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Volumn 21, Issue 7, 2010, Pages 719-726

Chaperone-mediated autophagy: Molecular mechanisms and physiological relevance

Author keywords

Chaperones; Lysosomes; Membrane proteins; Proteases; Protein translocation; Proteolysis

Indexed keywords

CHAPERONE; LIPID; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2; PROTEIN;

EID: 77956178939     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.semcdb.2010.02.005     Document Type: Review
Times cited : (220)

References (53)
  • 1
    • 34249019920 scopus 로고    scopus 로고
    • Intracellular protein degradation: from a vague idea through the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting
    • Ciechanover A. Intracellular protein degradation: from a vague idea through the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Hematol Am Soc Hematol Educ Program 2006, 1:505-506.
    • (2006) Hematol Am Soc Hematol Educ Program , vol.1 , pp. 505-506
    • Ciechanover, A.1
  • 3
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg A.L. Protein degradation and protection against misfolded or damaged proteins. Nature 2003, 18:895-899.
    • (2003) Nature , vol.18 , pp. 895-899
    • Goldberg, A.L.1
  • 4
    • 70349924078 scopus 로고    scopus 로고
    • Links between autophagy, innate immunity, inflammation and Crohn's disease
    • Deretic V. Links between autophagy, innate immunity, inflammation and Crohn's disease. Dig Dis 2009, 27:246-251.
    • (2009) Dig Dis , vol.27 , pp. 246-251
    • Deretic, V.1
  • 5
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem 2009, 78:477-513.
    • (2009) Annu Rev Biochem , vol.78 , pp. 477-513
    • Finley, D.1
  • 6
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He C., Klionsky D.J. Regulation mechanisms and signaling pathways of autophagy. Annu Rev Genet 2009, 43:67-93.
    • (2009) Annu Rev Genet , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 7
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N., Levine B., Cuervo A.M., Klionsky D.J. Autophagy fights disease through cellular self-digestion. Nature 2008, 451:1069-1075.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 8
    • 0004103749 scopus 로고    scopus 로고
    • Molecular Biology Intelligence Unit, Landes Bioscience, Austin, TX
    • Dice J. Lysosomal pathways of protein degradation 2000, Molecular Biology Intelligence Unit, Landes Bioscience, Austin, TX.
    • (2000) Lysosomal pathways of protein degradation
    • Dice, J.1
  • 9
    • 0021967444 scopus 로고
    • Uptake - microautophagy - and degradation of exogenous proteins by isolated rat liver lysosomes. Effects of pH, ATP, and inhibitors of proteolysis
    • Ahlberg J., Glaumann H. Uptake - microautophagy - and degradation of exogenous proteins by isolated rat liver lysosomes. Effects of pH, ATP, and inhibitors of proteolysis. Exp Mol Pathol 1985, 42:78-88.
    • (1985) Exp Mol Pathol , vol.42 , pp. 78-88
    • Ahlberg, J.1    Glaumann, H.2
  • 10
    • 34250822281 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy
    • Dice J. Chaperone-mediated autophagy. Autophagy 2007, 3:295-299.
    • (2007) Autophagy , vol.3 , pp. 295-299
    • Dice, J.1
  • 11
    • 77949328788 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: selectivity pays off
    • Cuervo A.M. Chaperone-mediated autophagy: selectivity pays off. Trends Endocrinol Metab 2009, 21:142-150.
    • (2009) Trends Endocrinol Metab , vol.21 , pp. 142-150
    • Cuervo, A.M.1
  • 12
    • 0142009674 scopus 로고    scopus 로고
    • Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions
    • Fuertes G., Martin De Llano J., Villarroya A., Rivett A., Knecht E. Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions. Biochem J 2003, 375:75-86.
    • (2003) Biochem J , vol.375 , pp. 75-86
    • Fuertes, G.1    Martin De Llano, J.2    Villarroya, A.3    Rivett, A.4    Knecht, E.5
  • 14
    • 19344373577 scopus 로고    scopus 로고
    • Lamp-2a facilitates MHC class II presentation of cytoplasmic antigens
    • Zhou D., Li P., Lin Y., Lott J.M., Hislop A.D., Canaday D.H., et al. Lamp-2a facilitates MHC class II presentation of cytoplasmic antigens. Immunity 2005, 22:571-581.
