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Volumn 284, Issue 9, 2017, Pages 1267-1278

Phosphatidylinositol-3-phosphate in the regulation of autophagy membrane dynamics

Author keywords

autophagosome; endosome; lysosome; membrane trafficking; PI3P

Indexed keywords

MEMBRANE PROTEIN; NUCLEAR RECEPTOR BINDING FACTOR 2; PHOSPHATIDYLINOSITOL 3 PHOSPHATE; UNCLASSIFIED DRUG; VACUOLE MEMBRANE PROTEIN 1; ATG14 PROTEIN, HUMAN; AUTOPHAGY RELATED PROTEIN; BECLIN 1; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 4 PHOSPHATE 3 KINASE; PHOSPHATIDYLINOSITOL 5-PHOSPHATE; POLYPHOSPHOINOSITIDE; VESICULAR TRANSPORT ADAPTOR PROTEIN;

EID: 85008466118     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.13987     Document Type: Review
Times cited : (157)

References (106)
  • 2
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo G & De Camilli P (2006) Phosphoinositides in cell regulation and membrane dynamics. Nature 443, 651–657.
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 3
    • 84862726617 scopus 로고    scopus 로고
    • Coordination between RAB GTPase and phosphoinositide regulation and functions
    • Jean S & Kiger A (2012) Coordination between RAB GTPase and phosphoinositide regulation and functions. Nat Rev Mol Cell Biol 13, 463–470.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 463-470
    • Jean, S.1    Kiger, A.2
  • 4
    • 77950506156 scopus 로고    scopus 로고
    • Regulation of autophagy by phosphatidylinositol 3-phosphate
    • Burman C & Ktistakis NT (2010) Regulation of autophagy by phosphatidylinositol 3-phosphate. FEBS Lett 584, 1302–1312.
    • (2010) FEBS Lett , vol.584 , pp. 1302-1312
    • Burman, C.1    Ktistakis, N.T.2
  • 5
    • 79953127788 scopus 로고    scopus 로고
    • Autophagosome formation in mammalian cells
    • Burman C & Ktistakis NT (2010) Autophagosome formation in mammalian cells. Semin Immunopathol 32, 397–413.
    • (2010) Semin Immunopathol , vol.32 , pp. 397-413
    • Burman, C.1    Ktistakis, N.T.2
  • 6
    • 84959138272 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphates-at the interface between cell signalling and membrane traffic
    • Marat AL & Haucke V (2016) Phosphatidylinositol 3-phosphates-at the interface between cell signalling and membrane traffic. EMBO J 35, 561–579.
    • (2016) EMBO J , vol.35 , pp. 561-579
    • Marat, A.L.1    Haucke, V.2
  • 8
    • 77950505030 scopus 로고    scopus 로고
    • The role of PI3P phosphatases in the regulation of autophagy
    • Vergne I & Deretic V (2010) The role of PI3P phosphatases in the regulation of autophagy. FEBS Lett 584, 1313–1318.
    • (2010) FEBS Lett , vol.584 , pp. 1313-1318
    • Vergne, I.1    Deretic, V.2
  • 9
    • 84888380983 scopus 로고    scopus 로고
    • The autophagosome: origins unknown, biogenesis complex
    • Lamb CA, Yoshimori T & Tooze SA (2013) The autophagosome: origins unknown, biogenesis complex. Nat Rev Mol Cell Biol 14, 759–774.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 759-774
    • Lamb, C.A.1    Yoshimori, T.2    Tooze, S.A.3
  • 10
    • 33645078650 scopus 로고    scopus 로고
    • Regulation of membrane traffic by phosphoinositide 3-kinases
    • Lindmo K & Stenmark H (2006) Regulation of membrane traffic by phosphoinositide 3-kinases. J Cell Sci 119, 605–614.
    • (2006) J Cell Sci , vol.119 , pp. 605-614
    • Lindmo, K.1    Stenmark, H.2
  • 11
    • 84892152241 scopus 로고    scopus 로고
    • Omegasomes: PI3P platforms that manufacture autophagosomes
    • Roberts R & Ktistakis NT (2013) Omegasomes: PI3P platforms that manufacture autophagosomes. Essays Biochem 55, 17–27.
    • (2013) Essays Biochem , vol.55 , pp. 17-27
    • Roberts, R.1    Ktistakis, N.T.2
  • 12
    • 84921628946 scopus 로고    scopus 로고
    • Retromer and sorting nexins in endosomal sorting
    • Gallon M & Cullen PJ (2015) Retromer and sorting nexins in endosomal sorting. Biochem Soc Trans 43, 33–47.
