Abstract
Autophagy can be defined as a catabolic process that maintains cellular homeostasis by the degradation of damaged or excess cellular organelles and protein aggregates from the cytoplasm, thereby enabling cell survival. Cell culture and in vivo studies have revealed the importance of autophagy in numerous diseases, including cancer, aging, neurodegenerative, infectious and inflammatory diseases. Therefore, understanding the molecular basis of the formation and composition of the different structures involved in autophagy, as well as the regulation of this pathway, is an important goal for converting autophagy into a potential therapeutic target in a plethora of diseases.
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Abbreviations
- AD:
-
Adenylate cyclase
- Akt:
-
v-akt murine thymoma viral oncogene homolog 1
- Ambra1:
-
Activating molecule in Beclin-1-regulated autophagy
- AMPK:
-
AMP-activated protein kinase
- Atg:
-
Autophagy-related genes
- Bcl:
-
B-cell lymphoma
- Bnip3:
-
Bcl-2/adenovirus E1B 19 kDa-interacting protein 3
- CMA:
-
Chaperone-mediated autophagy
- DEPTOR:
-
DEP-domain containing mTOR interacting protein
- 4E-BP1:
-
Translation initiation factor 4E-binding protein-1
- Epac:
-
Exchange protein directly activated by cAMP
- ER:
-
Endoplasmic reticulum
- ERK1/2:
-
Extracellular-signal-regulated kinase 1/2
- ESCRT:
-
Endosomal sorting complex required for transport
- FIP200:
-
Focal adhesion kinase family-interacting protein of 200 kDa
- FoxO3:
-
Forkhead box O3
- GAP:
-
GTPase-activating protein
- GPCRs:
-
G-protein-coupled receptors
- HOPS:
-
Homotypic fusion and protein sorting vacuoles
- hVps:
-
Mammalian homologue of vacuolar protein sorting
- IKK:
-
Inhibitor of nuclear factor κB kinase
- IMPase:
-
inositol monophosphatase
- IP3R:
-
Inositol 1,4,5-triphosphate receptor
- I1R:
-
Imidazoline-1 receptor
- JNK1:
-
c-Jun N-terminal kinase 1
- LC3:
-
Microtubule-associated protein light chain 3
- LKB1:
-
Liver Kinase B1
- mLST8:
-
Lethal mammalian protein SEC13 With 8
- mSIN1:
-
mammalian stress-activated protein kinase mitogen activated-interacting protein 1
- mTOR:
-
Mammalian target of rapamycin
- mTORC:
-
mTOR complex
- p70S6K:
-
Ribosomal protein S6 kinase-1
- PDK1:
-
Phosphoinositide-dependent kinase 1
- PE:
-
Phosphatidylethanolamine
- PI3K:
-
Phosphoinositide 3-kinase
- PI3KC1a:
-
Class Ia PI3K
- PI3KC3:
-
Class III PI3K
- PI3KK:
-
PI3K-related protein kinase
- PRAS40:
-
Proline-rich Akt substrate of 40 kDa
- PTEN:
-
Phosphatase and tensin homologue deleted from chromosome 10
- Raptor:
-
Regulatory-associated protein of mTOR
- Rheb:
-
Ras homologue enriched in brain
- Rictor:
-
Rapamycin-insensitive companion of mTOR
- SLC:
-
Solute carrier
- SNARE:
-
N-ethylmaleimide-sensitive factor-attachment protein receptor
- TFEB:
-
Transcription factor EB
- TOR:
-
Target of rapamycin
- TSC:
-
Tuberous sclerosis complex
- UPS:
-
Ubiquitin-proteasome system
- ULK1:
-
UNC-51-like kinase 1
- UVRAG:
-
UV irradiation resistance-associated gene
- v-ATPase:
-
Vacuolar H+-ATPase
- Vps:
-
Vacuolar protein sorting
References
