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Short Communication

New Ca2+-dependent regulators of autophagosome maturation

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Pages 308-311 | Published online: 01 Jul 2012

References

  • Knecht E, Aguado C, Cárcel J, Esteban I, Esteve JM, Ghislat G, et al. Intracellular protein degradation in mammalian cells: recent developments. Cell Mol Life Sci 2009; 66:2427 - 43; http://dx.doi.org/10.1007/s00018-009-0030-6; PMID: 19399586
  • Ravikumar B, Acevedo-Arozena A, Imarisio S, Berger Z, Vacher C, O’Kane CJ, et al. Dynein mutations impair autophagic clearance of aggregate-prone proteins. Nat Genet 2005; 37:771 - 6; http://dx.doi.org/10.1038/ng1591; PMID: 15980862
  • Fass E, Shvets E, Degani I, Hirschberg K, Elazar Z. Microtubules support production of starvation-induced autophagosomes but not their targeting and fusion with lysosomes. J Biol Chem 2006; 281:36303 - 16; http://dx.doi.org/10.1074/jbc.M607031200; PMID: 16963441
  • Parlati F, McNew JA, Fukuda R, Miller R, Söllner TH, Rothman JE. Topological restriction of SNARE-dependent membrane fusion. Nature 2000; 407:194 - 8; http://dx.doi.org/10.1038/35025076; PMID: 11001058
  • Atlashkin V, Kreykenbohm V, Eskelinen EL, Wenzel D, Fayyazi A, Fischer von Mollard G. Deletion of the SNARE vti1b in mice results in the loss of a single SNARE partner, syntaxin 8. Mol Cell Biol 2003; 23:5198 - 207; http://dx.doi.org/10.1128/MCB.23.15.5198-5207.2003; PMID: 12861006
  • Jena BP. Role of SNAREs in membrane fusion. Adv Exp Med Biol 2011; 713:13 - 32; http://dx.doi.org/10.1007/978-94-007-0763-4_3; PMID: 21432012
  • Zerial M, McBride H. Rab proteins as membrane organizers. Nat Rev Mol Cell Biol 2001; 2:107 - 17; http://dx.doi.org/10.1038/35052055; PMID: 11252952
  • Sun Q, Westphal W, Wong KN, Tan I, Zhong Q. Rubicon controls endosome maturation as a Rab7 effector. Proc Natl Acad Sci U S A 2010; 107:19338 - 43; http://dx.doi.org/10.1073/pnas.1010554107; PMID: 20974968
  • Sato TK, Rehling P, Peterson MR, Emr SD. Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion. Mol Cell 2000; 6:661 - 71; http://dx.doi.org/10.1016/S1097-2765(00)00064-2; PMID: 11030345
  • Seals DF, Eitzen G, Margolis N, Wickner WT, Price AA. A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion. Proc Natl Acad Sci U S A 2000; 97:9402 - 7; http://dx.doi.org/10.1073/pnas.97.17.9402; PMID: 10944212
  • Katzmann DJ, Babst M, Emr SD. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell 2001; 106:145 - 55; http://dx.doi.org/10.1016/S0092-8674(01)00434-2; PMID: 11511343
  • Babst M, Katzmann DJ, Snyder WB, Wendland B, Emr SD. Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body. Dev Cell 2002; 3:283 - 9; http://dx.doi.org/10.1016/S1534-5807(02)00219-8; PMID: 12194858
  • Babst M, Katzmann DJ, Estepa-Sabal EJ, Meerloo T, Emr SD. Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting. Dev Cell 2002; 3:271 - 82; http://dx.doi.org/10.1016/S1534-5807(02)00220-4; PMID: 12194857
  • Rusten TE, Stenmark H. How do ESCRT proteins control autophagy?. J Cell Sci 2009; 122:2179 - 83; http://dx.doi.org/10.1242/jcs.050021; PMID: 19535733
  • Ghislat G, Aguado C, Knecht E. Annexin A5 stimulates autophagy and inhibits endocytosis. J Cell Sci 2012; 125:92 - 107; http://dx.doi.org/10.1242/jcs.086728; PMID: 22266906
  • Ganley IG, Wong PM, Gammoh N, Jiang X. Distinct autophagosomal-lysosomal fusion mechanism revealed by thapsigargin-induced autophagy arrest. Mol Cell 2011; 42:731 - 43; http://dx.doi.org/10.1016/j.molcel.2011.04.024; PMID: 21700220
  • Fader CM, Sánchez D, Furlán M, Colombo MI. Induction of autophagy promotes fusion of multivesicular bodies with autophagic vacuoles in k562 cells. Traffic 2008; 9:230 - 50; http://dx.doi.org/10.1111/j.1600-0854.2007.00677.x; PMID: 17999726
  • Kang JH, Li M, Chen X, Yin XM. Proteomics analysis of starved cells revealed Annexin A1 as an important regulator of autophagic degradation. Biochem Biophys Res Commun 2011; 407:581 - 6; http://dx.doi.org/10.1016/j.bbrc.2011.03.067; PMID: 21420379