    • (2015) Biochem Soc Trans , vol.43 , pp. 33-47
    • Gallon, M.1    Cullen, P.J.2
  • 13
    • 84883783979 scopus 로고    scopus 로고
    • Molecular mechanisms of the membrane sculpting ESCRT pathway
    • Henne WM, Stenmark H & Emr SD (2013) Molecular mechanisms of the membrane sculpting ESCRT pathway. Cold Spring Harb Perspect Biol 5, pii: a016766. doi: 10.1101/cshperspect.a016766.
    • (2013) Cold Spring Harb Perspect Biol , vol.5
    • Henne, W.M.1    Stenmark, H.2    Emr, S.D.3
  • 14
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N, Levine B, Cuervo AM & Klionsky DJ (2008) Autophagy fights disease through cellular self-digestion. Nature 451, 1069–1075.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 15
    • 84864318195 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: a unique way to enter the lysosome world
    • Kaushik S & Cuervo AM (2012) Chaperone-mediated autophagy: a unique way to enter the lysosome world. Trends Cell Biol 22, 407–417.
    • (2012) Trends Cell Biol , vol.22 , pp. 407-417
    • Kaushik, S.1    Cuervo, A.M.2
  • 16
    • 84880376355 scopus 로고    scopus 로고
    • Emerging regulation and functions of autophagy
    • Boya P, Reggiori F & Codogno P (2013) Emerging regulation and functions of autophagy. Nat Cell Biol 15, 713–720.
    • (2013) Nat Cell Biol , vol.15 , pp. 713-720
    • Boya, P.1    Reggiori, F.2    Codogno, P.3
  • 17
    • 1842784049 scopus 로고    scopus 로고
    • The biogenesis of multivesicular endosomes
    • Gruenberg J & Stenmark H (2004) The biogenesis of multivesicular endosomes. Nat Rev Mol Cell Biol 5, 317–323.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 317-323
    • Gruenberg, J.1    Stenmark, H.2
  • 18
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • Axe EL, Walker SA, Manifava M, Chandra P, Roderick HL, Habermann A, Griffiths G & Ktistakis NT (2008) Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J Cell Biol 182, 685–701.
    • (2008) J Cell Biol , vol.182 , pp. 685-701
    • Axe, E.L.1    Walker, S.A.2    Manifava, M.3    Chandra, P.4    Roderick, H.L.5    Habermann, A.6    Griffiths, G.7    Ktistakis, N.T.8
  • 19
    • 84892185830 scopus 로고    scopus 로고
    • Current views on the source of the autophagosome membrane
    • Tooze SA (2013) Current views on the source of the autophagosome membrane. Essays Biochem 55, 29–38.
    • (2013) Essays Biochem , vol.55 , pp. 29-38
    • Tooze, S.A.1
  • 20
    • 84881506338 scopus 로고    scopus 로고
    • The ER-Golgi intermediate compartment is a key membrane source for the LC3 lipidation step of autophagosome biogenesis
    • Ge L, Melville D, Zhang M & Schekman R (2013) The ER-Golgi intermediate compartment is a key membrane source for the LC3 lipidation step of autophagosome biogenesis. Elife 2, e00947.
    • (2013) Elife , vol.2
    • Ge, L.1    Melville, D.2    Zhang, M.3    Schekman, R.4
  • 21
    • 84988422403 scopus 로고    scopus 로고
    • ATG16L1 meets ATG9 in recycling endosomes additional roles for the plasma membrane and endocytosis in autophagosome biogenesis
    • Puri C, Renna M, Bento CF, Moreau K & Rubinsztein DC (2014) ATG16L1 meets ATG9 in recycling endosomes additional roles for the plasma membrane and endocytosis in autophagosome biogenesis. Autophagy 10, 182–184.
    • (2014) Autophagy , vol.10 , pp. 182-184
    • Puri, C.1    Renna, M.2    Bento, C.F.3    Moreau, K.4    Rubinsztein, D.C.5
  • 22
    • 84855645313 scopus 로고    scopus 로고
    • Mechanisms of autophagosome biogenesis
    • Rubinsztein DC, Shpilka T & Elazar Z (2012) Mechanisms of autophagosome biogenesis. Curr Biol 22, R29–R34.
    • (2012) Curr Biol , vol.22 , pp. R29-R34
    • Rubinsztein, D.C.1    Shpilka, T.2    Elazar, Z.3
  • 23
    • 79960774898 scopus 로고    scopus 로고
    • Autophagosome precursor maturation requires homotypic fusion
    • Moreau K, Ravikumar B, Renna M, Puri C & Rubinsztein DC (2011) Autophagosome precursor maturation requires homotypic fusion. Cell 146, 303–317.