Abrahamsen H, Stenmark H, Platta HW (2012) Ubiquitination and phosphorylation of beclin 1 and its binding partners: tuning class III phosphatidylinositol 3-kinase activity and tumor suppression. FEBS Lett 586(11):1584–1591. doi:10.1016/j.febslet.2012.04.046
Agarraberes FA, Dice JF (2001) A molecular chaperone complex at the lysosomal membrane is required for protein translocation. J Cell Sci 114(Pt 13):2491–2499
Agarraberes FA, Terlecky SR, Dice JF (1997) An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation. J Cell Biol 137(4):825–834. doi:10.1083/jcb.137.4.825
Ashford TP, Porter KR (1962) Cytoplasmic components in hepatic cell lysosomes. J Cell Biol 12:198–202
Baba M, Takeshige K, Baba N, Ohsumi Y (1994) Ultrastructural analysis of the autophagic process in yeast: detection of autophagosomes and their characterization. J Cell Biol 124(6):903–913
Baehrecke EH (2005) Autophagy: dual roles in life and death? Nat Rev Mol Cell Biol 6(6):505–510. doi:10.1038/nrm1666
Behrends C, Sowa ME, Gygi SP, Harper JW (2010) Network organization of the human autophagy system. Nature 466(7302):68–76. doi:10.1038/nature09204
Bjorkoy G, Lamark T, Johansen T (2006) p62/SQSTM1: a missing link between protein aggregates and the autophagy machinery. Autophagy 2(2):138–139
Bursch W (2001) The autophagosomal-lysosomal compartment in programmed cell death. Cell Death Differ 8(6):569–581. doi:10.1038/sj.cdd.4400852
Bursch W, Ellinger A, Gerner C, Frohwein U, Schulte-Hermann R (2000) Programmed cell death (PCD). Apoptosis, autophagic PCD, or others? Ann N Y Acad Sci 926:1–12
Buytaert E, Callewaert G, Vandenheede JR, Agostinis P (2006) Deficiency in apoptotic effectors Bax and Bak reveals an autophagic cell death pathway initiated by photodamage to the endoplasmic reticulum. Autophagy 2(3):238–240
Ciechanover A (2005) Proteolysis: from the lysosome to ubiquitin and the proteasome. Nature Rev Mol Cell Biol 6(1):79–87. doi:10.1038/nrm1552
Ciechomska IA, Goemans GC, Skepper JN, Tolkovsky AM (2009) Bcl-2 complexed with Beclin-1 maintains full anti-apoptotic function. Oncogene 28(21):2128–2141. doi:10.1038/onc.2009.60
Colman RJ, Anderson RM, Johnson SC, Kastman EK, Kosmatka KJ, Beasley TM, Allison DB, Cruzen C, Simmons HA, Kemnitz JW, Weindruch R (2009) Caloric restriction delays disease onset and mortality in rhesus monkeys. Science 325(5937):201–204. doi:10.1126/science.1173635
Criollo A, Senovilla L, Authier H, Maiuri MC, Morselli E, Vitale I, Kepp O, Tasdemir E, Galluzzi L, Shen S, Tailler M, Delahaye N, Tesniere A, De Stefano D, Younes AB, Harper F, Pierron G, Lavandero S, Zitvogel L, Israel A, Baud V, Kroemer G (2010) The IKK complex contributes to the induction of autophagy. EMBO J 29(3):619–631. doi:10.1038/emboj.2009.364
Chiang HL, Dice JF (1988) Peptide sequences that target proteins for enhanced degradation during serum withdrawal. J Biol Chem 263(14):6797–6805
Chin RM, Fu X, Pai MY, Vergnes L, Hwang H, Deng G, Diep S, Lomenick B, Meli VS, Monsalve GC, Hu E, Whelan SA, Wang JX, Jung G, Solis GM, Fazlollahi F, Kaweeteerawat C, Quach A, Nili M, Krall AS, Godwin HA, Chang HR, Faull KF, Guo F, Jiang M, Trauger SA, Saghatelian A, Braas D, Christofk HR, Clarke CF, Teitell MA, Petrascheck M, Reue K, Jung ME, Frand AR, Huang J (2014) The metabolite alpha-ketoglutarate extends lifespan by inhibiting ATP synthase and TOR. Nature 510(7505):397–401. doi:10.1038/nature13264
