.2013.192
J Mol Biol X Wen 428 1681 2016 10.1016/j.jmb.2016.02.021 Wen X, Klionsky DJ (2016) An overview of macroautophagy in yeast. J Mol Biol 428:1681-1699. https://doi.org/10.1016/j.jmb.2016.02.021
Curr Genet B Zhang 2019 10.1007/s00294-019-01016-3 Zhang B, Herman PK (2019) It is all about the process(ing): P-body granules and the regulation of signal transduction. Curr Genet. https://doi.org/10.1007/s00294-019-01016-3
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