    • (2011) Cell , vol.146 , pp. 303-317
    • Moreau, K.1    Ravikumar, B.2    Renna, M.3    Puri, C.4    Rubinsztein, D.C.5
  • 24
    • 4344624322 scopus 로고    scopus 로고
    • LC3 conjugation system in mammalian autophagy
    • Tanida I, Ueno T & Kominami E (2004) LC3 conjugation system in mammalian autophagy. Int J Biochem Cell Biol 36, 2503–2518.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2503-2518
    • Tanida, I.1    Ueno, T.2    Kominami, E.3
  • 25
    • 84891461247 scopus 로고    scopus 로고
    • The LC3 interactome at a glance
    • Wild P, McEwan DG & Dikic I (2014) The LC3 interactome at a glance. J Cell Sci 127, 3–9.
    • (2014) J Cell Sci , vol.127 , pp. 3-9
    • Wild, P.1    McEwan, D.G.2    Dikic, I.3
  • 26
    • 0033618147 scopus 로고    scopus 로고
    • The Hansenula polymorpha PDD1 gene product, essential for the selective degradation of peroxisomes, is a homologue of Saccharomyces cerevisiae Vps34p
    • Kiel JA, Rechinger KB, van der Klei IJ, Salomons FA, Titorenko VI & Veenhuis M (1999) The Hansenula polymorpha PDD1 gene product, essential for the selective degradation of peroxisomes, is a homologue of Saccharomyces cerevisiae Vps34p. Yeast 15, 741–754.
    • (1999) Yeast , vol.15 , pp. 741-754
    • Kiel, J.A.1    Rechinger, K.B.2    van der Klei, I.J.3    Salomons, F.A.4    Titorenko, V.I.5    Veenhuis, M.6
  • 28
    • 84977137836 scopus 로고    scopus 로고
    • Mechanistic insights into selective autophagy pathways: lessons from yeast
    • Farré J-C & Subramani S (2016) Mechanistic insights into selective autophagy pathways: lessons from yeast. Nat Rev Mol Cell Biol 17, 537–552.
    • (2016) Nat Rev Mol Cell Biol , vol.17 , pp. 537-552
    • Farré, J.-C.1    Subramani, S.2
  • 29
    • 0005677775 scopus 로고
    • 3-Methyladenine: specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes
    • Seglen PO & Gordon PB (1982) 3-Methyladenine: specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes. Proc Natl Acad Sci USA 79, 1889–1892.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 1889-1892
    • Seglen, P.O.1    Gordon, P.B.2
  • 30
    • 8044257699 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase inhibitors wortmannin and LY294002 inhibit autophagy in isolated rat hepatocytes
    • Blommaart EF, Krause U, Schellens JP, Vreeling-Sindelárová H & Meijer AJ (1997) The phosphatidylinositol 3-kinase inhibitors wortmannin and LY294002 inhibit autophagy in isolated rat hepatocytes. Eur J Biochem 243, 240–246.
    • (1997) Eur J Biochem , vol.243 , pp. 240-246
    • Blommaart, E.F.1    Krause, U.2    Schellens, J.P.3    Vreeling-Sindelárová, H.4    Meijer, A.J.5
  • 32
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3′-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells
    • 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, 992–998.
    • (2000) J Biol Chem , vol.275 , pp. 992-998
    • Petiot, A.1    Ogier-Denis, E.2    Blommaart, E.F.3    Meijer, A.J.4    Codogno, P.5
  • 33
    • 77951217000 scopus 로고    scopus 로고
    • Dual role of 3-methyladenine in modulation of autophagy via different temporal patterns of inhibition on class I and III phosphoinositide 3-kinase
    • Wu Y-T, Tan H-L, Shui G, Bauvy C, Huang Q, Wenk MR, Ong C-N, Codogno P & Shen H-M (2010) Dual role of 3-methyladenine in modulation of autophagy via different temporal patterns of inhibition on class I and III phosphoinositide 3-kinase. J Biol Chem 285, 10850–10861.
    • (2010) J Biol Chem , vol.285 , pp. 10850-10861
    • Wu, Y.-T.1    Tan, H.-L.2    Shui, G.3    Bauvy, C.4    Huang, Q.5    Wenk, M.R.6    Ong, C.-N.7    Codogno, P.8    Shen, H.-M.9
  • 34
    • 0035809160 scopus 로고    scopus 로고
    • Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae
    • Kihara A, Noda T, Ishihara N & Ohsumi Y (2001) Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae. J Cell Biol 152, 519–530.
