Hitchhiking vesicular transport routes to the vacuole: Amyloid recruitment to the Insoluble Protein Deposit (IPOD)

REFERENCES

• Kumar R, Nawroth PP, Tyedmers J. Prion aggregates are recruited to the insoluble protein deposit (IPOD) via myosin 2-based vesicular transport. PLoS Genet 2016; 12:e1006324; PMID:27689885; http://dx.doi.org/10.1371/journal.pgen.1006324
   PubMed Web of Science ®Google Scholar
• Hill SM, Hao X, Gronvall J, Spikings-Nordby S, Widlund PO, Amen T, Jörhov A, Josefson R, Kaganovich D, Liu B, et al. Asymmetric inheritance of aggregated proteins and age reset in yeast are regulated by Vac17-dependent vacuolar functions. Cell Rep 2016; 16:826-38; PMID:27373154
   PubMed Web of Science ®Google Scholar
• Kaganovich D, Kopito R, Frydman J. Misfolded proteins partition between two distinct quality control compartments. Nature 2008; 454:1088-95; PMID:18756251; http://dx.doi.org/10.1038/nature07195
   PubMed Web of Science ®Google Scholar
• Miller SB, Ho CT, Winkler J, Khokhrina M, Neuner A, Mohamed MY, Guilbride DL, Richter K, Lisby M, Schiebel E, et al. Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition. EMBO J 2015; 34:778-97; PMID:25672362; http://dx.doi.org/10.15252/embj.201489524
   PubMed Web of Science ®Google Scholar
• Gallina I, Colding C, Henriksen P, Beli P, Nakamura K, Offman J, Mathiasen DP, Silva S, Hoffmann E, Groth A, et al. Cmr1/WDR76 defines a nuclear genotoxic stress body linking genome integrity and protein quality control. Nat Commun 2015; 6:6533; PMID:25817432; http://dx.doi.org/10.1038/ncomms7533
   PubMed Web of Science ®Google Scholar
• Escusa-Toret S, Vonk WI, Frydman J. Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress. Nat Cell Biol 2013; 15:1231-43; PMID:24036477; http://dx.doi.org/10.1038/ncb2838
   PubMed Web of Science ®Google Scholar
• Specht S, Miller SB, Mogk A, Bukau B. Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae. J Cell Biol 2011; 195:617-29; PMID:22065637; http://dx.doi.org/10.1083/jcb.201106037
   PubMed Web of Science ®Google Scholar
• Spokoini R, Moldavski O, Nahmias Y, England JL, Schuldiner M, Kaganovich D. Confinement to organelle-associated inclusion structures mediates asymmetric inheritance of aggregated protein in budding yeast. Cell Rep 2012; 2:738-47; PMID:23022486; http://dx.doi.org/10.1016/j.celrep.2012.08.024
   PubMed Web of Science ®Google Scholar
• Tyedmers J, Treusch S, Dong J, McCaffery JM, Bevis B, Lindquist S. Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation. Proc Natl Acad Sci U S A 2010; 107:8633-8; PMID:20421488; http://dx.doi.org/10.1073/pnas.1003895107
   PubMed Web of Science ®Google Scholar
• Peters LZ, Karmon O, David-Kadoch G, Hazan R, Yu T, Glickman MH, Ben-Aroya S. The protein quality control machinery regulates its misassembled proteasome subunits. PLoS Genet 2015; 11:e1005178; PMID:25919710; http://dx.doi.org/10.1371/journal.pgen.1005178
   PubMedGoogle Scholar
• Peters LZ, Karmon O, Miodownik S, Ben-Aroya S. Proteasome storage granules are transiently associated with the insoluble protein deposit in Saccharomyces cerevisiae. J Cell Sci 2016; 129:1190-7; PMID:26826189; http://dx.doi.org/10.1242/jcs.179648
   PubMed Web of Science ®Google Scholar
• Marshall RS, McLoughlin F, Vierstra RD. Autophagic turnover of inactive 26s proteasomes in yeast is directed by the ubiquitin receptor Cue5 and the Hsp42 chaperone. Cell Rep 2016; 16:1717-32; PMID:27477278; http://dx.doi.org/10.1016/j.celrep.2016.07.015
   PubMed Web of Science ®Google Scholar
• Malinovska L, Kroschwald S, Munder MC, Richter D, Alberti S. Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates. Mol Biol Cell 2012; 23:3041-56; PMID:22718905; http://dx.doi.org/10.1091/mbc.E12-03-0194