    • (2005) Immunity , vol.22 , pp. 571-581
    • Zhou, D.1    Li, P.2    Lin, Y.3    Lott, J.M.4    Hislop, A.D.5    Canaday, D.H.6
  • 15
    • 0025294506 scopus 로고
    • Peptide sequences that target cytosolic proteins for lysosomal proteolysis
    • Dice J. Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends Biochem Sci 1990, 15:305-309.
    • (1990) Trends Biochem Sci , vol.15 , pp. 305-309
    • Dice, J.1
  • 16
    • 0023891846 scopus 로고
    • Peptide sequences that target proteins for enhanced degradation during serum withdrawal
    • Chiang H., Dice J. Peptide sequences that target proteins for enhanced degradation during serum withdrawal. J Biol Chem 1988, 263:6797-6803.
    • (1988) J Biol Chem , vol.263 , pp. 6797-6803
    • Chiang, H.1    Dice, J.2
  • 17
    • 0024975155 scopus 로고
    • A role for a 70kDa heat shock protein in lysosomal degradation of intracellular protein
    • Chiang H., Terlecky S., Plant C., Dice J. A role for a 70kDa heat shock protein in lysosomal degradation of intracellular protein. Science 1989, 246:382-385.
    • (1989) Science , vol.246 , pp. 382-385
    • Chiang, H.1    Terlecky, S.2    Plant, C.3    Dice, J.4
  • 18
    • 0034914206 scopus 로고    scopus 로고
    • A molecular chaperone complex at the lysosomal membrane is required for protein translocation
    • Agarraberes F., Dice J.F. A molecular chaperone complex at the lysosomal membrane is required for protein translocation. J Cell Sci 2001, 114:2491-2499.
    • (2001) J Cell Sci , vol.114 , pp. 2491-2499
    • Agarraberes, F.1    Dice, J.F.2
  • 19
    • 0031041902 scopus 로고    scopus 로고
    • A lysosomal population responsible for the hsc73-mediated degradation of cytosolic proteins in lysosomes
    • Cuervo A., Dice J., Knecht E. A lysosomal population responsible for the hsc73-mediated degradation of cytosolic proteins in lysosomes. J Biol Chem 1997, 272:5606-5615.
    • (1997) J Biol Chem , vol.272 , pp. 5606-5615
    • Cuervo, A.1    Dice, J.2    Knecht, E.3
  • 20
    • 0030923854 scopus 로고    scopus 로고
    • An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation
    • Agarraberes F., Terlecky S., Dice J. An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation. J Cell Biol 1997, 137:825-834.
    • (1997) J Cell Biol , vol.137 , pp. 825-834
    • Agarraberes, F.1    Terlecky, S.2    Dice, J.3
  • 21
    • 0028848119 scopus 로고
    • Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation
    • Cuervo A., Knecht E., Terlecky S., Dice J. Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation. Am J Physiol 1995, 269:C1200-C1208.
    • (1995) Am J Physiol , vol.269
    • Cuervo, A.1    Knecht, E.2    Terlecky, S.3    Dice, J.4
  • 22
    • 6344275803 scopus 로고    scopus 로고
    • Activation of chaperone-mediated autophagy during oxidative stress
    • Kiffin R., Christian C., Knecht E., Cuervo A.M. Activation of chaperone-mediated autophagy during oxidative stress. Mol Biol Cell 2004, 15:4829-4840.
    • (2004) Mol Biol Cell , vol.15 , pp. 4829-4840
    • Kiffin, R.1    Christian, C.2    Knecht, E.3    Cuervo, A.M.4
  • 23
    • 51349130544 scopus 로고    scopus 로고
    • The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane
    • Bandyopadhyay U., Kaushik S., Varticovski L., Cuervo A.M. The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane. Mol Cell Biol 2008, 28:5747-5763.
    • (2008) Mol Cell Biol , vol.28 , pp. 5747-5763
    • Bandyopadhyay, U.1    Kaushik, S.2    Varticovski, L.3    Cuervo, A.M.4
  • 24
    • 21244499845 scopus 로고    scopus 로고
    • The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways
    • Shin Y., Klucken J., Patterson C., Hyman B.T., McLean P.J. The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways. J Biol Chem 2005, 280:23727-23734.