    • (2001) J Cell Biol , vol.152 , pp. 519-530
    • Kihara, A.1    Noda, T.2    Ishihara, N.3    Ohsumi, Y.4
  • 35
    • 0035032723 scopus 로고    scopus 로고
    • Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network
    • Kihara A, Kabeya Y, Ohsumi Y & Yoshimori T (2001) Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network. EMBO Rep 2, 330–335.
    • (2001) EMBO Rep , vol.2 , pp. 330-335
    • Kihara, A.1    Kabeya, Y.2    Ohsumi, Y.3    Yoshimori, T.4
  • 39
    • 77953543377 scopus 로고    scopus 로고
    • The Beclin 1-VPS34 complex – at the crossroads of autophagy and beyond
    • Funderburk SF, Wang QJ & Yue Z (2010) The Beclin 1-VPS34 complex – at the crossroads of autophagy and beyond. Trends Cell Biol 20, 355–362.
    • (2010) Trends Cell Biol , vol.20 , pp. 355-362
    • Funderburk, S.F.1    Wang, Q.J.2    Yue, Z.3
  • 40
    • 85009423797 scopus 로고    scopus 로고
    • The intricate regulation and complex functions of the Class III phosphoinositide 3-kinase Vps34
    • Backer JM (2016) The intricate regulation and complex functions of the Class III phosphoinositide 3-kinase Vps34. Biochem J 473, 2251–2271.
    • (2016) Biochem J , vol.473 , pp. 2251-2271
    • Backer, J.M.1
  • 43
    • 84911389754 scopus 로고    scopus 로고
    • Vmp1 regulates PtdIns3P signaling during autophagosome formation in Dictyostelium discoideum
    • Calvo-Garrido J, King JS, Muñoz-Braceras S & Escalante R (2014) Vmp1 regulates PtdIns3P signaling during autophagosome formation in Dictyostelium discoideum. Traffic 15, 1235–1246.
    • (2014) Traffic , vol.15 , pp. 1235-1246
    • Calvo-Garrido, J.1    King, J.S.2    Muñoz-Braceras, S.3    Escalante, R.4
  • 47
    • 84907215529 scopus 로고    scopus 로고
    • Nrbf2 protein suppresses autophagy by modulating Atg14L protein-containing Beclin 1-Vps34 complex architecture and reducing intracellular phosphatidylinositol-3 phosphate levels
    • Zhong Y, Morris DH, Jin L, Patel MS, Karunakaran SK, Fu Y-J, Matuszak EA, Weiss HL, Chait BT & Wang QJ (2014) Nrbf2 protein suppresses autophagy by modulating Atg14L protein-containing Beclin 1-Vps34 complex architecture and reducing intracellular phosphatidylinositol-3 phosphate levels. J Biol Chem 289, 26021–26037.
    • (2014) J Biol Chem , vol.289 , pp. 26021-26037
    • Zhong, Y.1    Morris, D.H.2    Jin, L.3    Patel, M.S.4    Karunakaran, S.K.5    Fu, Y.-J.6    Matuszak, E.A.7    Weiss, H.L.8    Chait, B.T.9    Wang, Q.J.10
  • 50
    • 73949124443 scopus 로고    scopus 로고
    • Binding Rubicon to cross the Rubicon
    • Matsunaga K, Noda T & Yoshimori T (2009) Binding Rubicon to cross the Rubicon. Autophagy 5, 876–877.
    • (2009) Autophagy , vol.5 , pp. 876-877
    • Matsunaga, K.1    Noda, T.2    Yoshimori, T.3
  • 51
    • 32244442749 scopus 로고    scopus 로고
    • Functional specificity of the mammalian Beclin-Vps34 PI 3-kinase complex in macroautophagy versus endocytosis and lysosomal enzyme trafficking
    • Zeng X, Overmeyer JH & Maltese WA (2006) Functional specificity of the mammalian Beclin-Vps34 PI 3-kinase complex in macroautophagy versus endocytosis and lysosomal enzyme trafficking. J Cell Sci 119, 259–270.
    • (2006) J Cell Sci , vol.119 , pp. 259-270
    • Zeng, X.1    Overmeyer, J.H.2    Maltese, W.A.3
  • 52
    • 84875450015 scopus 로고    scopus 로고
    • Dissociation of Bcl-2-Beclin1 complex by activated AMPK enhances cardiac autophagy and protects against cardiomyocyte apoptosis in diabetes
    • He C, Zhu H, Li H, Zou M-H & Xie Z (2013) Dissociation of Bcl-2-Beclin1 complex by activated AMPK enhances cardiac autophagy and protects against cardiomyocyte apoptosis in diabetes. Diabetes 62, 1270–1281.
