메뉴 건너뛰기




Volumn 33, Issue 5, 2015, Pages 603-610

Lipid Droplets Are Essential for Efficient Clearance of Cytosolic Inclusion Bodies

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MARKER; FAT DROPLET; HEAT SHOCK PROTEIN 104; HEAT SHOCK PROTEIN 26; TAUROURSODEOXYCHOLIC ACID; TRIACYLGLYCEROL; SACCHAROMYCES CEREVISIAE PROTEIN; STEROL;

EID: 84930577438     PISSN: 15345807     EISSN: 18781551     Source Type: Journal    
DOI: 10.1016/j.devcel.2015.04.015     Document Type: Article
Times cited : (93)

References (46)
  • 1
    • 84921936587 scopus 로고    scopus 로고
    • Dynamic droplets: the role of cytoplasmic inclusions in stress, function, and disease
    • Amen T., Kaganovich D. Dynamic droplets: the role of cytoplasmic inclusions in stress, function, and disease. Cell. Mol. Life Sci. 2015, 72:401-415.
    • (2015) Cell. Mol. Life Sci. , vol.72 , pp. 401-415
    • Amen, T.1    Kaganovich, D.2
  • 2
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh E.G., Dyer W.J. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 1959, 37:911-917.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 3
    • 84876305060 scopus 로고    scopus 로고
    • A novel single-cell screening platform reveals proteome plasticity during yeast stress responses
    • Breker M., Gymrek M., Schuldiner M. A novel single-cell screening platform reveals proteome plasticity during yeast stress responses. J.Cell Biol. 2013, 200:839-850.
    • (2013) J.Cell Biol. , vol.200 , pp. 839-850
    • Breker, M.1    Gymrek, M.2    Schuldiner, M.3
  • 4
    • 9244263009 scopus 로고    scopus 로고
    • The chemical chaperone proline relieves the thermosensitivity of a dnaK deletion mutant at 42 degrees C
    • Chattopadhyay M.K., Kern R., Mistou M.Y., Dandekar A.M., Uratsu S.L., Richarme G. The chemical chaperone proline relieves the thermosensitivity of a dnaK deletion mutant at 42 degrees C. J.Bacteriol. 2004, 186:8149-8152.
    • (2004) J.Bacteriol. , vol.186 , pp. 8149-8152
    • Chattopadhyay, M.K.1    Kern, R.2    Mistou, M.Y.3    Dandekar, A.M.4    Uratsu, S.L.5    Richarme, G.6
  • 5
    • 80054723502 scopus 로고    scopus 로고
    • Advanced methods for high-throughput microscopy screening of genetically modified yeast libraries
    • Cohen Y., Schuldiner M. Advanced methods for high-throughput microscopy screening of genetically modified yeast libraries. Methods Mol. Biol. 2011, 781:127-159.
    • (2011) Methods Mol. Biol. , vol.781 , pp. 127-159
    • Cohen, Y.1    Schuldiner, M.2
  • 6
  • 7
    • 0037155197 scopus 로고    scopus 로고
    • Lipid droplet binding and oligomerization properties of the Parkinson's disease protein alpha-synuclein
    • Cole N.B., Murphy D.D., Grider T., Rueter S., Brasaemle D., Nussbaum R.L. Lipid droplet binding and oligomerization properties of the Parkinson's disease protein alpha-synuclein. J.Biol. Chem. 2002, 277:6344-6352.
    • (2002) J.Biol. Chem. , vol.277 , pp. 6344-6352
    • Cole, N.B.1    Murphy, D.D.2    Grider, T.3    Rueter, S.4    Brasaemle, D.5    Nussbaum, R.L.6
  • 9
    • 84885095437 scopus 로고    scopus 로고
    • Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress
    • Escusa-Toret S., Vonk W.I., Frydman J. Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress. Nat. Cell Biol. 2013, 15:1231-1243.
