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Volumn 28, Issue 3, 2014, Pages 169-177

Rab proteins implicated in lipid storage and mobilization

Author keywords

Effector; GAP; GEF; GTPase; Lipid droplet; Rab protein

Indexed keywords

FAT DROPLET; GUANOSINE TRIPHOSPHATASE; RAB PROTEIN; RAB18 PROTEIN; RAB7 PROTEIN; TRIACYLGLYCEROL; UNCLASSIFIED DRUG;

EID: 84923846462     PISSN: 16748301     EISSN: None     Source Type: Journal    
DOI: 10.7555/JBR.28.20140029     Document Type: Article
Times cited : (35)

References (103)
  • 1
    • 0026782950 scopus 로고
    • Isoprenylation of rab proteins on structurally distinct cysteine motifs
    • Peter M, Chavrier P, Nigg EA, Zerial M. Isoprenylation of rab proteins on structurally distinct cysteine motifs. J Cell Sci 1992;102:857-65.
    • (1992) J Cell Sci , vol.102 , pp. 857-865
    • Peter, M.1    Chavrier, P.2    Nigg, E.A.3    Zerial, M.4
  • 2
    • 0028067898 scopus 로고
    • Rab escort protein-1 is a multifunctional protein that accompanies newly prenylated rab proteins to their target membranes
    • Alexandrov K, Horiuchi H, Steele-Mortimer O, Seabra MC, Zerial M. Rab escort protein-1 is a multifunctional protein that accompanies newly prenylated rab proteins to their target membranes. EMBO J 1994;13:5262-73.
    • (1994) EMBO J , vol.13 , pp. 5262-5273
    • Alexandrov, K.1    Horiuchi, H.2    Steele-Mortimer, O.3    Seabra, M.C.4    Zerial, M.5
  • 3
    • 84892633429 scopus 로고    scopus 로고
    • Mechanism of statin-induced rhabdomyolysis
    • Sakamoto K, Kimura J. Mechanism of statin-induced rhabdomyolysis. J Pharmacol Sci 2013;123:289-94.
    • (2013) J Pharmacol Sci , vol.123 , pp. 289-294
    • Sakamoto, K.1    Kimura, J.2
  • 4
    • 79959512148 scopus 로고    scopus 로고
    • Inhibition of Rab1 GTPase and endoplasmic reticulum-to-Golgi trafficking underlies statin s toxicity in rat skeletal myofibers
    • Sakamoto K, Wada I, Kimura J. Inhibition of Rab1 GTPase and endoplasmic reticulum-to-Golgi trafficking underlies statin s toxicity in rat skeletal myofibers. J Pharmacol Exp Ther 2011;338:62-9.
    • (2011) J Pharmacol Exp Ther , vol.338 , pp. 62-69
    • Sakamoto, K.1    Wada, I.2    Kimura, J.3
  • 5
    • 35848968214 scopus 로고    scopus 로고
    • The protein microscope: incorporating mass spectrometry into cell biology
    • Bell AW, Nilsson T, Kearney RE, Bergeron JJ. The protein microscope: incorporating mass spectrometry into cell biology. Nat Methods 2007;4:783-4.
    • (2007) Nat Methods , vol.4 , pp. 783-784
    • Bell, A.W.1    Nilsson, T.2    Kearney, R.E.3    Bergeron, J.J.4
  • 7
    • 0242446165 scopus 로고    scopus 로고
    • Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11
    • Sonnichsen B, de Renzis S, Nielsen E, Rietdorf J, Zerial M. Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11. J Cell Biol 2000;149:901-14.
    • (2000) J Cell Biol , vol.149 , pp. 901-914
    • Sonnichsen, B.1    de Renzis, S.2    Nielsen, E.3    Rietdorf, J.4    Zerial, M.5
  • 9
    • 84859833144 scopus 로고    scopus 로고
    • The interaction properties of the human Rab GTPase family-comparative analysis reveals determinants of molecular binding selectivity
    • Stein M, Pilli M, Bernauer S, Habermann BH, Zerial M, Wade RC. The interaction properties of the human Rab GTPase family-comparative analysis reveals determinants of molecular binding selectivity. PLoS One 2012;7: e34870.
    • (2012) PLoS One , vol.7
    • Stein, M.1    Pilli, M.2    Bernauer, S.3    Habermann, B.H.4    Zerial, M.5    Wade, R.C.6
  • 11
    • 84870197315 scopus 로고    scopus 로고
    • Specific localization of Rabs at intracellular membranes
    • Blumer J, Wu YW, Goody RS, Itzen A. Specific localization of Rabs at intracellular membranes. Biochem Soc Trans 2012;40:1421-5.
    • (2012) Biochem Soc Trans , vol.40 , pp. 1421-1425
    • Blumer, J.1    Wu, Y.W.2    Goody, R.S.3    Itzen, A.4
  • 13
    • 84879904590 scopus 로고    scopus 로고
    • Rab1a and Rab5a preferentially bind to binary lipid compositions with higher stored curvature elastic energy
    • Kirsten ML, Baron RA, Seabra MC, Ces O. Rab1a and Rab5a preferentially bind to binary lipid compositions with higher stored curvature elastic energy. Mol Membr Biol 2013;30:303-14.