    • (2013) Diabetes , vol.62 , pp. 1270-1281
    • He, C.1    Zhu, H.2    Li, H.3    Zou, M.-H.4    Xie, Z.5
  • 53
    • 84864960430 scopus 로고    scopus 로고
    • Two-site recognition of phosphatidylinositol 3-phosphate by PROPPINs in autophagy
    • Baskaran S, Ragusa MJ, Boura E & Hurley JH (2012) Two-site recognition of phosphatidylinositol 3-phosphate by PROPPINs in autophagy. Mol Cell 47, 339–348.
    • (2012) Mol Cell , vol.47 , pp. 339-348
    • Baskaran, S.1    Ragusa, M.J.2    Boura, E.3    Hurley, J.H.4
  • 54
    • 84904575441 scopus 로고    scopus 로고
    • WIPI2 links LC3 conjugation with PI3P, autophagosome formation, and pathogen clearance by recruiting Atg12-5-16L1
    • Dooley HC, Razi M, Polson HEJ, Girardin SE, Wilson MI & Tooze SA (2014) WIPI2 links LC3 conjugation with PI3P, autophagosome formation, and pathogen clearance by recruiting Atg12-5-16L1. Mol Cell 55, 238–252.
    • (2014) Mol Cell , vol.55 , pp. 238-252
    • Dooley, H.C.1    Razi, M.2    Polson, H.E.J.3    Girardin, S.E.4    Wilson, M.I.5    Tooze, S.A.6
  • 57
    • 84901815187 scopus 로고    scopus 로고
    • Cargo recognition and trafficking in selective autophagy
    • Stolz A, Ernst A & Dikic I (2014) Cargo recognition and trafficking in selective autophagy. Nat Cell Biol 16, 495–501.
    • (2014) Nat Cell Biol , vol.16 , pp. 495-501
    • Stolz, A.1    Ernst, A.2    Dikic, I.3
  • 61
    • 84872117614 scopus 로고    scopus 로고
    • The role of lipids in the control of autophagy
    • Dall'Armi C, Devereaux KA & Di Paolo G (2013) The role of lipids in the control of autophagy. Curr Biol 23, R33–R45.
    • (2013) Curr Biol , vol.23 , pp. R33-R45
    • Dall'Armi, C.1    Devereaux, K.A.2    Di Paolo, G.3
  • 62
    • 70349919804 scopus 로고    scopus 로고
    • Coordination of membrane events during autophagy by multiple class III PI3-kinase complexes
    • Simonsen A & Tooze SA (2009) Coordination of membrane events during autophagy by multiple class III PI3-kinase complexes. J Cell Biol 186, 773–782.
    • (2009) J Cell Biol , vol.186 , pp. 773-782
    • Simonsen, A.1    Tooze, S.A.2
  • 64
    • 84861158462 scopus 로고    scopus 로고
    • Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy
    • Orsi A, Razi M, Dooley HC, Robinson D, Weston AE, Collinson LM & Tooze SA (2012) Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy. Mol Biol Cell 23, 1860–1873.
    • (2012) Mol Biol Cell , vol.23 , pp. 1860-1873
    • Orsi, A.1    Razi, M.2    Dooley, H.C.3    Robinson, D.4    Weston, A.E.5    Collinson, L.M.6    Tooze, S.A.7
  • 65
    • 84880019176 scopus 로고    scopus 로고
    • Fine mapping of autophagy-related proteins during autophagosome formation in Saccharomyces cerevisiae
    • Suzuki K, Akioka M, Kondo-Kakuta C, Yamamoto H & Ohsumi Y (2013) Fine mapping of autophagy-related proteins during autophagosome formation in Saccharomyces cerevisiae. J Cell Sci 126, 2534–2544.
    • (2013) J Cell Sci , vol.126 , pp. 2534-2544
    • Suzuki, K.1    Akioka, M.2    Kondo-Kakuta, C.3    Yamamoto, H.4    Ohsumi, Y.5
  • 66
    • 84884220705 scopus 로고    scopus 로고
    • Diverse autophagosome membrane sources coalesce in recycling endosomes
    • Puri C, Renna M, Bento CF, Moreau K & Rubinsztein DC (2013) Diverse autophagosome membrane sources coalesce in recycling endosomes. Cell 154, 1285–1299.
    • (2013) Cell , vol.154 , pp. 1285-1299
    • Puri, C.1    Renna, M.2    Bento, C.F.3    Moreau, K.4    Rubinsztein, D.C.5
  • 67
    • 84921396314 scopus 로고    scopus 로고
    • Membrane dynamics in autophagosome biogenesis
    • Carlsson SR & Simonsen A (2015) Membrane dynamics in autophagosome biogenesis. J Cell Sci 128, 193–205.