    • (2013) Nat. Cell Biol. , vol.15 , pp. 1231-1243
    • Escusa-Toret, S.1    Vonk, W.I.2    Frydman, J.3
  • 10
    • 17644396667 scopus 로고    scopus 로고
    • Degradation-mediated protein quality control in the nucleus
    • Gardner R.G., Nelson Z.W., Gottschling D.E. Degradation-mediated protein quality control in the nucleus. Cell 2005, 120:803-815.
    • (2005) Cell , vol.120 , pp. 803-815
    • Gardner, R.G.1    Nelson, Z.W.2    Gottschling, D.E.3
  • 11
    • 33847732649 scopus 로고    scopus 로고
    • Ultrastructural localization of intraneuronal Abeta-peptide in Alzheimer disease brains
    • Gómez-Ramos P., Asunción Morán M. Ultrastructural localization of intraneuronal Abeta-peptide in Alzheimer disease brains. J.Alzheimers Dis. 2007, 11:53-59.
    • (2007) J.Alzheimers Dis. , vol.11 , pp. 53-59
    • Gómez-Ramos, P.1    Asunción Morán, M.2
  • 12
    • 77953530388 scopus 로고    scopus 로고
    • Sterol-induced dislocation of 3-hydroxy-3-methylglutaryl coenzyme A reductase from endoplasmic reticulum membranes into the cytosol through a subcellular compartment resembling lipid droplets
    • Hartman I.Z., Liu P., Zehmer J.K., Luby-Phelps K., Jo Y., Anderson R.G., DeBose-Boyd R.A. Sterol-induced dislocation of 3-hydroxy-3-methylglutaryl coenzyme A reductase from endoplasmic reticulum membranes into the cytosol through a subcellular compartment resembling lipid droplets. J.Biol. Chem. 2010, 285:19288-19298.
    • (2010) J.Biol. Chem. , vol.285 , pp. 19288-19298
    • Hartman, I.Z.1    Liu, P.2    Zehmer, J.K.3    Luby-Phelps, K.4    Jo, Y.5    Anderson, R.G.6    DeBose-Boyd, R.A.7
  • 13
    • 21244497886 scopus 로고    scopus 로고
    • Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104
    • Haslbeck M., Miess A., Stromer T., Walter S., Buchner J. Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104. J.Biol. Chem. 2005, 280:23861-23868.
    • (2005) J.Biol. Chem. , vol.280 , pp. 23861-23868
    • Haslbeck, M.1    Miess, A.2    Stromer, T.3    Walter, S.4    Buchner, J.5
  • 14
    • 84902666176 scopus 로고    scopus 로고
    • Life-span extension by a metacaspase in the yeast Saccharomyces cerevisiae
    • Hill S.M., Hao X., Liu B., Nyström T. Life-span extension by a metacaspase in the yeast Saccharomyces cerevisiae. Science 2014, 344:1389-1392.
    • (2014) Science , vol.344 , pp. 1389-1392
    • Hill, S.M.1    Hao, X.2    Liu, B.3    Nyström, T.4
  • 16
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich D., Kopito R., Frydman J. Misfolded proteins partition between two distinct quality control compartments. Nature 2008, 454:1088-1095.
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 17
    • 67849103757 scopus 로고    scopus 로고
    • SAM-T08, HMM-based protein structure prediction
    • Karplus K. SAM-T08, HMM-based protein structure prediction. Nucleic Acids Res. 2009, 37:W492-W497.
    • (2009) Nucleic Acids Res. , vol.37 , pp. W492-W497
    • Karplus, K.1
  • 19
    • 14044272811 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae YLL012/YEH1, YLR020/YEH2, and TGL1 genes encode a novel family of membrane-anchored lipases that are required for steryl ester hydrolysis
    • Köffel R., Tiwari R., Falquet L., Schneiter R. The Saccharomyces cerevisiae YLL012/YEH1, YLR020/YEH2, and TGL1 genes encode a novel family of membrane-anchored lipases that are required for steryl ester hydrolysis. Mol. Cell. Biol. 2005, 25:1655-1668.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 1655-1668
    • Köffel, R.1    Tiwari, R.2    Falquet, L.3    Schneiter, R.4
  • 20
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito R.R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 2000, 10:524-530.