    • (2013) Mol Membr Biol , vol.30 , pp. 303-314
    • Kirsten, M.L.1    Baron, R.A.2    Seabra, M.C.3    Ces, O.4
  • 14
    • 0034427027 scopus 로고    scopus 로고
    • Purification and identification of novel Rab effectors using affinity chromatography
    • Christoforidis S, Zerial M. Purification and identification of novel Rab effectors using affinity chromatography. Methods 2000;20:403-10.
    • (2000) Methods , vol.20 , pp. 403-410
    • Christoforidis, S.1    Zerial, M.2
  • 15
    • 0028791634 scopus 로고
    • Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion
    • Stenmark H, Vitale G, Ullrich O, Zerial M. Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion. Cell 1995;83:423-32.
    • (1995) Cell , vol.83 , pp. 423-432
    • Stenmark, H.1    Vitale, G.2    Ullrich, O.3    Zerial, M.4
  • 16
    • 0242351052 scopus 로고    scopus 로고
    • RIN3: a novel Rab5 GEF interacting with amphiphysin II involved in the early endocytic pathway
    • Kajiho H, Saito K, Tsujita K, Kontani K, Araki Y, Kurosu H, Katada T. RIN3: a novel Rab5 GEF interacting with amphiphysin II involved in the early endocytic pathway. J Cell Sci 2003;116:4159-68.
    • (2003) J Cell Sci , vol.116 , pp. 4159-4168
    • Kajiho, H.1    Saito, K.2    Tsujita, K.3    Kontani, K.4    Araki, Y.5    Kurosu, H.6    Katada, T.7
  • 17
    • 17344377424 scopus 로고    scopus 로고
    • A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function
    • Horiuchi H, Lippe R, McBride HM, Rubino M, Woodman P, Stenmark H, et al. A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function. Cell 1997;90:1149- 59.
    • (1997) Cell , vol.90 , pp. 1149-1159
    • Horiuchi, H.1    Lippe, R.2    McBride, H.M.3    Rubino, M.4    Woodman, P.5    Stenmark, H.6
  • 18
    • 0036172652 scopus 로고    scopus 로고
    • Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes
    • de Renzis S, Sonnichsen B, Zerial M. Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes. Nat Cell Biol 2002;4:124-33.
    • (2002) Nat Cell Biol , vol.4 , pp. 124-133
    • de Renzis, S.1    Sonnichsen, B.2    Zerial, M.3
  • 19
    • 0034735512 scopus 로고    scopus 로고
    • Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain
    • Nielsen E, Christoforidis S, Uttenweiler-Joseph S, Miaczynska M, Dewitte F, Wilm M, et al. Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain. J Cell Biol 2000;151:601-12.
    • (2000) J Cell Biol , vol.151 , pp. 601-612
    • Nielsen, E.1    Christoforidis, S.2    Uttenweiler-Joseph, S.3    Miaczynska, M.4    Dewitte, F.5    Wilm, M.6
  • 23
    • 0033580299 scopus 로고    scopus 로고
    • The Rab5 effector EEA1 is a core component of endosome docking
    • Christoforidis S, McBride HM, Burgoyne RD, Zerial M. The Rab5 effector EEA1 is a core component of endosome docking. Nature 1999;397:621-5.
    • (1999) Nature , vol.397 , pp. 621-625
    • Christoforidis, S.1    McBride, H.M.2    Burgoyne, R.D.3    Zerial, M.4
  • 24
    • 23944437499 scopus 로고    scopus 로고
    • An enzymatic cascade of Rab5 effectors regulates phosphoinositide turnover in the endocytic pathway
    • Shin HW, Hayashi M, Christoforidis S, Lacas-Gervais S, Hoepfner S, Wenk MR, et al. An enzymatic cascade of Rab5 effectors regulates phosphoinositide turnover in the endocytic pathway. J Cell Biol 2005;170:607-18.
    • (2005) J Cell Biol , vol.170 , pp. 607-618
    • Shin, H.W.1    Hayashi, M.2    Christoforidis, S.3    Lacas-Gervais, S.4    Hoepfner, S.5    Wenk, M.R.6
  • 27
    • 0033529564 scopus 로고    scopus 로고
    • Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13
    • McBride HM, Rybin V, Murphy C, Giner A, Teasdale R, Zerial M. Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13. Cell 1999;98:377-86.
    • (1999) Cell , vol.98 , pp. 377-386
    • McBride, H.M.1    Rybin, V.2    Murphy, C.3    Giner, A.4    Teasdale, R.5    Zerial, M.6
  • 28
    • 0037413690 scopus 로고    scopus 로고
    • Divalent interaction of the GGAs with the Rabaptin-5- Rabex-5 complex
    • Mattera R, Arighi CN, Lodge R, Zerial M, Bonifacino JS. Divalent interaction of the GGAs with the Rabaptin-5- Rabex-5 complex. EMBO J 2003;22:78-88.
    • (2003) EMBO J , vol.22 , pp. 78-88
    • Mattera, R.1    Arighi, C.N.2    Lodge, R.3    Zerial, M.4    Bonifacino, J.S.5
  • 29
    • 32644434386 scopus 로고    scopus 로고
    • Huntingtin-HAP40 complex is a novel Rab5 effector that regulates early endosome motility and is up-regulated in Huntington s disease
    • Pal A, Severin F, Lommer B, Shevchenko A, Zerial M. Huntingtin-HAP40 complex is a novel Rab5 effector that regulates early endosome motility and is up-regulated in Huntington s disease. J Cell Biol 2006;172:605-18.