    • (2015) J Cell Sci , vol.128 , pp. 193-205
    • Carlsson, S.R.1    Simonsen, A.2
  • 69
    • 84885175531 scopus 로고    scopus 로고
    • PtdIns(3)P-bound UVRAG coordinates Golgi-ER retrograde and Atg9 transport by differential interactions with the ER tether and the beclin 1 complex
    • He S, Ni D, Ma B, Lee J-H, Zhang T, Ghozalli I, Pirooz SD, Zhao Z, Bharatham N, Li B et al. (2013) PtdIns(3)P-bound UVRAG coordinates Golgi-ER retrograde and Atg9 transport by differential interactions with the ER tether and the beclin 1 complex. Nat Cell Biol 15, 1206–1219.
    • (2013) Nat Cell Biol , vol.15 , pp. 1206-1219
    • He, S.1    Ni, D.2    Ma, B.3    Lee, J.-H.4    Zhang, T.5    Ghozalli, I.6    Pirooz, S.D.7    Zhao, Z.8    Bharatham, N.9    Li, B.10
  • 70
    • 47149089713 scopus 로고    scopus 로고
    • Dynein-dependent movement of autophagosomes mediates efficient encounters with lysosomes
    • Kimura S, Noda T & Yoshimori T (2008) Dynein-dependent movement of autophagosomes mediates efficient encounters with lysosomes. Cell Struct Funct 33, 109–122.
    • (2008) Cell Struct Funct , vol.33 , pp. 109-122
    • Kimura, S.1    Noda, T.2    Yoshimori, T.3
  • 72
    • 84892875805 scopus 로고    scopus 로고
    • At the end of the autophagic road: an emerging understanding of lysosomal functions in autophagy
    • Shen H-M & Mizushima N (2014) At the end of the autophagic road: an emerging understanding of lysosomal functions in autophagy. Trends Biochem Sci 39, 61–71.
    • (2014) Trends Biochem Sci , vol.39 , pp. 61-71
    • Shen, H.-M.1    Mizushima, N.2
  • 73
    • 84862777210 scopus 로고    scopus 로고
    • A mammalian autophagosome maturation mechanism mediated by TECPR1 and the Atg12-Atg5 conjugate
    • Chen D, Fan W, Lu Y, Ding X, Chen S & Zhong Q (2012) A mammalian autophagosome maturation mechanism mediated by TECPR1 and the Atg12-Atg5 conjugate. Mol Cell 45, 629–641.
    • (2012) Mol Cell , vol.45 , pp. 629-641
    • Chen, D.1    Fan, W.2    Lu, Y.3    Ding, X.4    Chen, S.5    Zhong, Q.6
  • 74
  • 75
    • 84862168102 scopus 로고    scopus 로고
    • Lipids in autophagy: constituents, signaling molecules and cargo with relevance to disease
    • Knævelsrud H & Simonsen A (2012) Lipids in autophagy: constituents, signaling molecules and cargo with relevance to disease. Biochim Biophys Acta 1821, 1133–1145.
    • (2012) Biochim Biophys Acta , vol.1821 , pp. 1133-1145
    • Knævelsrud, H.1    Simonsen, A.2
  • 76
    • 84856275868 scopus 로고    scopus 로고
    • PtdIns 3-kinase orchestrates autophagosome formation in yeast
    • Obara K & Ohsumi Y (2011) PtdIns 3-kinase orchestrates autophagosome formation in yeast. J Lipids 2011, 498768.
    • (2011) J Lipids , vol.2011 , pp. 498768
    • Obara, K.1    Ohsumi, Y.2
  • 78
    • 77954164144 scopus 로고    scopus 로고
    • Zebrafish MTMR14 is required for excitation-contraction coupling, developmental motor function and the regulation of autophagy
    • Dowling JJ, Low SE, Busta AS & Feldman EL (2010) Zebrafish MTMR14 is required for excitation-contraction coupling, developmental motor function and the regulation of autophagy. Hum Mol Genet 19, 2668–2681.
    • (2010) Hum Mol Genet , vol.19 , pp. 2668-2681
    • Dowling, J.J.1    Low, S.E.2    Busta, A.S.3    Feldman, E.L.4
  • 82
    • 84981723836 scopus 로고    scopus 로고
    • Autophagosome-lysosome fusion in neurons requires INPP5E, a protein associated with Joubert syndrome
    • Hasegawa J, Iwamoto R, Otomo T, Nezu A, Hamasaki M & Yoshimori T (2016) Autophagosome-lysosome fusion in neurons requires INPP5E, a protein associated with Joubert syndrome. EMBO J 35, 1853–1867.