   PubMed Web of Science ®Google Scholar
• Park SH, Kukushkin Y, Gupta R, Chen T, Konagai A, Hipp MS, Hayer-Hartl M, Hartl FU. PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone. Cell 2013; 154:134-45; PMID:23791384; http://dx.doi.org/10.1016/j.cell.2013.06.003
   PubMed Web of Science ®Google Scholar
• Ganusova EE, Ozolins LN, Bhagat S, Newnam GP, Wegrzyn RD, Sherman MY, Chernoff YO. Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast. Mol Cell Biol 2006; 26:617-29; PMID:16382152; http://dx.doi.org/10.1128/MCB.26.2.617-629.2006
   PubMed Web of Science ®Google Scholar
• Chernova TA, Romanyuk AV, Karpova TS, Shanks JR, Ali M, Moffatt N, Howie RL, O'Dell A, McNally JG, Liebman SW, et al. Prion induction by the short-lived, stress-induced protein Lsb2 is regulated by ubiquitination and association with the actin cytoskeleton. Mol Cell 2011; 43:242-52; PMID:21777813; http://dx.doi.org/10.1016/j.molcel.2011.07.001
   PubMed Web of Science ®Google Scholar
• Aguilaniu H, Gustafsson L, Rigoulet M, Nystrom T. Asymmetric inheritance of oxidatively damaged proteins during cytokinesis. Science 2003; 299:1751-3; PMID:12610228; http://dx.doi.org/10.1126/science.1080418
   PubMed Web of Science ®Google Scholar
• Erjavec N, Larsson L, Grantham J, Nystrom T. Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p. Genes Dev 2007; 21:2410-21; http://dx.doi.org/10.1101/gad.439307
   PubMed Web of Science ®Google Scholar
• Liu B, Larsson L, Caballero A, Hao X, Oling D, Grantham J, Nyström T. The polarisome is required for segregation and retrograde transport of protein aggregates. Cell 2010; 140:257-67; PMID:20141839; http://dx.doi.org/10.1016/j.cell.2009.12.031
   PubMed Web of Science ®Google Scholar
• Liu B, Larsson L, Franssens V, Hao X, Hill SM, Andersson V, Höglund D, Song J, Yang X, Öling D, et al. Segregation of protein aggregates involves actin and the polarity machinery. Cell 2011; 147:959-61; PMID:22118450; http://dx.doi.org/10.1016/j.cell.2011.11.018
   PubMed Web of Science ®Google Scholar
• Song J, Yang Q, Yang J, Larsson L, Hao X, Zhu X, Malmgren-Hill S, Cvijovic M, Fernandez-Rodriguez J, Grantham J, et al. Essential genetic interactors of SIR2 required for spatial sequestration and asymmetrical inheritance of protein aggregates. PLoS Genet 2014; 10:e1004539; PMID:25079602; http://dx.doi.org/10.1371/journal.pgen.1004539
   PubMedGoogle Scholar
• Kim J, Scott SV, Oda MN, Klionsky DJ. Transport of a large oligomeric protein by the cytoplasm to vacuole protein targeting pathway. J Cell Biol 1997; 137:609-18; PMID:9151668; http://dx.doi.org/10.1083/jcb.137.3.609
   PubMed Web of Science ®Google Scholar
• Klionsky DJ, Cueva R, Yaver DS. Aminopeptidase I of Saccharomyces cerevisiae is localized to the vacuole independent of the secretory pathway. J Cell Biol 1992; 119:287-99; PMID:1400574; http://dx.doi.org/10.1083/jcb.119.2.287
   PubMed Web of Science ®Google Scholar
• Lynch-Day MA, Klionsky DJ. The Cvt pathway as a model for selective autophagy. FEBS Lett 2010; 584:1359-66; PMID:20146925; http://dx.doi.org/10.1016/j.febslet.2010.02.013
   PubMed Web of Science ®Google Scholar
• Suzuki K. Selective autophagy in budding yeast. Cell Death Differ 2013; 20:43-8; PMID:22705847; http://dx.doi.org/10.1038/cdd.2012.73
   PubMed Web of Science ®Google Scholar
• Monastyrska I, Rieter E, Klionsky DJ, Reggiori F. Multiple roles of the cytoskeleton in autophagy. Biol Rev Camb Philos Soc 2009; 84:431-48; PMID:19659885; http://dx.doi.org/10.1111/j.1469-185X.2009.00082.x
   PubMed Web of Science ®Google Scholar
• Reggiori F, Monastyrska I, Shintani T, Klionsky DJ. The actin cytoskeleton is required for selective types of autophagy, but not nonspecific autophagy, in the yeast Saccharomyces cerevisiae. Mol Biol Cell 2005; 16:5843-56; PMID:16221887; http://dx.doi.org/10.1091/mbc.E05-07-0629