    • (2006) J Cell Biol , vol.172 , pp. 605-618
    • Pal, A.1    Severin, F.2    Lommer, B.3    Shevchenko, A.4    Zerial, M.5
  • 30
    • 0037993790 scopus 로고    scopus 로고
    • Recombinant antibodies to the small GTPase Rab6 as conformation sensors
    • Nizak C, Monier S, del Nery E, Moutel S, Goud B, Perez F. Recombinant antibodies to the small GTPase Rab6 as conformation sensors. Science 2003;300:984-7.
    • (2003) Science , vol.300 , pp. 984-987
    • Nizak, C.1    Monier, S.2    del Nery, E.3    Moutel, S.4    Goud, B.5    Perez, F.6
  • 33
    • 84864864505 scopus 로고    scopus 로고
    • Lipid droplet formation on opposing sides of the endoplasmic reticulum
    • Sturley SL, Hussain MM. Lipid droplet formation on opposing sides of the endoplasmic reticulum. J Lipid Res 2012;53:1800-10.
    • (2012) J Lipid Res , vol.53 , pp. 1800-1810
    • Sturley, S.L.1    Hussain, M.M.2
  • 34
    • 84856072854 scopus 로고    scopus 로고
    • Packaging of fat: an evolving model of lipid droplet assembly and expansion
    • Brasaemle DL, Wolins NE. Packaging of fat: an evolving model of lipid droplet assembly and expansion. J Biol Chem 2012;287:2273-9.
    • (2012) J Biol Chem , vol.287 , pp. 2273-2279
    • Brasaemle, D.L.1    Wolins, N.E.2
  • 36
    • 46749130169 scopus 로고    scopus 로고
    • Identification of a novel N-terminal hydrophobic sequence that targets proteins to lipid droplets
    • Zehmer JK, Bartz R, Liu P, Anderson RG. Identification of a novel N-terminal hydrophobic sequence that targets proteins to lipid droplets. J Cell Sci 2008;121: 1852-60.
    • (2008) J Cell Sci , vol.121 , pp. 1852-1860
    • Zehmer, J.K.1    Bartz, R.2    Liu, P.3    Anderson, R.G.4
  • 37
    • 78650159016 scopus 로고    scopus 로고
    • Biogenesis of lipid droplets-how cells get fatter
    • Kalantari F, Bergeron JJ, Nilsson T. Biogenesis of lipid droplets-how cells get fatter. Mol Membr Biol 2010;27: 462-8.
    • (2010) Mol Membr Biol , vol.27 , pp. 462-468
    • Kalantari, F.1    Bergeron, J.J.2    Nilsson, T.3
  • 40
    • 80455135722 scopus 로고    scopus 로고
    • Perilipin 5, a lipid droplet-associated protein, provides physical and metabolic linkage to mitochondria
    • Wang H, Sreenivasan U, Hu H, Saladino A, Polster BM, Lund LM, et al. Perilipin 5, a lipid droplet-associated protein, provides physical and metabolic linkage to mitochondria. J Lipid Res 2011;52:2159-68.
    • (2011) J Lipid Res , vol.52 , pp. 2159-2168
    • Wang, H.1    Sreenivasan, U.2    Hu, H.3    Saladino, A.4    Polster, B.M.5    Lund, L.M.6
  • 41
    • 80053062569 scopus 로고    scopus 로고
    • Interactomic study on interaction between lipid droplets and mitochondria
    • Pu J, Ha CW, Zhang S, Jung JP, Huh WK, Liu P. Interactomic study on interaction between lipid droplets and mitochondria. Protein Cell 2011;2:487-96.
    • (2011) Protein Cell , vol.2 , pp. 487-496
    • Pu, J.1    Ha, C.W.2    Zhang, S.3    Jung, J.P.4    Huh, W.K.5    Liu, P.6
  • 42
    • 65549166714 scopus 로고    scopus 로고
    • Lipophagy: selective catabolism designed for lipids
    • Weidberg H, Shvets E, Elazar Z. Lipophagy: selective catabolism designed for lipids. Dev Cell 2009;16:628-30.
    • (2009) Dev Cell , vol.16 , pp. 628-630
    • Weidberg, H.1    Shvets, E.2    Elazar, Z.3
  • 43
    • 84870995648 scopus 로고    scopus 로고
    • Regulation of lipid stores and metabolism by lipophagy
    • Liu K, Czaja MJ. Regulation of lipid stores and metabolism by lipophagy. Cell Death Differ 2013;20:3-11.
    • (2013) Cell Death Differ , vol.20 , pp. 3-11
    • Liu, K.1    Czaja, M.J.2
  • 44
    • 84859768059 scopus 로고    scopus 로고
    • Lipophagy: connecting autophagy and lipid metabolism.
    • Singh R, Cuervo AM. Lipophagy: connecting autophagy and lipid metabolism. Int J Cell Biol 2012:2012:282041.
    • (2012) Int J Cell Biol , vol.2012
    • Singh, R.1    Cuervo, A.M.2
  • 45
    • 79958030075 scopus 로고    scopus 로고
    • Autophagy regulates cholesterol efflux from macrophage foam cells via lysosomal acid lipase
    • Ouimet M, Franklin V, Mak E, Liao X, Tabas I, Marcel YL. Autophagy regulates cholesterol efflux from macrophage foam cells via lysosomal acid lipase. Cell Metab 2011;13:655-67.