Degtyarev M, De Maziere A, Orr C, Lin J, Lee BB, Tien JY, Prior WW, van Dijk S, Wu H, Gray DC, Davis DP, Stern HM, Murray LJ, Hoeflich KP, Klumperman J, Friedman LS, Lin K (2008) Akt inhibition promotes autophagy and sensitizes PTEN-null tumors to lysosomotropic agents. J Cell Biol 183(1):101–116. doi:10.1083/jcb.200801099
Dubouloz F, Deloche O, Wanke V, Cameroni E, De Virgilio C (2005) The TOR and EGO protein complexes orchestrate microautophagy in yeast. Mol Cell 19(1):15–26. doi:10.1016/j.molcel.2005.05.020
Feng Y, He D, Yao Z, Klionsky DJ (2014) The machinery of macroautophagy. Cell Res 24(1):24–41. doi:10.1038/cr.2013.168
Fengsrud M, Roos N, Berg T, Liou W, Slot JW, Seglen PO (1995) Ultrastructural and immunocytochemical characterization of autophagic vacuoles in isolated hepatocytes: effects of vinblastine and asparagine on vacuole distributions. Exp Cell Res 221(2):504–519. doi:10.1006/excr.1995.1402
Fimia GM, Stoykova A, Romagnoli A, Giunta L, Di Bartolomeo S, Nardacci R, Corazzari M, Fuoco C, Ucar A, Schwartz P, Gruss P, Piacentini M, Chowdhury K, Cecconi F (2007) Ambra1 regulates autophagy and development of the nervous system. Nature 447(7148):1121–1125. doi:10.1038/nature05925
Fujiwara Y, Furuta A, Kikuchi H, Aizawa S, Hatanaka Y, Konya C, Uchida K, Yoshimura A, Tamai Y, Wada K, Kabuta T (2013) Discovery of a novel type of autophagy targeting RNA. Autophagy 9(3):403–409. doi:10.4161/auto.23002
Ganley IG, Wong PM, Gammoh N, Jiang X (2011) Distinct autophagosomal-lysosomal fusion mechanism revealed by thapsigargin-induced autophagy arrest. Mol Cell 42(6):731–743. doi:10.1016/j.molcel.2011.04.024
Gonzalez-Polo RA, Niso-Santano M, Ortiz-Ortiz MA, Gomez-Martin A, Moran JM, Garcia-Rubio L, Francisco-Morcillo J, Zaragoza C, Soler G, Fuentes JM (2007) Relationship between autophagy and apoptotic cell death in human neuroblastoma cells treated with paraquat: could autophagy be a “brake” in paraquat-induced apoptotic death? Autophagy 3(4):366–367
Gordon PB, Holen I, Fosse M, Rotnes JS, Seglen PO (1993) Dependence of hepatocytic autophagy on intracellularly sequestered calcium. J Biol Chem 268(35):26107–26112
He C, Levine B (2010) The Beclin 1 interactome. Curr Opin Cell Biol 22(2):140–149. doi:10.1016/j.ceb.2010.01.001
Inoki K, Li Y, Zhu T, Wu J, Guan KL (2002) TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling. Nat Cell Biol 4(9):648–657. doi:10.1038/ncb839
Inoki K, Zhu T, Guan KL (2003) TSC2 mediates cellular energy response to control cell growth and survival. Cell 115(5):577–590
Jewell JL, Russell RC, Guan KL (2013) Amino acid signalling upstream of mTOR. Nat Rev Mol Cell Biol 14(3):133–139. doi:10.1038/nrm3522
Jung CH, Ro SH, Cao J, Otto NM, Kim DH (2010) mTOR regulation of autophagy. FEBS Lett 584(7):1287–1295. doi:10.1016/j.febslet.2010.01.017
Kabeya Y, Mizushima N, Ueno T, Yamamoto A, Kirisako T, Noda T, Kominami E, Ohsumi Y, Yoshimori T (2000) LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 19(21):5720–5728. doi:10.1093/emboj/19.21.5720