   PubMed Web of Science ®Google Scholar
• Kakuta S, Yamamoto H, Negishi L, Kondo-Kakuta C, Hayashi N, Ohsumi Y. Atg9 vesicles recruit vesicle-tethering proteins Trs85 and Ypt1 to the autophagosome formation site. J Biol Chem 2012; 287:44261-9; PMID:23129774; http://dx.doi.org/10.1074/jbc.M112.411454
   PubMed Web of Science ®Google Scholar
• He C, Song H, Yorimitsu T, Monastyrska I, Yen WL, Legakis JE, Klionsky DJ. Recruitment of Atg9 to the preautophagosomal structure by Atg11 is essential for selective autophagy in budding yeast. J Cell Biol 2006; 175:925-35; PMID:17178909; http://dx.doi.org/10.1083/jcb.200606084
   PubMed Web of Science ®Google Scholar
• Yamamoto H, Kakuta S, Watanabe TM, Kitamura A, Sekito T, Kondo-Kakuta C, Ichikawa R, Kinjo M, Ohsumi Y. Atg9 vesicles are an important membrane source during early steps of autophagosome formation. J Cell Biol 2012; 198:219-33; PMID:22826123; http://dx.doi.org/10.1083/jcb.201202061
   PubMed Web of Science ®Google Scholar
• Mari M, Griffith J, Rieter E, Krishnappa L, Klionsky DJ, Reggiori F. An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis. J Cell Biol 2010; 190:1005-22; PMID:20855505; http://dx.doi.org/10.1083/jcb.200912089
   PubMed Web of Science ®Google Scholar
• Ohashi Y, Munro S. Membrane delivery to the yeast autophagosome from the Golgi-endosomal system. Mol Biol Cell 2010; 21:3998-4008; PMID:20861302; http://dx.doi.org/10.1091/mbc.E10-05-0457
   PubMed Web of Science ®Google Scholar
• Nair U, Jotwani A, Geng J, Gammoh N, Richerson D, Yen WL, Griffith J, Nag S, Wang K, Moss T, et al. SNARE proteins are required for macroautophagy. Cell 2011; 146:290-302; PMID:21784249; http://dx.doi.org/10.1016/j.cell.`2011.06.022
   PubMed Web of Science ®Google Scholar
• Nair U, Klionsky DJ. Autophagosome biogenesis requires SNAREs. Autophagy 2011; 7:1570-2; PMID:22024744; http://dx.doi.org/10.4161/auto.7.12.18001
   PubMed Web of Science ®Google Scholar
• Moreau K, Ravikumar B, Renna M, Puri C, Rubinsztein DC. Autophagosome precursor maturation requires homotypic fusion. Cell 2011; 146:303-17; PMID:21784250; http://dx.doi.org/10.1016/j.cell.2011.06.023
   PubMed Web of Science ®Google Scholar
• Monastyrska I, He C, Geng J, Hoppe AD, Li Z, Klionsky DJ. Arp2 links autophagic machinery with the actin cytoskeleton. Mol Biol Cell 2008; 19:1962-75; PMID:18287533; http://dx.doi.org/10.1091/mbc.E07-09-0892
   PubMed Web of Science ®Google Scholar
• Hammer JA, 3rd, Sellers JR. Walking to work: roles for class V myosins as cargo transporters. Nat Rev Mol Cell Biol 2011; 13:13-26; PMID:22146746; http://dx.doi.org/10.1038/ncb2135
   PubMed Web of Science ®Google Scholar
• Bankaitis VA, Aitken JR, Cleves AE, Dowhan W. An essential role for a phospholipid transfer protein in yeast Golgi function. Nature 1990; 347:561-2; PMID:2215682; http://dx.doi.org/10.1038/347561a0
   PubMed Web of Science ®Google Scholar
• Cleves AE, McGee TP, Whitters EA, Champion KM, Aitken JR, Dowhan W, Goebl M, Bankaitis VA. Mutations in the CDP-choline pathway for phospholipid biosynthesis bypass the requirement for an essential phospholipid transfer protein. Cell 1991; 64:789-800; PMID:1997207; http://dx.doi.org/10.1016/0092-8674(91)90508-V
   PubMed Web of Science ®Google Scholar
• Grabon A, Khan D, Bankaitis VA. Phosphatidylinositol transfer proteins and instructive regulation of lipid kinase biology. Biochim Biophys Acta 2015; 1851:724-35; PMID:25592381; http://dx.doi.org/10.1016/j.bbalip.2014.12.011
   PubMed Web of Science ®Google Scholar