    • (2011) Cell Metab , vol.13 , pp. 655-667
    • Ouimet, M.1    Franklin, V.2    Mak, E.3    Liao, X.4    Tabas, I.5    Marcel, Y.L.6
  • 47
    • 0346874342 scopus 로고    scopus 로고
    • Proteomic characterization of the human centrosome by protein correlation profiling
    • Andersen JS, Wilkinson CJ, Mayor T, Mortensen P, Nigg EA, Mann M. Proteomic characterization of the human centrosome by protein correlation profiling. Nature 2003;426:570-4.
    • (2003) Nature , vol.426 , pp. 570-574
    • Andersen, J.S.1    Wilkinson, C.J.2    Mayor, T.3    Mortensen, P.4    Nigg, E.A.5    Mann, M.6
  • 49
    • 84875367136 scopus 로고    scopus 로고
    • Protein correlation profiles identify lipid droplet proteins with high confidence
    • Krahmer N, Hilger M, Kory N, Wilfling F, Stoehr G,Mann M, et al. Protein correlation profiles identify lipid droplet proteins with high confidence. Mol Cell Proteomics 2013;12:1115-26.
    • (2013) Mol Cell Proteomics , vol.12 , pp. 1115-1126
    • Krahmer, N.1    Hilger, M.2    Kory, N.3    Wilfling, F.4    Stoehr, G.5    Mann, M.6
  • 50
    • 36048946762 scopus 로고    scopus 로고
    • Identification of the domains required for the localization of Prp19p to lipid droplets or the nucleus
    • Cho SY, Park PJ, Lee JH, Kim JJ, Lee TR. Identification of the domains required for the localization of Prp19p to lipid droplets or the nucleus. Biochem Biophys Res Commun 2007;364:844-9.
    • (2007) Biochem Biophys Res Commun , vol.364 , pp. 844-849
    • Cho, S.Y.1    Park, P.J.2    Lee, J.H.3    Kim, J.J.4    Lee, T.R.5
  • 52
    • 84860436155 scopus 로고    scopus 로고
    • Proteomic profiling of lipid droplet-associated proteins in primary adipocytes of normal and obese mouse
    • Ding Y, Wu Y, Zeng R, Liao K. Proteomic profiling of lipid droplet-associated proteins in primary adipocytes of normal and obese mouse. Acta Biochim Biophys Sin (Shanghai) 2012;44:394-406.
    • (2012) Acta Biochim Biophys Sin (Shanghai) , vol.44 , pp. 394-406
    • Ding, Y.1    Wu, Y.2    Zeng, R.3    Liao, K.4
  • 53
    • 84880036446 scopus 로고    scopus 로고
    • Balancing the fat: lipid droplets and human disease
    • Krahmer N, Farese RV, Jr., Walther TC. Balancing the fat: lipid droplets and human disease. EMBO Mol Med 2013;5:905-15.
    • (2013) EMBO Mol Med , vol.5 , pp. 905-915
    • Krahmer, N.1    Farese Jr, R.V.2    Walther, T.C.3
  • 54
    • 84856656225 scopus 로고    scopus 로고
    • Characterization of the lipid droplet proteome of a clonal insulin-producing beta-cell line (INS-1 832/13)
    • Larsson S, Resjo S, Gomez MF, James P, Holm C. Characterization of the lipid droplet proteome of a clonal insulin-producing beta-cell line (INS-1 832/13). J Proteome Res 2012;11:1264-73.
    • (2012) J Proteome Res , vol.11 , pp. 1264-1273
    • Larsson, S.1    Resjo, S.2    Gomez, M.F.3    James, P.4    Holm, C.5
  • 55
    • 0942287191 scopus 로고    scopus 로고
    • Chinese hamster ovary K2 cell lipid droplets appear to be metabolic organelles involved in membrane traffic
    • Liu P, Ying Y, Zhao Y, Mundy DI, Zhu M, Anderson RG. Chinese hamster ovary K2 cell lipid droplets appear to be metabolic organelles involved in membrane traffic. J Biol Chem 2004;279:3787-92.
    • (2004) J Biol Chem , vol.279 , pp. 3787-3792
    • Liu, P.1    Ying, Y.2    Zhao, Y.3    Mundy, D.I.4    Zhu, M.5    Anderson, R.G.6
  • 56
    • 84893666243 scopus 로고    scopus 로고
    • Rab GTPases Associate with Isolated Lipid Droplets (LDs) and Show Altered Content After Ethanol Administration: Potential Role in Alcohol-Impaired LD Metabolism
    • Rasineni K, McVicker BL, Tuma DJ, McNiven MA, Casey CA. Rab GTPases Associate with Isolated Lipid Droplets (LDs) and Show Altered Content After Ethanol Administration: Potential Role in Alcohol-Impaired LD Metabolism. Alcohol Clin Exp Res 2014;38:327-35.
    • (2014) Alcohol Clin Exp Res , vol.38 , pp. 327-335
    • Rasineni, K.1    McVicker, B.L.2    Tuma, D.J.3    McNiven, M.A.4    Casey, C.A.5
  • 57
    • 84884947695 scopus 로고    scopus 로고
    • Analysis of yeast lipid droplet proteome and lipidome
    • Schmidt C, Ploier B, Koch B, Daum G. Analysis of yeast lipid droplet proteome and lipidome. Methods Cell Biol 2013;116:15-37.