Kaushik S, Bandyopadhyay U, Sridhar S, Kiffin R, Martinez-Vicente M, Kon M, Orenstein SJ, Wong E, Cuervo AM (2011) Chaperone-mediated autophagy at a glance. J Cell Sci 124(Pt 4):495–499. doi:10.1242/jcs.073874
Kaushik S, Massey AC, Mizushima N, Cuervo AM (2008) Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy. Mol Biol Cell 19(5):2179–2192. doi:10.1091/mbc.E07-11-1155
Klionsky DJ (2005) The molecular machinery of autophagy: unanswered questions. J Cell Sci 118(Pt 1):7–18. doi:10.1242/jcs.01620
Klionsky DJ, Cuervo AM, Dunn WA Jr, Levine B, van der Klei I, Seglen PO (2007) How shall I eat thee? Autophagy 3(5):413–416. doi:4377
Klionsky DJ, Schulman BA (2014) Dynamic regulation of macroautophagy by distinctive ubiquitin-like proteins. Nat Struct Mol Biol 21(4):336–345. doi:10.1038/nsmb.2787
Kondo Y, Kondo S (2006) Autophagy and cancer therapy. Autophagy 2(2):85–90
Kuma A, Matsui M, Mizushima N (2007) LC3, an autophagosome marker, can be incorporated into protein aggregates independent of autophagy: caution in the interpretation of LC3 localization. Autophagy 3(4):323–328
Larrea MD, Liang J, Da Silva T, Hong F, Shao SH, Han K, Dumont D, Slingerland JM (2008) Phosphorylation of p27Kip1 regulates assembly and activation of cyclin D1-Cdk4. Mol Cell Biol 28(20):6462–6472. doi:10.1128/MCB.02300-07
Leroy E, Boyer R, Auburger G, Leube B, Ulm G, Mezey E, Harta G, Brownstein MJ, Jonnalagada S, Chernova T, Dehejia A, Lavedan C, Gasser T, Steinbach PJ, Wilkinson KD, Polymeropoulos MH (1998) The ubiquitin pathway in Parkinson’s disease. Nature 395(6701):451–452. doi:10.1038/26652
Levine B, Klionsky DJ (2004) Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev Cell 6(4):463–477
Loewith R, Jacinto E, Wullschleger S, Lorberg A, Crespo JL, Bonenfant D, Oppliger W, Jenoe P, Hall MN (2002) Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control. Mol Cell 10(3):457–468
Loos B, Engelbrecht AM, Lockshin RA, Klionsky DJ, Zakeri Z (2013) The variability of autophagy and cell death susceptibility Unanswered questions. Autophagy 9(9):1270–1285. doi:10.4161/Auto.25560
LoPiccolo J, Blumenthal GM, Bernstein WB, Dennis PA (2008) Targeting the PI3K/Akt/mTOR pathway: effective combinations and clinical considerations. Drug Resist Updat 11(1–2):32–50. doi:10.1016/j.drup.2007.11.003
Madeo F, Pietrocola F, Eisenberg T, Kroemer G (2014) Caloric restriction mimetics: towards a molecular definition. Nat Rev Drug Discov 13(10):727–740. doi:10.1038/nrd4391
Marino G, Niso-Santano M, Baehrecke EH, Kroemer G (2014) Self-consumption: the interplay of autophagy and apoptosis. Nat Rev Mol Cell Biol 15(2):81–94. doi:10.1038/nrm3735
Martinez-Vicente M, Cuervo AM (2007) Autophagy and neurodegeneration: when the cleaning crew goes on strike. Lancet Neurol 6(4):352–361. doi:10.1016/S1474-4422(07)70076-5
Masiero E, Agatea L, Mammucari C, Blaauw B, Loro E, Komatsu M, Metzger D, Reggiani C, Schiaffino S, Sandri M (2009) Autophagy is required to maintain muscle mass. Cell Metab 10(6):507–515. doi:10.1016/j.cmet.2009.10.008
Matsunaga K, Saitoh T, Tabata K, Omori H, Satoh T, Kurotori N, Maejima I, Shirahama-Noda K, Ichimura T, Isobe T, Akira S, Noda T, Yoshimori T (2009) Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages. Nat Cell Biol 11(4):385–396. doi:10.1038/ncb1846