    • (2016) EMBO J , vol.35 , pp. 1853-1867
    • Hasegawa, J.1    Iwamoto, R.2    Otomo, T.3    Nezu, A.4    Hamasaki, M.5    Yoshimori, T.6
  • 84
    • 84940719535 scopus 로고    scopus 로고
    • mTOR activates the VPS34-UVRAG complex to regulate autolysosomal tubulation and cell survival
    • Munson MJ, Allen GF, Toth R, Campbell DG, Lucocq JM & Ganley IG (2015) mTOR activates the VPS34-UVRAG complex to regulate autolysosomal tubulation and cell survival. EMBO J 34, 2272–2290.
    • (2015) EMBO J , vol.34 , pp. 2272-2290
    • Munson, M.J.1    Allen, G.F.2    Toth, R.3    Campbell, D.G.4    Lucocq, J.M.5    Ganley, I.G.6
  • 85
    • 84870730914 scopus 로고    scopus 로고
    • Autophagic lysosome reformation
    • Chen Y & Yu L (2013) Autophagic lysosome reformation. Exp Cell Res 319, 142–146.
    • (2013) Exp Cell Res , vol.319 , pp. 142-146
    • Chen, Y.1    Yu, L.2
  • 86
    • 84865776097 scopus 로고    scopus 로고
    • Clathrin and phosphatidylinositol-4,5-bisphosphate regulate autophagic lysosome reformation
    • Rong Y, Liu M, Ma L, Du W, Zhang H, Tian Y, Cao Z, Li Y, Ren H, Zhang C et al. (2012) Clathrin and phosphatidylinositol-4,5-bisphosphate regulate autophagic lysosome reformation. Nat Cell Biol 14, 924–934.
    • (2012) Nat Cell Biol , vol.14 , pp. 924-934
    • Rong, Y.1    Liu, M.2    Ma, L.3    Du, W.4    Zhang, H.5    Tian, Y.6    Cao, Z.7    Li, Y.8    Ren, H.9    Zhang, C.10
  • 88
    • 33847048316 scopus 로고    scopus 로고
    • Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenylpyridinium-induced cell death
    • Zhu J, Horbinski C, Guo F, Watkins S, Uchiyama Y & Chu CT (2007) Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenylpyridinium-induced cell death. Am J Pathol 170, 75–86.
    • (2007) Am J Pathol , vol.170 , pp. 75-86
    • Zhu, J.1    Horbinski, C.2    Guo, F.3    Watkins, S.4    Uchiyama, Y.5    Chu, C.T.6
  • 89
    • 84355162283 scopus 로고    scopus 로고
    • Canonical and non-canonical autophagy: variations on a common theme of self-eating?
    • Codogno P, Mehrpour M & Proikas-Cezanne T (2011) Canonical and non-canonical autophagy: variations on a common theme of self-eating? Nat Rev Mol Cell Biol 13, 7–12.
    • (2011) Nat Rev Mol Cell Biol , vol.13 , pp. 7-12
    • Codogno, P.1    Mehrpour, M.2    Proikas-Cezanne, T.3
  • 91
    • 84863679458 scopus 로고    scopus 로고
    • New targets for acetylation in autophagy
    • Hamaï A & Codogno P (2012) New targets for acetylation in autophagy. Sci Signal 5, pe29.
    • (2012) Sci Signal , vol.5 , pp. pe29
    • Hamaï, A.1    Codogno, P.2
  • 92
    • 84872586081 scopus 로고    scopus 로고
    • Differential regulation of distinct Vps34 complexes by AMPK in nutrient stress and autophagy
    • Kim J, Kim YC, Fang C, Russell RC, Kim JH, Fan W, Liu R, Zhong Q & Guan K-L (2013) Differential regulation of distinct Vps34 complexes by AMPK in nutrient stress and autophagy. Cell 152, 290–303.
    • (2013) Cell , vol.152 , pp. 290-303
    • Kim, J.1    Kim, Y.C.2    Fang, C.3    Russell, R.C.4    Kim, J.H.5    Fan, W.6    Liu, R.7    Zhong, Q.8    Guan, K.-L.9
  • 96
    • 0030884527 scopus 로고    scopus 로고
    • Cloning of a human phosphoinositide 3-kinase with a C2 domain that displays reduced sensitivity to the inhibitor wortmannin
    • Domin J, Pages F, Volinia S, Rittenhouse SE, Zvelebil MJ, Stein RC & Waterfield MD (1997) Cloning of a human phosphoinositide 3-kinase with a C2 domain that displays reduced sensitivity to the inhibitor wortmannin. Biochem J 326, 139–147.