    • (2013) Methods Cell Biol , vol.116 , pp. 15-37
    • Schmidt, C.1    Ploier, B.2    Koch, B.3    Daum, G.4
  • 59
    • 84876551716 scopus 로고    scopus 로고
    • High fat diet feeding exaggerates perfluorooctanoic acidinduced liver injury in mice via modulating multiple metabolic pathways
    • Tan X, Xie G, Sun X, Li Q, Zhong W, Qiao P, et al. High fat diet feeding exaggerates perfluorooctanoic acidinduced liver injury in mice via modulating multiple metabolic pathways. PLoS One 2013;8:e61409.
    • (2013) PLoS One , vol.8
    • Tan, X.1    Xie, G.2    Sun, X.3    Li, Q.4    Zhong, W.5    Qiao, P.6
  • 60
    • 33746959419 scopus 로고    scopus 로고
    • Identification and characterization of associated with lipid droplet protein 1: A novel membrane-associated protein that resides on hepatic lipid droplets
    • Turro S, Ingelmo-Torres M, Estanyol JM, Tebar F, Fernandez MA, Albor CV, et al. Identification and characterization of associated with lipid droplet protein 1: A novel membrane-associated protein that resides on hepatic lipid droplets. Traffic 2006;7:1254-69.
    • (2006) Traffic , vol.7 , pp. 1254-1269
    • Turro, S.1    Ingelmo-Torres, M.2    Estanyol, J.M.3    Tebar, F.4    Fernandez, M.A.5    Albor, C.V.6
  • 62
    • 84857626057 scopus 로고    scopus 로고
    • Cytoskeleton disruption in J774 macrophages: consequences for lipid droplet formation and cholesterol flux
    • Weibel GL, Joshi MR, Jerome WG, Bates SR, Yu KJ, Phillips MC, et al. Cytoskeleton disruption in J774 macrophages: consequences for lipid droplet formation and cholesterol flux. Biochim Biophys Acta 2012;1821: 464-72.
    • (2012) Biochim Biophys Acta , vol.1821 , pp. 464-472
    • Weibel, G.L.1    Joshi, M.R.2    Jerome, W.G.3    Bates, S.R.4    Yu, K.J.5    Phillips, M.C.6
  • 63
    • 84880282714 scopus 로고    scopus 로고
    • Hepatitis B virus X protein upregulates oncogene Rab18 to result in the dysregulation of lipogenesis and proliferation of hepatoma cells
    • You X, Liu F, Zhang T, Li Y, Ye L, Zhang X. Hepatitis B virus X protein upregulates oncogene Rab18 to result in the dysregulation of lipogenesis and proliferation of hepatoma cells. Carcinogenesis 2013;34:1644-52.
    • (2013) Carcinogenesis , vol.34 , pp. 1644-1652
    • You, X.1    Liu, F.2    Zhang, T.3    Li, Y.4    Ye, L.5    Zhang, X.6
  • 64
    • 35748972649 scopus 로고    scopus 로고
    • SNARE proteins mediate fusion between cytosolic lipid droplets and are implicated in insulin sensitivity
    • Bostrom P, Andersson L, Rutberg M, Perman J, Lidberg U, Johansson BR, et al. SNARE proteins mediate fusion between cytosolic lipid droplets and are implicated in insulin sensitivity. Nat Cell Biol 2007;9:1286- 93.
    • (2007) Nat Cell Biol , vol.9 , pp. 1286-1293
    • Bostrom, P.1    Andersson, L.2    Rutberg, M.3    Perman, J.4    Lidberg, U.5    Johansson, B.R.6
  • 65
    • 67349280293 scopus 로고    scopus 로고
    • Lipid droplet-organelle interactions; sharing the fats
    • Murphy S, Martin S, Parton RG. Lipid droplet-organelle interactions; sharing the fats. Biochim Biophys Acta 2009;1791:441-7.
    • (2009) Biochim Biophys Acta , vol.1791 , pp. 441-447
    • Murphy, S.1    Martin, S.2    Parton, R.G.3
  • 66
    • 8744267532 scopus 로고    scopus 로고
    • Proteomic analysis of proteins associated with lipid droplets of basal and lipolytically stimulated 3T3-L1 adipocytes
    • Brasaemle DL, Dolios G, Shapiro L, Wang R. Proteomic analysis of proteins associated with lipid droplets of basal and lipolytically stimulated 3T3-L1 adipocytes. J Biol Chem 2004;279:46835-42.
    • (2004) J Biol Chem , vol.279
    • Brasaemle, D.L.1    Dolios, G.2    Shapiro, L.3    Wang, R.4
  • 67
    • 84871808790 scopus 로고    scopus 로고
    • Proteomic analysis of lipid droplets from Caco-2/TC7 enterocytes identifies novel modulators of lipid secretion
    • Beilstein F, Bouchoux J, Rousset M, Demignot S. Proteomic analysis of lipid droplets from Caco-2/TC7 enterocytes identifies novel modulators of lipid secretion. PLoS One 2013;8:e53017.
    • (2013) PLoS One , vol.8
    • Beilstein, F.1    Bouchoux, J.2    Rousset, M.3    Demignot, S.4
  • 68
    • 80053909233 scopus 로고    scopus 로고
    • Proteome of skeletal muscle lipid droplet reveals association with mitochondria and apolipoprotein a-I
    • Zhang H, Wang Y, Li J, Yu J, Pu J, Li L, et al. Proteome of skeletal muscle lipid droplet reveals association with mitochondria and apolipoprotein a-I. J Proteome Res 2011;10:4757-68.