Meijer AJ (2008) Amino acid regulation of autophagosome formation. Methods Mol Biol 445:89–109. doi:10.1007/978-1-59745-157-4_5
Mijaljica D, Prescott M, Devenish RJ (2011) Microautophagy in mammalian cells: revisiting a 40-year-old conundrum. Autophagy 7(7):673–682
Mizushima N, Noda T, Yoshimori T, Tanaka Y, Ishii T, George MD, Klionsky DJ, Ohsumi M, Ohsumi Y (1998) A protein conjugation system essential for autophagy. Nature 395(6700):395–398. doi:10.1038/26506
Mizushima N, Yamamoto A, Hatano M, Kobayashi Y, Kabeya Y, Suzuki K, Tokuhisa T, Ohsumi Y, Yoshimori T (2001) Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells. J Cell Biol 152(4):657–668
Nakai A, Yamaguchi O, Takeda T, Higuchi Y, Hikoso S, Taniike M, Omiya S, Mizote I, Matsumura Y, Asahi M, Nishida K, Hori M, Mizushima N, Otsu K (2007) The role of autophagy in cardiomyocytes in the basal state and in response to hemodynamic stress. Nat Med 13(5):619–624. doi:10.1038/nm1574
Nicklin P, Bergman P, Zhang B, Triantafellow E, Wang H, Nyfeler B, Yang H, Hild M, Kung C, Wilson C, Myer VE, MacKeigan JP, Porter JA, Wang YK, Cantley LC, Finan PM, Murphy LO (2009) Bidirectional transport of amino acids regulates mTOR and autophagy. Cell 136(3):521–534. doi:10.1016/j.cell.2008.11.044
Ohsumi Y (2001) Molecular dissection of autophagy: two ubiquitin-like systems. Nat Rev Mol Cell Biol 2(3):211–216. doi:10.1038/35056522
Pankiv S, Clausen TH, Lamark T, Brech A, Bruun JA, Outzen H, Overvatn A, Bjorkoy G, Johansen T (2007) p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J Biol Chem 282(33):24131–24145. doi:10.1074/jbc.M702824200
Papandreou I, Lim AL, Laderoute K, Denko NC (2008) Hypoxia signals autophagy in tumor cells via AMPK activity, independent of HIF-1, BNIP3, and BNIP3L. Cell Death Differ 15(10):1572–1581. doi:10.1038/cdd.2008.84
Parys JB, Decuypere JP, Bultynck G (2012) Role of the inositol 1,4,5-trisphosphate receptor/Ca2 + −release channel in autophagy. Cell Commun Signal 10(1):17. doi:10.1186/1478-811X-10-17
Parzych KR, Klionsky DJ (2014) An overview of autophagy: morphology, mechanism, and regulation. Antioxid Redox Signal 20(3):460–473. doi:10.1089/ars.2013.5371
Petiot A, Ogier-Denis E, Blommaart EF, Meijer AJ, Codogno P (2000) Distinct classes of phosphatidylinositol 3′-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells. J Biol Chem 275(2):992–998
Puissant A, Auberger P (2010) AMPK- and p62/SQSTM1-dependent autophagy mediate resveratrol-induced cell death in chronic myelogenous leukemia. Autophagy 6(5):655–657. doi:10.4161/auto.6.5.12126
Ravikumar B, Imarisio S, Sarkar S, O’Kane CJ, Rubinsztein DC (2008) Rab5 modulates aggregation and toxicity of mutant huntingtin through macroautophagy in cell and fly models of Huntington disease. J Cell Sci 121(Pt 10):1649–1660. doi:10.1242/jcs.025726
Ravikumar B, Rubinsztein DC (2004) Can autophagy protect against neurodegeneration caused by aggregate-prone proteins? Neuroreport 15(16):2443–2445
Rusten TE, Stenmark H (2009) How do ESCRT proteins control autophagy? J Cell Sci 122(Pt 13):2179–2183. doi:10.1242/jcs.050021
Salminen A, Kaarniranta K, Kauppinen A (2013) Beclin 1 interactome controls the crosstalk between apoptosis, autophagy and inflammasome activation: impact on the aging process. Ageing Res Rev 12(2):520–534. doi:10.1016/j.arr.2012.11.004