    • (2005) J Biol Chem , vol.280 , pp. 23727-23734
    • Shin, Y.1    Klucken, J.2    Patterson, C.3    Hyman, B.T.4    McLean, P.J.5
  • 25
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo A.M., Dice J. A receptor for the selective uptake and degradation of proteins by lysosomes. Science 1996, 273:501-503.
    • (1996) Science , vol.273 , pp. 501-503
    • Cuervo, A.M.1    Dice, J.2
  • 26
    • 0028804783 scopus 로고
    • An alternatively spliced form of the human lysosome-associated membrane protein-2 gene is expressed in a tissue-specific manner
    • Konecki D., Foetisch K., Zimmer K., Schlotter M., Lichter-Konecki U. An alternatively spliced form of the human lysosome-associated membrane protein-2 gene is expressed in a tissue-specific manner. Biochem Biophys Res Commun 1995, 215:757-767.
    • (1995) Biochem Biophys Res Commun , vol.215 , pp. 757-767
    • Konecki, D.1    Foetisch, K.2    Zimmer, K.3    Schlotter, M.4    Lichter-Konecki, U.5
  • 27
    • 0034510572 scopus 로고    scopus 로고
    • Unique properties of lamp2a compared to other lamp2 isoforms
    • Cuervo A., Dice J. Unique properties of lamp2a compared to other lamp2 isoforms. J Cell Sci 2000, 113:4441-4450.
    • (2000) J Cell Sci , vol.113 , pp. 4441-4450
    • Cuervo, A.1    Dice, J.2
  • 28
    • 33748374920 scopus 로고    scopus 로고
    • Lysosome membrane lipid microdomains: novel regulators of chaperone-mediated autophagy
    • Kaushik S., Massey A.C., Cuervo A.M. Lysosome membrane lipid microdomains: novel regulators of chaperone-mediated autophagy. EMBO J 2006, 25:3921-3933.
    • (2006) EMBO J , vol.25 , pp. 3921-3933
    • Kaushik, S.1    Massey, A.C.2    Cuervo, A.M.3
  • 29
    • 0037413688 scopus 로고    scopus 로고
    • Cathepsin A regulates chaperone-mediated autophagy through cleavage of the lysosomal receptor
    • Cuervo A.M., Mann L., Bonten E., d'Azzo A., Dice J. Cathepsin A regulates chaperone-mediated autophagy through cleavage of the lysosomal receptor. EMBO J 2003, 22:12-19.
    • (2003) EMBO J , vol.22 , pp. 12-19
    • Cuervo, A.M.1    Mann, L.2    Bonten, E.3    d'Azzo, A.4    Dice, J.5
  • 30
    • 0034232418 scopus 로고    scopus 로고
    • Regulation of lamp2a levels in the lysosomal membrane
    • Cuervo A., Dice J. Regulation of lamp2a levels in the lysosomal membrane. Traffic 2000, 1:570-583.
    • (2000) Traffic , vol.1 , pp. 570-583
    • Cuervo, A.1    Dice, J.2
  • 31
    • 48249091611 scopus 로고    scopus 로고
    • Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy
    • Kaushik S., Massey A., Mizushima N., Cuervo A.M. Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy. Mol Biol Cell 2008, 19:2179-2192.
    • (2008) Mol Biol Cell , vol.19 , pp. 2179-2192
    • Kaushik, S.1    Massey, A.2    Mizushima, N.3    Cuervo, A.M.4
  • 32
    • 43949117436 scopus 로고    scopus 로고
    • Early cellular changes after blockage of chaperone-mediated autophagy
    • Massey A.C., Follenzi A., Kiffin R., Zhang C., Cuervo A.M. Early cellular changes after blockage of chaperone-mediated autophagy. Autophagy 2008, 4:442-456.
    • (2008) Autophagy , vol.4 , pp. 442-456
    • Massey, A.C.1    Follenzi, A.2    Kiffin, R.3    Zhang, C.4    Cuervo, A.M.5
  • 33
    • 60549093730 scopus 로고    scopus 로고
    • Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates
    • Korolchuk V.I., Mansilla A., Menzies F.M., Rubinsztein D.C. Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates. Mol Cell 2009, 33:517-527.
