메뉴 건너뛰기




Volumn 5, Issue 4, 2012, Pages 308-311

New Ca2+-dependent regulators of autophagosome maturation

Author keywords

Annexin A1; Annexin A5; Autophagosomal maturation; Ca2+; Copine 1; Endosomes; Lysosomes

Indexed keywords


EID: 84869828593     PISSN: 19420889     EISSN: 19420889     Source Type: Journal    
DOI: 10.4161/cib.20076     Document Type: Article
Times cited : (25)

References (36)
  • 1
    • 67650789599 scopus 로고    scopus 로고
    • Intracellular protein degradation in mammalian cells: recent developments
    • 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
    • (2009) Cell Mol Life Sci; , vol.66 , pp. 2427-2443
    • Knecht, E.1    Aguado, C.2    Cárcel, J.3    Esteban, I.4    Esteve, J.M.5    Ghislat, G.6
  • 3
    • 33846010776 scopus 로고    scopus 로고
    • Microtubules support production of starvation-induced autophagosomes but not their targeting and fusion with lysosomes
    • 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
    • (2006) J Biol Chem; , vol.281 , pp. 36303-36316
    • Fass, E.1    Shvets, E.2    Degani, I.3    Hirschberg, K.4    Elazar, Z.5
  • 5
    • 0042592913 scopus 로고    scopus 로고
    • Fischer von Mollard G. Deletion of the SNARE vti1b in mice results in the loss of a single SNARE partner, syntaxin 8
    • 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
    • (2003) Mol Cell Biol , vol.23 , pp. 5198-5207
    • Atlashkin, V.1    Kreykenbohm, V.2    Eskelinen, E.L.3    Wenzel, D.4    Fayyazi, A.5
  • 6
    • 79960962456 scopus 로고    scopus 로고
    • Role of SNAREs in membrane fusion
    • 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
    • (2011) Adv Exp Med Biol , vol.713 , pp. 13-32
    • Jena, B.P.1
  • 7
    • 0035257013 scopus 로고    scopus 로고
    • Rab proteins as membrane organizers
    • 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
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 107-117
    • Zerial, M.1    McBride, H.2
  • 8
    • 78650600158 scopus 로고    scopus 로고
    • Rubicon controls endosome maturation as a Rab7 effector
    • 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
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 19338-19343
    • Sun, Q.1    Westphal, W.2    Wong, K.N.3    Tan, I.4    Zhong, Q.5
  • 9
    • 0033634646 scopus 로고    scopus 로고
    • Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion
    • 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
    • (2000) Mol Cell , vol.6 , pp. 661-671
    • Sato, T.K.1    Rehling, P.2    Peterson, M.R.3    Emr, S.D.4
  • 10
    • 0034662876 scopus 로고    scopus 로고
    • A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion
    • 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
    • (2000) Proc Natl Acad Sci U S A; , vol.97 , pp. 9402-9407
    • Seals, D.F.1    Eitzen, G.2    Margolis, N.3    Wickner, W.T.4    Price, A.A.5
  • 11
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex
    • 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
    • (2001) ESCRT-I. Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 12
    • 0036697166 scopus 로고    scopus 로고
    • Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body
    • 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
    • (2002) Dev Cell , vol.3 , pp. 283-289
    • Babst, M.1    Katzmann, D.J.2    Snyder, W.B.3    Wendland, B.4    Emr, S.D.5
  • 13
    • 0036696804 scopus 로고    scopus 로고
    • Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting
    • 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
    • (2002) Dev Cell , vol.3 , pp. 271-282
    • Babst, M.1    Katzmann, D.J.2    Estepa-Sabal, E.J.3    Meerloo, T.4    Emr, S.D.5
  • 14
    • 69449089915 scopus 로고    scopus 로고
    • How do ESCRT proteins control autophagy?
    • 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
    • (2009) J Cell Sci; , vol.122 , pp. 2179-2183
    • Rusten, T.E.1    Stenmark, H.2
  • 15
    • 84858145258 scopus 로고    scopus 로고
    • Annexin A5 stimulates autophagy and inhibits endocytosis
    • 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
    • (2012) J Cell Sci; , vol.125 , pp. 92-107
    • Ghislat, G.1    Aguado, C.2    Knecht, E.3
  • 16
    • 79959346132 scopus 로고    scopus 로고
    • Distinct autophagosomal-lysosomal fusion mechanism revealed by thapsigargin-induced autophagy arrest
    • 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
    • (2011) Mol Cell; , vol.42 , pp. 731-743
    • Ganley, I.G.1    Wong, P.M.2    Gammoh, N.3    Jiang, X.4
  • 17
    • 38149044992 scopus 로고    scopus 로고
    • Induction of autophagy promotes fusion of multivesicular bodies with autophagic vacuoles in k562 cells
    • 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
    • (2008) Traffic , vol.9 , pp. 230-250
    • Fader, C.M.1    Sánchez, D.2    Furlán, M.3    Colombo, M.I.4
  • 18
    • 79954597240 scopus 로고    scopus 로고
    • Proteomics analysis of starved cells revealed Annexin A1 as an important regulator of autophagic degradation
    • 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
    • (2011) Biochem Biophys Res Commun , vol.407 , pp. 581-586
    • Kang, J.H.1    Li, M.2    Chen, X.3    Yin, X.M.4
  • 20
    • 33845951914 scopus 로고    scopus 로고
    • Requirement for annexin A1 in plasma membrane repair