Salvador N, Aguado C, Horst M, Knecht E (2000) Import of a cytosolic protein into lysosomes by chaperone-mediated autophagy depends on its folding state. J Biol Chem 275(35):27447–27456. doi:10.1074/jbc.M001394200
Sarkar S (2013) Regulation of autophagy by mTOR-dependent and mTOR-independent pathways: autophagy dysfunction in neurodegenerative diseases and therapeutic application of autophagy enhancers. Biochem Soc Trans 41(5):1103–1130. doi:10.1042/BST20130134
Sarkar S, Floto RA, Berger Z, Imarisio S, Cordenier A, Pasco M, Cook LJ, Rubinsztein DC (2005) Lithium induces autophagy by inhibiting inositol monophosphatase. J Cell Biol 170(7):1101–1111. doi:10.1083/jcb.200504035
Sarkar S, Korolchuk VI, Renna M, Imarisio S, Fleming A, Williams A, Garcia-Arencibia M, Rose C, Luo S, Underwood BR, Kroemer G, O’Kane CJ, Rubinsztein DC (2011) Complex inhibitory effects of nitric oxide on autophagy. Mol Cell 43(1):19–32. doi:10.1016/j.molcel.2011.04.029
Schneider JL, Suh Y, Cuervo AM (2014) Deficient chaperone-mediated autophagy in liver leads to metabolic dysregulation. Cell Metab 20(3):417–432. doi:10.1016/j.cmet.2014.06.009
Schroeder S, Pendl T, Zimmermann A, Eisenberg T, Carmona-Gutierrez D, Ruckenstuhl C, Marino G, Pietrocola F, Harger A, Magnes C, Sinner F, Pieber TR, Dengjel J, Sigrist SJ, Kroemer G, Madeo F (2014) Acetyl-coenzyme A: a metabolic master regulator of autophagy and longevity. Autophagy 10(7):1335–1337. doi:10.4161/auto.28919
Shinojima N, Yokoyama T, Kondo Y, Kondo S (2007) Roles of the Akt/mTOR/p70S6K and ERK1/2 signaling pathways in curcumin-induced autophagy. Autophagy 3(6):635–637
Singh R, Xiang Y, Wang Y, Baikati K, Cuervo AM, Luu YK, Tang Y, Pessin JE, Schwartz GJ, Czaja MJ (2009) Autophagy regulates adipose mass and differentiation in mice. J Clin Invest 119(11):3329–3339. doi:10.1172/JCI39228
Skupin A, Falcke M (2008) The role of IP3R clustering in Ca2+ signalinG. Genome Inform 20:15–24
Stroupe C (2011) Autophagy: cells SNARE selves. Curr Biol 21(18):R697–R699. doi:10.1016/j.cub.2011.08.017
Suzuki K, Ohsumi Y (2007) Molecular machinery of autophagosome formation in yeast, Saccharomyces cerevisiae. FEBS Lett 581(11):2156–2161. doi:10.1016/j.febslet.2007.01.096
Tanida I, Ueno T, Kominami E (2004) LC3 conjugation system in mammalian autophagy. Int J Biochem Cell Biol 36(12):2503–2518. doi:10.1016/j.biocel.2004.05.009
Tasdemir E, Maiuri MC, Galluzzi L, Vitale I, Djavaheri-Mergny M, D’Amelio M, Criollo A, Morselli E, Zhu C, Harper F, Nannmark U, Samara C, Pinton P, Vicencio JM, Carnuccio R, Moll UM, Madeo F, Paterlini-Brechot P, Rizzuto R, Szabadkai G, Pierron G, Blomgren K, Tavernarakis N, Codogno P, Cecconi F, Kroemer G (2008) Regulation of autophagy by cytoplasmic p53. Nat Cell Biol 10(6):676–687. doi:10.1038/ncb1730
Terlecky SR, Dice JF (1993) Polypeptide import and degradation by isolated lysosomes. J Biol Chem 268(31):23490–23495
Todde V, Veenhuis M, van der Klei IJ (2009) Autophagy: principles and significance in health and disease. Biochim Biophys Acta 1792(1):3–13. doi:10.1016/j.bbadis.2008.10.016