    • (2009) Mol Cell , vol.33 , pp. 517-527
    • Korolchuk, V.I.1    Mansilla, A.2    Menzies, F.M.3    Rubinsztein, D.C.4
  • 34
    • 0025801067 scopus 로고
    • Proteins containing peptide sequences related to KFERQ are selectively depleted in liver and heart, but not skeletal muscle, of fasted rats
    • Wing S., Chiang H., Goldberg A., Dice J. Proteins containing peptide sequences related to KFERQ are selectively depleted in liver and heart, but not skeletal muscle, of fasted rats. Biochem J 1991, 275:165-169.
    • (1991) Biochem J , vol.275 , pp. 165-169
    • Wing, S.1    Chiang, H.2    Goldberg, A.3    Dice, J.4
  • 35
    • 4544385218 scopus 로고    scopus 로고
    • Autophagy: many pathways to the same end
    • Cuervo A.M. Autophagy: many pathways to the same end. Mol Cell Biochem 2004, 263:55-72.
    • (2004) Mol Cell Biochem , vol.263 , pp. 55-72
    • Cuervo, A.M.1
  • 36
    • 0031595780 scopus 로고    scopus 로고
    • IκB is a substrate for a selective pathway of lysosomal proteolysis
    • Cuervo A.M., Hu W., Lim B., Dice J.F. IκB is a substrate for a selective pathway of lysosomal proteolysis. Mol Biol Cell 1998, 9:1995-2010.
    • (1998) Mol Biol Cell , vol.9 , pp. 1995-2010
    • Cuervo, A.M.1    Hu, W.2    Lim, B.3    Dice, J.F.4
  • 37
    • 51349095898 scopus 로고    scopus 로고
    • Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function
    • Zhang C., Cuervo A.M. Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function. Nat Med 2008, 14:959-965.
    • (2008) Nat Med , vol.14 , pp. 959-965
    • Zhang, C.1    Cuervo, A.M.2
  • 38
    • 56349168452 scopus 로고    scopus 로고
    • Autophagy and aging: keeping that old broom working
    • Cuervo A.M. Autophagy and aging: keeping that old broom working. Trends Genet 2008, 24:604-612.
    • (2008) Trends Genet , vol.24 , pp. 604-612
    • Cuervo, A.M.1
  • 39
    • 0020405985 scopus 로고
    • Altered degradation of proteins microinjected into senescent human fibroblasts
    • Dice J. Altered degradation of proteins microinjected into senescent human fibroblasts. J Biol Chem 1982, 257:14624-14627.
    • (1982) J Biol Chem , vol.257 , pp. 14624-14627
    • Dice, J.1
  • 40
    • 0034613294 scopus 로고    scopus 로고
    • Age-related decline in chaperone-mediated autophagy
    • Cuervo A.M., Dice J. Age-related decline in chaperone-mediated autophagy. J Biol Chem 2000, 275:31505-31513.
    • (2000) J Biol Chem , vol.275 , pp. 31505-31513
    • Cuervo, A.M.1    Dice, J.2
  • 41
    • 33847690636 scopus 로고    scopus 로고
    • Altered dynamics of the lysosomal receptor for chaperone-mediated autophagy with age
    • Kiffin R., Kaushik S., Zeng M., Bandyopadhyay U., Zhang C., Massey A.C., et al. Altered dynamics of the lysosomal receptor for chaperone-mediated autophagy with age. J Cell Sci 2007, 120:782-791.
    • (2007) J Cell Sci , vol.120 , pp. 782-791
    • Kiffin, R.1    Kaushik, S.2    Zeng, M.3    Bandyopadhyay, U.4    Zhang, C.5    Massey, A.C.6
  • 42
    • 33847652900 scopus 로고    scopus 로고
    • Autophagy and neurodegeneration: when the cleaning crew goes on strike
    • Martinez-Vicente M., Cuervo A.M. Autophagy and neurodegeneration: when the cleaning crew goes on strike. Lancet Neurol 2007, 6:352-361.