• Hama H, Schnieders EA, Thorner J, Takemoto JY, DeWald DB. Direct involvement of phosphatidylinositol 4-phosphate in secretion in the yeast Saccharomyces cerevisiae. J Biol Chem 1999; 274:34294-300; PMID:10567405; http://dx.doi.org/10.1074/jbc.274.48.34294
   PubMed Web of Science ®Google Scholar
• Fang M, Kearns BG, Gedvilaite A, Kagiwada S, Kearns M, Fung MK, Bankaitis VA. Kes1p shares homology with human oxysterol binding protein and participates in a novel regulatory pathway for yeast Golgi-derived transport vesicle biogenesis. EMBO J 1996; 15:6447-59; PMID:8978672
   PubMed Web of Science ®Google Scholar
• Walch-Solimena C, Novick P. The yeast phosphatidylinositol-4-OH kinase pik1 regulates secretion at the Golgi. Nat Cell Biol 1999; 1:523-5; PMID:10587649; http://dx.doi.org/10.1038/70319
   PubMed Web of Science ®Google Scholar
• Wang K, Yang Z, Liu X, Mao K, Nair U, Klionsky DJ. Phosphatidylinositol 4-kinases are required for autophagic membrane trafficking. J Biol Chem 2012; 287:37964-72; PMID:22977244; http://dx.doi.org/10.1074/jbc.M112.371591
   PubMed Web of Science ®Google Scholar
• Desrivieres S, Cooke FT, Parker PJ, Hall MN. MSS4, a phosphatidylinositol-4-phosphate 5-kinase required for organization of the actin cytoskeleton in Saccharomyces cerevisiae. J Biol Chem 1998; 273:15787-93; PMID:9624178; http://dx.doi.org/10.1074/jbc.273.25.15787
   PubMed Web of Science ®Google Scholar
• Santiago-Tirado FH, Legesse-Miller A, Schott D, Bretscher A. PI4P and Rab inputs collaborate in myosin-V-dependent transport of secretory compartments in yeast. Dev Cell 2011; 20:47-59; PMID:21238924; http://dx.doi.org/10.1016/j.devcel.2010.11.006
   PubMed Web of Science ®Google Scholar
• Mayer A, Wickner W, Haas A. Sec 18p (NSF)-driven release of Sec 17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles. Cell 1996; 85:83-94; PMID:8620540; http://dx.doi.org/10.1016/S0092-8674(00)81084-3
   PubMed Web of Science ®Google Scholar
• Ishihara N, Hamasaki M, Yokota S, Suzuki K, Kamada Y, Kihara A, Yoshimori T, Noda T, Ohsumi Y. Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion. Mol Biol Cell 2001; 12:3690-702; PMID:11694599; http://dx.doi.org/10.1091/mbc.12.11.3690
   PubMed Web of Science ®Google Scholar
• Geng J, Nair U, Yasumura-Yorimitsu K, Klionsky DJ. Post-Golgi Sec proteins are required for autophagy in Saccharomyces cerevisiae. Mol Biol Cell 2010; 21:2257-69; PMID:20444978; http://dx.doi.org/10.1091/mbc.E09-11-0969
   PubMed Web of Science ®Google Scholar
• Jin Y, Sultana A, Gandhi P, Franklin E, Hamamoto S, Khan AR, Munson M, Schekman R, Weisman LS. Myosin V transports secretory vesicles via a Rab GTPase cascade and interaction with the exocyst complex. Dev Cell 2011; 21:1156-70; PMID:22172676; http://dx.doi.org/10.1016/j.devcel.2011.10.009
   PubMed Web of Science ®Google Scholar
• Meriin AB, Zhang X, Miliaras NB, Kazantsev A, Chernoff YO, McCaffery JM, Wendland B, Sherman MY. Aggregation of expanded polyglutamine domain in yeast leads to defects in endocytosis. Mol Cell Biol 2003; 23:7554-65; PMID:14560003; http://dx.doi.org/10.1128/MCB.23.21.7554-7565.2003
   PubMed Web of Science ®Google Scholar
• Meriin AB, Zhang X, Alexandrov IM, Salnikova AB, Ter-Avanesian MD, Chernoff YO, Sherman MY. Endocytosis machinery is involved in aggregation of proteins with expanded polyglutamine domains. FASEB J 2007; 21:1915-25; PMID:17341688; http://dx.doi.org/10.1096/fj.06-6878com
   PubMed Web of Science ®Google Scholar
• Zhou C, Slaughter BD, Unruh JR, Guo F, Yu Z, Mickey K, Narkar A, Ross RT, McClain M, Li R. Organelle-based aggregation and retention of damaged proteins in asymmetrically dividing cells. Cell 2014; 159:530-42; PMID:25417105; http://dx.doi.org/10.1016/j.cell.2014.09.026
   PubMed Web of Science ®Google Scholar