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 22
    • 0032519345 scopus 로고    scopus 로고
    • Differential screening and suppression subtractive hybridization identified genes differentially expressed in an estrogen receptor-positive breast carcinoma cell line
    • Kuang W.W., Thompson D.A., Hoch R.V., Weigel R.J. Differential screening and suppression subtractive hybridization identified genes differentially expressed in an estrogen receptor-positive breast carcinoma cell line. Nucleic Acids Res. 1998, 26:1116-1123.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1116-1123
    • Kuang, W.W.1    Thompson, D.A.2    Hoch, R.V.3    Weigel, R.J.4
  • 23
    • 84920724964 scopus 로고    scopus 로고
    • Storage lipid synthesis is necessary for autophagy induced by nitrogen starvation
    • Li D., Song J.Z., Li H., Shan M.H., Liang Y., Zhu J., Xie Z. Storage lipid synthesis is necessary for autophagy induced by nitrogen starvation. FEBS Lett. 2015, 589:269-276.
    • (2015) FEBS Lett. , vol.589 , pp. 269-276
    • Li, D.1    Song, J.Z.2    Li, H.3    Shan, M.H.4    Liang, Y.5    Zhu, J.6    Xie, Z.7
  • 24
    • 84865277422 scopus 로고    scopus 로고
    • Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates
    • Malinovska L., Kroschwald S., Munder M.C., Richter D., Alberti S. Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates. Mol. Biol. Cell 2012, 23:3041-3056.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 3041-3056
    • Malinovska, L.1    Kroschwald, S.2    Munder, M.C.3    Richter, D.4    Alberti, S.5
  • 26
    • 20444413061 scopus 로고    scopus 로고
    • Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways
    • McClellan A.J., Scott M.D., Frydman J. Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways. Cell 2005, 121:739-748.
    • (2005) Cell , vol.121 , pp. 739-748
    • McClellan, A.J.1    Scott, M.D.2    Frydman, J.3
  • 28
    • 33744755382 scopus 로고    scopus 로고
    • Cytoplasmic lipid droplets are sites of convergence of proteasomal and autophagic degradation of apolipoprotein B
    • Ohsaki Y., Cheng J., Fujita A., Tokumoto T., Fujimoto T. Cytoplasmic lipid droplets are sites of convergence of proteasomal and autophagic degradation of apolipoprotein B. Mol. Biol. Cell 2006, 17:2674-2683.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2674-2683
    • Ohsaki, Y.1    Cheng, J.2    Fujita, A.3    Tokumoto, T.4    Fujimoto, T.5
  • 29
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell D.A., Kowal A.S., Singer M.A., Lindquist S. Protein disaggregation mediated by heat-shock protein Hsp104. Nature 1994, 372:475-478.
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 32
    • 80053062569 scopus 로고    scopus 로고
    • Interactomic study on interaction between lipid droplets and mitochondria
    • Pu J., Ha C.W., Zhang S., Jung J.P., Huh W.K., Liu P. Interactomic study on interaction between lipid droplets and mitochondria. Protein Cell 2011, 2:487-496.
    • (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
  • 33
    • 84896855937 scopus 로고    scopus 로고
    • Aphosphatidylinositol transfer protein integrates phosphoinositide signaling with lipid droplet metabolism to regulate a developmental program of nutrient stress-induced membrane biogenesis
    • Ren J., Pei-Chen Lin C., Pathak M.C., Temple B.R., Nile A.H., Mousley C.J., Duncan M.C., Eckert D.M., Leiker T.J., Ivanova P.T., et al. Aphosphatidylinositol transfer protein integrates phosphoinositide signaling with lipid droplet metabolism to regulate a developmental program of nutrient stress-induced membrane biogenesis. Mol. Biol. Cell 2014, 25:712-727.