    • 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
    • (2006) J Biol Chem , vol.281 , pp. 35202-35207
    • McNeil, A.K.1    Rescher, U.2    Gerke, V.3    McNeil, P.L.4
  • 21
    • 70350399462 scopus 로고    scopus 로고
    • Transmembrane protein-free membranes fuse into xenopus nuclear envelope and promote assembly of functional pores
    • 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
    • (2009) J Biol Chem , vol.284 , pp. 29847-29859
    • Rafikova, E.R.1    Melikov, K.2    Ramos, C.3    Dye, L.4    Chernomordik, L.V.5
  • 22
    • 65649135421 scopus 로고    scopus 로고
    • Prm3p is a pheromoneinduced peripheral nuclear envelope protein required for yeast nuclear fusion
    • Shen S, Tobery CE, Rose MD. Prm3p is a pheromoneinduced 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
    • (2009) Mol Biol Cell , vol.20 , pp. 2438-2450
    • Shen, S.1    Tobery, C.E.2    Rose, M.D.3
  • 23
    • 68549097911 scopus 로고    scopus 로고
    • The annexins: spatial and temporal coordination of signaling events during cellular stress
    • 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
    • (2009) Cell Mol Life Sci , vol.66 , pp. 2623-2642
    • Monastyrskaya, K.1    Babiychuk, E.B.2    Draeger, A.3
  • 24
    • 77955789211 scopus 로고    scopus 로고
    • Altered lipid content inhibits autophagic vesicular fusion
    • 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
    • (2010) FASEB J , vol.24 , pp. 3052-3065
    • Koga, H.1    Kaushik, S.2    Cuervo, A.M.3
  • 25
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • 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
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 26
    • 65649136884 scopus 로고    scopus 로고
    • The structure of Atg4B-LC3 complex reveals the mechanism of LC3 processing and delipidation during autophagy
    • 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
    • (2009) EMBO J , vol.28 , pp. 1341-1350
    • Satoo, K.1    Noda, N.N.2    Kumeta, H.3    Fujioka, Y.4    Mizushima, N.5    Ohsumi, Y.6
  • 27
    • 77953122645 scopus 로고    scopus 로고
    • LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis
    • 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
    • (2010) EMBO J , vol.29 , pp. 1792-1802
    • Weidberg, H.1    Shvets, E.2    Shpilka, T.3    Shimron, F.4    Shinder, V.5    Elazar, Z.6
  • 28
    • 34447099450 scopus 로고    scopus 로고
    • Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion
    • 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
    • (2007) Cell , vol.130 , pp. 165-178
    • Nakatogawa, H.1    Ichimura, Y.2    Ohsumi, Y.3
  • 30
    • 0031939689 scopus 로고    scopus 로고
    • The copines, a novel class of C2 domain-containing, calcium-dependent, phospholipidbinding proteins conserved from Paramecium to humans
    • 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, phospholipidbinding proteins conserved from Paramecium to humans. J Biol Chem 1998; 273:1393-402; http://dx.doi.org/10.1074/jbc.273.3.1393
    • (1998) J Biol Chem , vol.273 , pp. 1393-1402
    • Creutz, C.E.1    Tomsig, J.L.2    Snyder, S.L.3    Gautier, M.C.4    Skouri, F.5    Beisson, J.6
  • 31
    • 34250828455 scopus 로고    scopus 로고
    • Proteomic analysis of membrane-associated proteins from rat liver autophagosomes
    • Øverbye A, Fengsrud M, Seglen PO. Proteomic analysis of membrane-associated proteins from rat liver autophagosomes. Autophagy 2007; 3:300-22
    • (2007) Autophagy , vol.3 , pp. 300-322
    • Øverbye, A.1    Fengsrud, M.2    Seglen, P.O.3
  • 32
    • 29244437151 scopus 로고    scopus 로고
    • a calcium-dependent membrane-binding protein, transiently localizes to the plasma membrane and intracellular vacuoles in Dictyostelium
    • 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
    • (2005) BMC Cell Biol , vol.6 , pp. 46
    • Damer, C.K.1    Bayeva, M.2    Hahn, E.S.3    Rivera, J.4    Socec, C.I.5    Copine, A.6
  • 33
    • 68749117644 scopus 로고    scopus 로고
    • Organization and synergistic binding of copine I and annexin A1 on supported lipid bilayers observed by atomic force microscopy
    • 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.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1950-1961
    • Creutz, C.E.1    Edwardson, J.M.2
  • 34
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: from structure to function
    • Gerke V, Moss SE. Annexins: from structure to function. Physiol Rev 2002; 82:331-71
    • (2002) Physiol Rev , vol.82 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 35
    • 38149094836 scopus 로고    scopus 로고
    • Membrane phosphatidylserine regulates surface charge and protein localization
    • 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
    • (2008) Science , vol.319 , pp. 210-213
    • Yeung, T.1    Gilbert, G.E.2    Shi, J.3    Silvius, J.4    Kapus, A.5    Grinstein, S.6
  • 36
    • 0038532315 scopus 로고    scopus 로고
    • Identification of targets for calcium signaling through the copine family of proteins Characterization of a coiled-coil copine-binding motif
    • 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
    • (2003) J Biol Chem , vol.278 , pp. 10048-10054
    • Tomsig, J.L.1    Snyder, S.L.2    Creutz, C.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.