    • (2011) J Proteome Res , vol.10 , pp. 4757-4768
    • Zhang, H.1    Wang, Y.2    Li, J.3    Yu, J.4    Pu, J.5    Li, L.6
  • 69
    • 84866143955 scopus 로고    scopus 로고
    • Perilipin family members preferentially sequester to either triacylglycerol-specific or cholesterylester- specific intracellular lipid storage droplets
    • Hsieh K, Lee YK, Londos C, Raaka BM, Dalen KT, Kimmel AR. Perilipin family members preferentially sequester to either triacylglycerol-specific or cholesterylester- specific intracellular lipid storage droplets. J Cell Sci 2012;125:4067-76.
    • (2012) J Cell Sci , vol.125 , pp. 4067-4076
    • Hsieh, K.1    Lee, Y.K.2    Londos, C.3    Raaka, B.M.4    Dalen, K.T.5    Kimmel, A.R.6
  • 70
    • 29644442801 scopus 로고    scopus 로고
    • Regulated localization of Rab18 to lipid droplets: effects of lipolytic stimulation and inhibition of lipid droplet catabolism
    • Martin S, Driessen K, Nixon SJ, Zerial M, Parton RG. Regulated localization of Rab18 to lipid droplets: effects of lipolytic stimulation and inhibition of lipid droplet catabolism. J Biol Chem 2005;280:42325-35.
    • (2005) J Biol Chem , vol.280
    • Martin, S.1    Driessen, K.2    Nixon, S.J.3    Zerial, M.4    Parton, R.G.5
  • 71
    • 21644459401 scopus 로고    scopus 로고
    • Rab18 localizes to lipid droplets and induces their close apposition to the endoplasmic reticulum- derived membrane
    • Ozeki S, Cheng J, Tauchi-Sato K, Hatano N, Taniguchi H, Fujimoto T. Rab18 localizes to lipid droplets and induces their close apposition to the endoplasmic reticulum- derived membrane. J Cell Sci 2005;118:2601- 11.
    • (2005) J Cell Sci , vol.118 , pp. 2601-2611
    • Ozeki, S.1    Cheng, J.2    Tauchi-Sato, K.3    Hatano, N.4    Taniguchi, H.5    Fujimoto, T.6
  • 74
    • 45549084407 scopus 로고    scopus 로고
    • Characterization of Rab18, a lipid droplet-associated small GTPase
    • Martin S, Parton RG. Characterization of Rab18, a lipid droplet-associated small GTPase. Methods Enzymol 2008;438:109-29.
    • (2008) Methods Enzymol , vol.438 , pp. 109-129
    • Martin, S.1    Parton, R.G.2
  • 75
    • 84872046952 scopus 로고    scopus 로고
    • Nutritional, hormonal, and depot-dependent regulation of the expression of the small GTPase Rab18 in rodent adipose tissue
    • Pulido MR, Rabanal-Ruiz Y, Almabouada F, Diaz-Ruiz A, Burrell MA, Vazquez MJ, et al. Nutritional, hormonal, and depot-dependent regulation of the expression of the small GTPase Rab18 in rodent adipose tissue. J Mol Endocrinol 2012;50:19-29.
    • (2012) J Mol Endocrinol , vol.50 , pp. 19-29
    • Pulido, M.R.1    Rabanal-Ruiz, Y.2    Almabouada, F.3    Diaz-Ruiz, A.4    Burrell, M.A.5    Vazquez, M.J.6
  • 76
    • 84891457161 scopus 로고    scopus 로고
    • Bidirectional Lipid Droplet Velocities Are Controlled by Differential Binding Strengths of HCV Core DII Protein
    • Lyn RK, Hope G, Sherratt AR, McLauchlan J, Pezacki JP. Bidirectional Lipid Droplet Velocities Are Controlled by Differential Binding Strengths of HCV Core DII Protein. PLoS One 2013;8:e78065.
    • (2013) PLoS One , vol.8
    • Lyn, R.K.1    Hope, G.2    Sherratt, A.R.3    McLauchlan, J.4    Pezacki, J.P.5
  • 77
    • 84861152007 scopus 로고    scopus 로고
    • Postlipolytic insulin-dependent remodeling of micro lipid droplets in adipocytes
    • Ariotti N, Murphy S, Hamilton NA, Wu L, Green K, Schieber NL, et al. Postlipolytic insulin-dependent remodeling of micro lipid droplets in adipocytes. Mol Biol Cell 2012;23:1826-37.
    • (2012) Mol Biol Cell , vol.23 , pp. 1826-1837
    • Ariotti, N.1    Murphy, S.2    Hamilton, N.A.3    Wu, L.4    Green, K.5    Schieber, N.L.6
  • 78
    • 84887898571 scopus 로고    scopus 로고
    • Long-term live cell microscopy studies of lipid droplet fusion dynamics in adipocytes
    • Jungst C, Klein M, Zumbusch A. Long-term live cell microscopy studies of lipid droplet fusion dynamics in adipocytes. J Lipid Res 2013;54:3419-29.