  • Nylandsted J, Becker AC, Bunkenborg J, Andersen JS, Dengjel J, Jäättelä M. ErbB2-associated changes in the lysosomal proteome. Proteomics 2011; 11:2830 - 8; http://dx.doi.org/10.1002/pmic.201000734; PMID: 21674799
  • McNeil AK, Rescher U, Gerke V, McNeil PL. Requirement for annexin A1 in plasma membrane repair. J Biol Chem 2006; 281:35202 - 7; http://dx.doi.org/10.1074/jbc.M606406200; PMID: 16984915
  • Rafikova ER, Melikov K, Ramos C, Dye L, Chernomordik LV. Transmembrane protein-free membranes fuse into xenopus nuclear envelope and promote assembly of functional pores. J Biol Chem 2009; 284:29847 - 59; http://dx.doi.org/10.1074/jbc.M109.044453; PMID: 19696024
  • Shen S, Tobery CE, Rose MD. Prm3p is a pheromone-induced peripheral nuclear envelope protein required for yeast nuclear fusion. Mol Biol Cell 2009; 20:2438 - 50; http://dx.doi.org/10.1091/mbc.E08-10-0987; PMID: 19297527
  • Monastyrskaya K, Babiychuk EB, Draeger A. The annexins: spatial and temporal coordination of signaling events during cellular stress. Cell Mol Life Sci 2009; 66:2623 - 42; http://dx.doi.org/10.1007/s00018-009-0027-1; PMID: 19381436
  • Koga H, Kaushik S, Cuervo AM. Altered lipid content inhibits autophagic vesicular fusion. FASEB J 2010; 24:3052 - 65; http://dx.doi.org/10.1096/fj.09-144519; PMID: 20375270
  • Behrends C, Sowa ME, Gygi SP, Harper JW. Network organization of the human autophagy system. Nature 2010; 466:68 - 76; http://dx.doi.org/10.1038/nature09204; PMID: 20562859
  • Satoo K, Noda NN, Kumeta H, Fujioka Y, Mizushima N, Ohsumi Y, et al. The structure of Atg4B-LC3 complex reveals the mechanism of LC3 processing and delipidation during autophagy. EMBO J 2009; 28:1341 - 50; http://dx.doi.org/10.1038/emboj.2009.80; PMID: 19322194
  • Weidberg H, Shvets E, Shpilka T, Shimron F, Shinder V, Elazar Z. LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis. EMBO J 2010; 29:1792 - 802; http://dx.doi.org/10.1038/emboj.2010.74; PMID: 20418806
  • Nakatogawa H, Ichimura Y, Ohsumi Y. Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion. Cell 2007; 130:165 - 78; http://dx.doi.org/10.1016/j.cell.2007.05.021; PMID: 17632063
  • Rusten TE, Vaccari T, Lindmo K, Rodahl LM, Nezis IP, Sem-Jacobsen C, et al. ESCRTs and Fab1 regulate distinct steps of autophagy. Curr Biol 2007; 17:1817 - 25; http://dx.doi.org/10.1016/j.cub.2007.09.032; PMID: 17935992
  • Creutz CE, Tomsig JL, Snyder SL, Gautier MC, Skouri F, Beisson J, et al. The copines, a novel class of C2 domain-containing, calcium-dependent, phospholipid-binding proteins conserved from Paramecium to humans. J Biol Chem 1998; 273:1393 - 402; http://dx.doi.org/10.1074/jbc.273.3.1393; PMID: 9430674
  • Øverbye A, Fengsrud M, Seglen PO. Proteomic analysis of membrane-associated proteins from rat liver autophagosomes. Autophagy 2007; 3:300 - 22; PMID: 17377489
  • Damer CK, Bayeva M, Hahn ES, Rivera J, Socec CI. Copine A, a calcium-dependent membrane-binding protein, transiently localizes to the plasma membrane and intracellular vacuoles in Dictyostelium. BMC Cell Biol 2005; 6:46; http://dx.doi.org/10.1186/1471-2121-6-46; PMID: 16343335
  • Creutz CE, Edwardson JM. Organization and synergistic binding of copine I and annexin A1 on supported lipid bilayers observed by atomic force microscopy. Biochim Biophys Acta 2009; 1788:1950 - 61
  • Gerke V, Moss SE. Annexins: from structure to function. Physiol Rev 2002; 82:331 - 71; PMID: 11917092
  • Yeung T, Gilbert GE, Shi J, Silvius J, Kapus A, Grinstein S. Membrane phosphatidylserine regulates surface charge and protein localization. Science 2008; 319:210 - 3; http://dx.doi.org/10.1126/science.1152066; PMID: 18187657
  • Tomsig JL, Snyder SL, Creutz CE. Identification of targets for calcium signaling through the copine family of proteins. Characterization of a coiled-coil copine-binding motif. J Biol Chem 2003; 278:10048 - 54; http://dx.doi.org/10.1074/jbc.M212632200; PMID: 12522145