Uemura T, Yamamoto M, Kametaka A, Sou YS, Yabashi A, Yamada A, Annoh H, Kametaka S, Komatsu M, Waguri S (2014) A cluster of thin tubular structures mediates transformation of the endoplasmic reticulum to autophagic isolation membrane. Mol Cell Biol 34(9):1695–1706. doi:10.1128/MCB.01327-13
Wada Y, Sun-Wada GH, Kawamura N (2013) Microautophagy in the visceral endoderm is essential for mouse early development. Autophagy 9(2):252–254. doi:10.4161/auto.22585
Williams A, Sarkar S, Cuddon P, Ttofi EK, Saiki S, Siddiqi FH, Jahreiss L, Fleming A, Pask D, Goldsmith P, O’Kane CJ, Floto RA, Rubinsztein DC (2008) Novel targets for Huntington’s disease in an mTOR-independent autophagy pathway. Nat Chem Biol 4(5):295–305. doi:10.1038/nchembio.79
Yakhine-Diop SM, Bravo-San Pedro JM, Gomez-Sanchez R, Pizarro-Estrella E, Rodriguez-Arribas M, Climent V, Aiastui A, Lopez de Munain A, Fuentes JM, Gonzalez-Polo RA (2014) G2019S LRRK2 mutant fibroblasts from Parkinson’s disease patients show increased sensitivity to neurotoxin 1-methyl-4-phenylpyridinium dependent of autophagy. Toxicology 324:1–9. doi:10.1016/j.tox.2014.07.001
Yang Q, Inoki K, Kim E, Guan KL (2006) TSC1/TSC2 and Rheb have different effects on TORC1 and TORC2 activity. Proc Natl Acad Sci U S A 103(18):6811–6816. doi:10.1073/pnas.0602282103
Yla-Anttila P, Vihinen H, Jokitalo E, Eskelinen EL (2009) 3D tomography reveals connections between the phagophore and endoplasmic reticulum. Autophagy 5(8):1180–1185
Young AR, Chan EY, Hu XW, Kochl R, Crawshaw SG, High S, Hailey DW, Lippincott-Schwartz J, Tooze SA (2006) Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes. J Cell Sci 119(Pt 18):3888–3900. doi:10.1242/jcs.03172
Zhong Y, Wang QJ, Li X, Yan Y, Backer JM, Chait BT, Heintz N, Yue Z (2009) Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex. Nat Cell Biol 11(4):468–476. doi:10.1038/ncb1854
Zhou J, Liao W, Yang J, Ma K, Li X, Wang Y, Wang D, Wang L, Zhang Y, Yin Y, Zhao Y, Zhu WG (2012) FOXO3 induces FOXO1-dependent autophagy by activating the AKT1 signaling pathway. Autophagy 8(12):1712–1723. doi:10.4161/auto.21830
Zoncu R, Efeyan A, Sabatini DM (2011) mTOR: from growth signal integration to cancer, diabetes and ageing. Nat Rev Mol Cell Biol 12(1):21–35. doi:10.1038/nrm3025
Acknowledgements
Rosa-Ana González-Polo was supported by a talent research contract (Junta de Extremadura, TA13009, Spain) and received research support from the Ministerio de Ciencia e Innovación, Spain (PI14/00170). Dr. José M. Fuentes received research support from the Ministerio de Ciencia e Innovación, Spain, CIBERNED (CB06/05/004), Consejería, Economía, Comercio e Innovación Junta de Extremadura (GR15045), Ministerio de Ciencia e Innovación, Spain (PI150034). This work is supported also by “Fondo Europeo de Desarrollo Regional” (FEDER), from European Union. We all thanks to FUNDESALUD for helpful assistance.
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González-Polo, R.A. et al. (2016). The Basics of Autophagy. In: Maiuri, M., De Stefano, D. (eds) Autophagy Networks in Inflammation. Progress in Inflammation Research. Springer, Cham. https://doi.org/10.1007/978-3-319-30079-5_1
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