    • (2013) J Lipid Res , vol.54 , pp. 3419-3429
    • Jungst, C.1    Klein, M.2    Zumbusch, A.3
  • 79
    • 79956293511 scopus 로고    scopus 로고
    • Fast and long term lipid droplet tracking with CARS microscopy
    • Jungst C, Winterhalder MJ, Zumbusch A. Fast and long term lipid droplet tracking with CARS microscopy. J Biophotonics 2011;4:435-41.
    • (2011) J Biophotonics , vol.4 , pp. 435-441
    • Jungst, C.1    Winterhalder, M.J.2    Zumbusch, A.3
  • 80
    • 84883350018 scopus 로고    scopus 로고
    • Rab18 binds to hepatitis C virus NS5A and promotes interaction between sites of viral replication and lipid droplets
    • Salloum S, Wang H, Ferguson C, Parton RG, Tai AW. Rab18 binds to hepatitis C virus NS5A and promotes interaction between sites of viral replication and lipid droplets. PLoS Pathog 2013;9:e1003513.
    • (2013) PLoS Pathog , vol.9
    • Salloum, S.1    Wang, H.2    Ferguson, C.3    Parton, R.G.4    Tai, A.W.5
  • 82
    • 84870203239 scopus 로고    scopus 로고
    • RAB3GAP1, RAB3GAP2 and RAB18: disease genes in Micro and Martsolf syndromes
    • Handley MT, Aligianis IA. RAB3GAP1, RAB3GAP2 and RAB18: disease genes in Micro and Martsolf syndromes. Biochem Soc Trans 2012;40:1394-7.
    • (2012) Biochem Soc Trans , vol.40 , pp. 1394-1397
    • Handley, M.T.1    Aligianis, I.A.2
  • 83
    • 84876322332 scopus 로고    scopus 로고
    • Mutation spectrum in RAB3GAP1, RAB3GAP2, and RAB18 and genotypephenotype correlations in warburg micro syndrome and Martsolf syndrome
    • Handley MT, Morris-Rosendahl DJ, Brown S, Macdonald F, Hardy C, Bem D, et al. Mutation spectrum in RAB3GAP1, RAB3GAP2, and RAB18 and genotypephenotype correlations in warburg micro syndrome and Martsolf syndrome. Hum Mutat 2013;34:686-96.
    • (2013) Hum Mutat , vol.34 , pp. 686-696
    • Handley, M.T.1    Morris-Rosendahl, D.J.2    Brown, S.3    Macdonald, F.4    Hardy, C.5    Bem, D.6
  • 85
    • 0034525907 scopus 로고    scopus 로고
    • A rab1 GTPase is required for transport between the endoplasmic reticulum and golgi apparatus and for normal golgi movement in plants
    • Batoko H, Zheng HQ, Hawes C, Moore I. A rab1 GTPase is required for transport between the endoplasmic reticulum and golgi apparatus and for normal golgi movement in plants. Plant Cell 2000;12:2201-18.
    • (2000) Plant Cell , vol.12 , pp. 2201-2218
    • Batoko, H.1    Zheng, H.Q.2    Hawes, C.3    Moore, I.4
  • 86
    • 77955239270 scopus 로고    scopus 로고
    • Autophagosome formation depends on the small GTPase Rab1 and functional ER exit sites
    • Zoppino FC, Militello RD, Slavin I, Alvarez C, Colombo MI. Autophagosome formation depends on the small GTPase Rab1 and functional ER exit sites. Traffic 2010;11: 1246-61.
    • (2010) Traffic , vol.11 , pp. 1246-1261
    • Zoppino, F.C.1    Militello, R.D.2    Slavin, I.3    Alvarez, C.4    Colombo, M.I.5
  • 88
    • 0034698202 scopus 로고    scopus 로고
    • Rab1 recruitment of p115 into a cis-SNARE complex: programming budding COPII vesicles for fusion
    • Allan BB, Moyer BD, Balch WE. Rab1 recruitment of p115 into a cis-SNARE complex: programming budding COPII vesicles for fusion. Science 2000;289:444-8.
    • (2000) Science , vol.289 , pp. 444-448
    • Allan, B.B.1    Moyer, B.D.2    Balch, W.E.3
  • 89
    • 0035024551 scopus 로고    scopus 로고
    • Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis- Golgi tethering
    • Moyer BD, Allan BB, Balch WE. Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis- Golgi tethering. Traffic 2001;2:268-76.
    • (2001) Traffic , vol.2 , pp. 268-276
    • Moyer, B.D.1    Allan, B.B.2    Balch, W.E.3
  • 91
    • 84864007958 scopus 로고    scopus 로고
    • Role for TBC1D20 and Rab1 in hepatitis C virus replication via interaction with lipid droplet-bound nonstructural protein 5A
    • Nevo-Yassaf I, Yaffe Y, Asher M, Ravid O, Eizenberg S, Henis YI et al. Role for TBC1D20 and Rab1 in hepatitis C virus replication via interaction with lipid droplet-bound nonstructural protein 5A. J Virol 2012;86:6491-6502.
    • (2012) J Virol , vol.86 , pp. 6491-6502
    • Nevo-Yassaf, I.1    Yaffe, Y.2    Asher, M.3    Ravid, O.4    Eizenberg, S.5    Henis, Y.I6
  • 93
    • 67649470529 scopus 로고    scopus 로고
    • Reconstitution of Rab- and SNAREdependent membrane fusion by synthetic endosomes
    • Ohya T, Miaczynska M, Coskun U, Lommer B, Runge A, Drechsel D, et al. Reconstitution of Rab- and SNAREdependent membrane fusion by synthetic endosomes. Nature 2012;459:1091-7.