    • (2014) Mol. Biol. Cell , vol.25 , pp. 712-727
    • Ren, J.1    Pei-Chen Lin, C.2    Pathak, M.C.3    Temple, B.R.4    Nile, A.H.5    Mousley, C.J.6    Duncan, M.C.7    Eckert, D.M.8    Leiker, T.J.9    Ivanova, P.T.10
  • 36
    • 81355149538 scopus 로고    scopus 로고
    • Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae
    • Specht S., Miller S.B., Mogk A., Bukau B. Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae. J.Cell Biol. 2011, 195:617-629.
    • (2011) J.Cell Biol. , vol.195 , pp. 617-629
    • Specht, S.1    Miller, S.B.2    Mogk, A.3    Bukau, B.4
  • 37
    • 84868149498 scopus 로고    scopus 로고
    • Confinement to organelle-associated inclusion structures mediates asymmetric inheritance of aggregated protein in budding yeast
    • Spokoini R., Moldavski O., Nahmias Y., England J.L., Schuldiner M., Kaganovich D. Confinement to organelle-associated inclusion structures mediates asymmetric inheritance of aggregated protein in budding yeast. Cell Rep. 2012, 2:738-747.
    • (2012) Cell Rep. , vol.2 , pp. 738-747
    • Spokoini, R.1    Moldavski, O.2    Nahmias, Y.3    England, J.L.4    Schuldiner, M.5    Kaganovich, D.6
  • 38
    • 34548680957 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation analysis system for invivo detection of protein-protein interaction in Saccharomyces cerevisiae
    • Sung M.K., Huh W.K. Bimolecular fluorescence complementation analysis system for invivo detection of protein-protein interaction in Saccharomyces cerevisiae. Yeast 2007, 24:767-775.
    • (2007) Yeast , vol.24 , pp. 767-775
    • Sung, M.K.1    Huh, W.K.2
  • 42
    • 33644807842 scopus 로고    scopus 로고
    • Synthetic genetic array analysis in Saccharomyces cerevisiae
    • Tong A.H., Boone C. Synthetic genetic array analysis in Saccharomyces cerevisiae. Methods Mol. Biol. 2006, 313:171-192.
    • (2006) Methods Mol. Biol. , vol.313 , pp. 171-192
    • Tong, A.H.1    Boone, C.2
  • 43
    • 0000942202 scopus 로고    scopus 로고
    • PDR16 and PDR17, two homologous genes of Saccharomyces cerevisiae, affect lipid biosynthesis and resistance to multiple drugs
    • van den Hazel H.B., Pichler H., do Valle Matta M.A., Leitner E., Goffeau A., Daum G. PDR16 and PDR17, two homologous genes of Saccharomyces cerevisiae, affect lipid biosynthesis and resistance to multiple drugs. J.Biol. Chem. 1999, 274:1934-1941.
    • (1999) J.Biol. Chem. , vol.274 , pp. 1934-1941
    • van den Hazel, H.B.1    Pichler, H.2    do Valle Matta, M.A.3    Leitner, E.4    Goffeau, A.5    Daum, G.6
  • 44
    • 84861913952 scopus 로고    scopus 로고
    • Lipid droplets and cellular lipid metabolism
    • Walther T.C., Farese R.V. Lipid droplets and cellular lipid metabolism. Annu. Rev. Biochem. 2012, 81:687-714.
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 687-714
    • Walther, T.C.1    Farese, R.V.2
  • 46
    • 34548514866 scopus 로고    scopus 로고
    • Proteins under new management: lipid droplets deliver
    • Welte M.A. Proteins under new management: lipid droplets deliver. Trends Cell Biol. 2007, 17:363-369.
    • (2007) Trends Cell Biol. , vol.17 , pp. 363-369
    • Welte, M.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.