    • (2007) Lancet Neurol , vol.6 , pp. 352-361
    • Martinez-Vicente, M.1    Cuervo, A.M.2
  • 43
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo A.M., Stefanis L., Fredenburg R., Lansbury P.T., Sulzer D. Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 2004, 305:1292-1295.
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 45
    • 65849127844 scopus 로고    scopus 로고
    • α-Synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy
    • Xilouri M., Vogiatzi T., Vekrellis K., Park D., Stefanis L., Abberant α-Synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy. PLoS One 2009, 4:e5515.
    • (2009) PLoS One , vol.4
    • Xilouri, M.1    Vogiatzi, T.2    Vekrellis, K.3    Park, D.4    Stefanis, L.5    Abberant6
  • 46
    • 53049101345 scopus 로고    scopus 로고
    • Aberrant interaction between Parkinson disease-associated mutant UCH-L1 and the lysosomal receptor for chaperone-mediated autophagy
    • Kabuta T., Furuta A., Aoki S., Furuta K., Wada K. Aberrant interaction between Parkinson disease-associated mutant UCH-L1 and the lysosomal receptor for chaperone-mediated autophagy. J Biol Chem 2008, 283:23731-23738.
    • (2008) J Biol Chem , vol.283 , pp. 23731-23738
    • Kabuta, T.1    Furuta, A.2    Aoki, S.3    Furuta, K.4    Wada, K.5
  • 47
    • 58149215720 scopus 로고    scopus 로고
    • Regulation of neuronal survival factor MEF2D by chaperone-mediated autophagy
    • Yang Q., She H., Gearing M., Colla E., Lee M., Shacka J., et al. Regulation of neuronal survival factor MEF2D by chaperone-mediated autophagy. Science 2009, 323:124-127.
    • (2009) Science , vol.323 , pp. 124-127
    • Yang, Q.1    She, H.2    Gearing, M.3    Colla, E.4    Lee, M.5    Shacka, J.6
  • 48
  • 49
    • 70349666552 scopus 로고    scopus 로고
    • Degradation of regulator of calcineurin 1 (RCAN1) is mediated by both chaperone-mediated autophagy and ubiquitin proteasome pathways
    • Liu H., Wang P., Song W., Sun X. Degradation of regulator of calcineurin 1 (RCAN1) is mediated by both chaperone-mediated autophagy and ubiquitin proteasome pathways. FASEB J 2009, 23:3383-3392.
    • (2009) FASEB J , vol.23 , pp. 3383-3392
    • Liu, H.1    Wang, P.2    Song, W.3    Sun, X.4
  • 50
    • 72149124383 scopus 로고    scopus 로고
    • IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome
    • Thompson L.M., Aiken C.T., Kaltenbach L.S., Agrawal N., Illes K., Khoshnan A., et al. IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome. J Cell Biol 2009, 187:1083-1099.
    • (2009) J Cell Biol , vol.187 , pp. 1083-1099
    • Thompson, L.M.1    Aiken, C.T.2    Kaltenbach, L.S.3    Agrawal, N.4    Illes, K.5    Khoshnan, A.6
  • 51
    • 0032938776 scopus 로고    scopus 로고
    • Direct lysosomal uptake of α2-microglobulin contributes to chemically induced nephropathy
    • Cuervo A., Hildebrand H., Bomhard E., Dice J. Direct lysosomal uptake of α2-microglobulin contributes to chemically induced nephropathy. Kidney Int 1999, 55:529-545.
    • (1999) Kidney Int , vol.55 , pp. 529-545
    • Cuervo, A.1    Hildebrand, H.2    Bomhard, E.3    Dice, J.4
  • 52
    • 2442643788 scopus 로고    scopus 로고
    • Suppression of chaperone-mediated autophagy in the renal cortex during acute diabetes mellitus
    • Sooparb S., Price S.R., Shaoguang J., Franch H.A. Suppression of chaperone-mediated autophagy in the renal cortex during acute diabetes mellitus. Kidney Int 2004, 65:2135-2144.
    • (2004) Kidney Int , vol.65 , pp. 2135-2144
    • Sooparb, S.1    Price, S.R.2    Shaoguang, J.3    Franch, H.A.4


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