    • (2012) Nature , vol.459 , pp. 1091-1097
    • Ohya, T.1    Miaczynska, M.2    Coskun, U.3    Lommer, B.4    Runge, A.5    Drechsel, D.6
  • 94
    • 79960557412 scopus 로고    scopus 로고
    • Membrane dynamics and fusion at late endosomes and vacuoles-Rab regulation, multisubunit tethering complexes and SNAREs
    • Epp N, Rethmeier R, Kramer L, Ungermann C. Membrane dynamics and fusion at late endosomes and vacuoles-Rab regulation, multisubunit tethering complexes and SNAREs. Eur J Cell Biol 2011;90:779- 85.
    • (2011) Eur J Cell Biol , vol.90 , pp. 779-785
    • Epp, N.1    Rethmeier, R.2    Kramer, L.3    Ungermann, C.4
  • 96
    • 45549097639 scopus 로고    scopus 로고
    • Rabregulated membrane traffic between adiposomes and multiple endomembrane systems
    • Liu P, Bartz R., Zehmer JK, Ying Y, Anderson RG. Rabregulated membrane traffic between adiposomes and multiple endomembrane systems. Methods Enzymol 2008;439:327-37.
    • (2008) Methods Enzymol , vol.439 , pp. 327-337
    • Liu, P.1    Bartz, R.2    Zehmer, J.K.3    Ying, Y.4    Anderson, R.G.5
  • 97
    • 76049106065 scopus 로고    scopus 로고
    • Endocytic Rab proteins are required for hepatitis C virus replication complex formation
    • Manna D, Aligo J, Xu C, ParkWS, Koc H, HeoWD, Konan KV. Endocytic Rab proteins are required for hepatitis C virus replication complex formation. Virology 2010; 398:21-37.
    • (2010) Virology , vol.398 , pp. 21-37
    • Manna, D.1    Aligo, J.2    Xu, C.3    Park, W.S.4    Koc, H.5    Heo, W.D.6    Konan, K.V.7
  • 98
    • 84893742386 scopus 로고    scopus 로고
    • Rab7 Is Functionally Required for Selective Cargo Sorting at the Early Endosome
    • Girard E, Chmiest D, Fournier N, Johannes L, Paul JL, Vedie B, et al. Rab7 Is Functionally Required for Selective Cargo Sorting at the Early Endosome. Traffic 2013;15:309-26.
    • (2013) Traffic , vol.15 , pp. 309-326
    • Girard, E.1    Chmiest, D.2    Fournier, N.3    Johannes, L.4    Paul, J.L.5    Vedie, B.6
  • 99
    • 84865365335 scopus 로고    scopus 로고
    • Rab GTPases regulating receptor trafficking at the late endosome-lysosome membranes
    • Ng EL, Gan BQ, Ng F, Tang BL. Rab GTPases regulating receptor trafficking at the late endosome-lysosome membranes. Cell Biochem Funct 2012;30:515-23.
    • (2012) Cell Biochem Funct , vol.30 , pp. 515-523
    • Ng, E.L.1    Gan, B.Q.2    Ng, F.3    Tang, B.L.4
  • 100
    • 66449123730 scopus 로고    scopus 로고
    • Rab7 regulates late endocytic trafficking downstream of multivesicular body biogenesis and cargo sequestration
    • Vanlandingham PA, Ceresa BP. Rab7 regulates late endocytic trafficking downstream of multivesicular body biogenesis and cargo sequestration. J Biol Chem 2009;284: 12110-24.
    • (2009) J Biol Chem , vol.284
    • Vanlandingham, P.A.1    Ceresa, B.P.2
  • 101
    • 77951918362 scopus 로고    scopus 로고
    • Identification of the switch in early-to-late endosome transition
    • Poteryaev D, Datta S, Ackema K, Zerial M, Spang A. Identification of the switch in early-to-late endosome transition. Cell 2010;141:497-508.
    • (2010) Cell , vol.141 , pp. 497-508
    • Poteryaev, D.1    Datta, S.2    Ackema, K.3    Zerial, M.4    Spang, A.5
  • 102
    • 84859863392 scopus 로고    scopus 로고
    • A hypothetical model of cargoselective rab recruitment during organelle maturation
    • Binder B, Holzhutter HG. A hypothetical model of cargoselective rab recruitment during organelle maturation. Cell Biochem Biophys 2012;63:59-71.
    • (2012) Cell Biochem Biophys , vol.63 , pp. 59-71
    • Binder, B.1    Holzhutter, H.G.2
  • 103
    • 84883382591 scopus 로고    scopus 로고
    • Late endosomal transport and tethering are coupled processes controlled by RILP and the cholesterol sensor ORP1L.
    • van der Kant, R, Fish A, Janssen L, Janssen H, Krom S, Ho N, et al. Late endosomal transport and tethering are coupled processes controlled by RILP and the cholesterol sensor ORP1L. J Cell Sci 2013:126:3462-74.
    • (2013) J Cell Sci , vol.126 , pp. 3462-3474
    • van der Kant, R.1    Fish, A.2    Janssen, L.3    Janssen, H.4    Krom, S.5    Ho, N.6


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