    • (1997) Biochem J , vol.326 , pp. 139-147
    • Domin, J.1    Pages, F.2    Volinia, S.3    Rittenhouse, S.E.4    Zvelebil, M.J.5    Stein, R.C.6    Waterfield, M.D.7
  • 97
    • 0035877577 scopus 로고    scopus 로고
    • Activation loop sequences confer substrate specificity to phosphoinositide 3-kinase alpha (PI3Kalpha). Functions of lipid kinase-deficient PI3Kalpha in signaling
    • Pirola L, Zvelebil MJ, Bulgarelli-Leva G, Van Obberghen E, Waterfield MD & Wymann MP (2001) Activation loop sequences confer substrate specificity to phosphoinositide 3-kinase alpha (PI3Kalpha). Functions of lipid kinase-deficient PI3Kalpha in signaling. J Biol Chem 276, 21544–21554.
    • (2001) J Biol Chem , vol.276 , pp. 21544-21554
    • Pirola, L.1    Zvelebil, M.J.2    Bulgarelli-Leva, G.3    Van Obberghen, E.4    Waterfield, M.D.5    Wymann, M.P.6
  • 99
    • 84864751451 scopus 로고    scopus 로고
    • Phosphatidylinositol 3,5-bisphosphate plays a role in the activation and subcellular localization of mechanistic target of rapamycin 1
    • Bridges D, Ma J-T, Park S, Inoki K, Weisman LS & Saltiel AR (2012) Phosphatidylinositol 3,5-bisphosphate plays a role in the activation and subcellular localization of mechanistic target of rapamycin 1. Mol Biol Cell 23, 2955–2962.
    • (2012) Mol Biol Cell , vol.23 , pp. 2955-2962
    • Bridges, D.1    Ma, J.-T.2    Park, S.3    Inoki, K.4    Weisman, L.S.5    Saltiel, A.R.6
  • 100
    • 84873802942 scopus 로고    scopus 로고
    • Essential role of class II phosphatidylinositol-3-kinase-C2α in sphingosine 1-phosphate receptor-1-mediated signaling and migration in endothelial cells
    • Biswas K, Yoshioka K, Asanuma K, Okamoto Y, Takuwa N, Sasaki T & Takuwa Y (2013) Essential role of class II phosphatidylinositol-3-kinase-C2α in sphingosine 1-phosphate receptor-1-mediated signaling and migration in endothelial cells. J Biol Chem 288, 2325–2339.
    • (2013) J Biol Chem , vol.288 , pp. 2325-2339
    • Biswas, K.1    Yoshioka, K.2    Asanuma, K.3    Okamoto, Y.4    Takuwa, N.5    Sasaki, T.6    Takuwa, Y.7
  • 104
    • 77953516805 scopus 로고    scopus 로고
    • Insulin-feedback via PI3K-C2alpha activated PKBalpha/Akt1 is required for glucose-stimulated insulin secretion
    • Leibiger B, Moede T, Uhles S, Barker CJ, Creveaux M, Domin J, Berggren P-O & Leibiger IB (2010) Insulin-feedback via PI3K-C2alpha activated PKBalpha/Akt1 is required for glucose-stimulated insulin secretion. FASEB J 24, 1824–1837.
    • (2010) FASEB J , vol.24 , pp. 1824-1837
    • Leibiger, B.1    Moede, T.2    Uhles, S.3    Barker, C.J.4    Creveaux, M.5    Domin, J.6    Berggren, P.-O.7    Leibiger, I.B.8
  • 105
    • 26244461921 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase C2alpha is essential for ATP-dependent priming of neurosecretory granule exocytosis
    • Meunier FA, Osborne SL, Hammond GRV, Cooke FT, Parker PJ, Domin J & Schiavo G (2005) Phosphatidylinositol 3-kinase C2alpha is essential for ATP-dependent priming of neurosecretory granule exocytosis. Mol Biol Cell 16, 4841–4851.
    • (2005) Mol Biol Cell , vol.16 , pp. 4841-4851
    • Meunier, F.A.1    Osborne, S.L.2    Hammond, G.R.V.3    Cooke, F.T.4    Parker, P.J.5    Domin, J.6    Schiavo, G.7
  • 106
    • 84994153936 scopus 로고    scopus 로고
    • Complex relations between phospholipids, autophagy, and neutral lipids
    • Shatz O, Holland P, Elazar Z & Simonsen A (2016) Complex relations between phospholipids, autophagy, and neutral lipids. Trends Biochem Sci 41, 907–923.
    • (2016) Trends Biochem Sci , vol.41 , pp. 907-923
    • Shatz, O.1    Holland, P.2    Elazar, Z.3    Simonsen, A.4


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