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Volumn 41, Issue , 2018, Pages 34-41

Connecting chaperone-mediated autophagy dysfunction to cellular senescence

Author keywords

Aging; Cellular senescence; Chaperone mediated autophagy; Macroautophagy; Proteostasis

Indexed keywords

CYCLIN DEPENDENT KINASE INHIBITOR 1A; HEAT SHOCK COGNATE PROTEIN 70; PROTEIN P21; CHAPERONE;

EID: 85033222929     PISSN: 15681637     EISSN: 18729649     Source Type: Journal    
DOI: 10.1016/j.arr.2017.11.001     Document Type: Review
Times cited : (28)

References (103)
  • 5
    • 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. 28 (2008), 5747–5763, 10.1128/MCB.02070-07.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 5747-5763
    • Bandyopadhyay, U.1    Kaushik, S.2    Varticovski, L.3    Cuervo, A.M.4
  • 9
    • 85020388158 scopus 로고    scopus 로고
    • The E3 ligase CHIP mediates p21 degradation to maintain radioresistance
    • Biswas, K., Sarkar, S., Du, K., Brautigan, D.L., Abbas, T., Larner, J.M., The E3 ligase CHIP mediates p21 degradation to maintain radioresistance. Mol. Cancer Res. 70 (2017), 1–10, 10.1158/1541-7786.MCR-16-0466.
    • (2017) Mol. Cancer Res. , vol.70 , pp. 1-10
    • Biswas, K.1    Sarkar, S.2    Du, K.3    Brautigan, D.L.4    Abbas, T.5    Larner, J.M.6
  • 10
    • 0030931491 scopus 로고    scopus 로고
    • Telomere shortening and tumor formation by mouse cells lacking telomerase RNA
    • S0092-8674(01)80006-4 [pii]
    • Blasco, M., Lee, H.W., Hande, M.P., Samper, E., Lansdorp, P.M., DePinho, R.A., Greider, C.W., Telomere shortening and tumor formation by mouse cells lacking telomerase RNA. Cell 91 (1997), 25–34 S0092-8674(01)80006-4 [pii].
    • (1997) Cell , vol.91 , pp. 25-34
    • Blasco, M.1    Lee, H.W.2    Hande, M.P.3    Samper, E.4    Lansdorp, P.M.5    DePinho, R.A.6    Greider, C.W.7
  • 11
    • 0029417080 scopus 로고
    • Interleukin-1β and interleukin-6 are elevated in the cerebrospinal fluid of Alzheimerüs and de novo Parkinsonüs disease patients
    • Blum-Degena, D., Müller, T., Kuhn, W., Gerlach, M., Przuntek, H., Riederer, P., Interleukin-1β and interleukin-6 are elevated in the cerebrospinal fluid of Alzheimerüs and de novo Parkinsonüs disease patients. Neurosci. Lett 202 (1995), 17–20, 10.1016/0304-3940(95)12192-7.
    • (1995) Neurosci. Lett , vol.202 , pp. 17-20
    • Blum-Degena, D.1    Müller, T.2    Kuhn, W.3    Gerlach, M.4    Przuntek, H.5    Riederer, P.6
  • 13
    • 84867271418 scopus 로고    scopus 로고
    • CDK inhibitors (p16/p19/p21) induce senescence and autophagy in cancer-associated fibroblasts, fueling tumor growth via paracrine interactions, without an increase in neo-angiogenesis
    • Capparelli, C., Chiavarina, B., Whitaker-Menezes, D., Pestell, T.G., Pestell, R.G., Hulit, J., Andò, S., Howell, A., Martinez-Outschoorn, U.E., Sotgia, F., Lisanti, M.P., CDK inhibitors (p16/p19/p21) induce senescence and autophagy in cancer-associated fibroblasts, fueling tumor growth via paracrine interactions, without an increase in neo-angiogenesis. Cell Cycle 11 (2012), 3599–3610, 10.4161/cc.21884.
    • (2012) Cell Cycle , vol.11 , pp. 3599-3610
    • Capparelli, C.1    Chiavarina, B.2    Whitaker-Menezes, D.3    Pestell, T.G.4    Pestell, R.G.5    Hulit, J.6    Andò, S.7    Howell, A.8    Martinez-Outschoorn, U.E.9    Sotgia, F.10    Lisanti, M.P.11
  • 16
    • 0024975155 scopus 로고
    • A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins
    • Chiang, H., Terlecky, Plant, C., Dice, J., A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science (80-.) 246 (1989), 382–385, 10.1126/science.2799391.
    • (1989) Science (80-.) , vol.246 , pp. 382-385
    • Chiang, H.1    Terlecky2    Plant, C.3    Dice, J.4
  • 17
    • 84949555897 scopus 로고    scopus 로고
    • Cellular senescence in aging and age-related disease: from mechanisms to therapy
    • Childs, B.G., Durik, M., Baker, D.J., van Deursen, J.M., Cellular senescence in aging and age-related disease: from mechanisms to therapy. Nat. Med. 21 (2015), 1424–1435, 10.1038/nm.4000.
    • (2015) Nat. Med. , vol.21 , pp. 1424-1435
    • Childs, B.G.1    Durik, M.2    Baker, D.J.3    van Deursen, J.M.4
  • 18
    • 77949881221 scopus 로고    scopus 로고
    • The senescence-associated secretory phenotype: the dark side of tumor suppression
    • Coppé, J.P., Desprez, P.Y., Krtolica, A., Campisi, J., The senescence-associated secretory phenotype: the dark side of tumor suppression. Annu. Rev. Pathol. 5 (2010), 99–118, 10.1146/annurev-pathol-121808-102144.
    • (2010) Annu. Rev. Pathol. , vol.5 , pp. 99-118
    • Coppé, J.P.1    Desprez, P.Y.2    Krtolica, A.3    Campisi, J.4
  • 20
    • 84899452308 scopus 로고    scopus 로고
    • Telomeres, oxidative stress and inflammatory factors: partners in cellular senescence?
    • Correia-Melo, C., Hewitt, G., Passos, J.F., Telomeres, oxidative stress and inflammatory factors: partners in cellular senescence?. Longev. Heal., 3, 2014, 1, 10.1186/2046-2395-3-1.
    • (2014) Longev. Heal. , vol.3 , pp. 1
    • Correia-Melo, C.1    Hewitt, G.2    Passos, J.F.3
  • 21
    • 0034613294 scopus 로고    scopus 로고
    • Age-related decline in chaperone-mediated autophagy
    • Cuervo, A.M., Dice, J.F., Age-related decline in chaperone-mediated autophagy. J. Biol. Chem. 275 (2000), 31505–31513, 10.1074/jbc.M002102200.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31505-31513
    • Cuervo, A.M.1    Dice, J.F.2
  • 22
    • 84891741302 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: roles in disease and aging
    • Cuervo, A.M., Wong, E., Chaperone-mediated autophagy: roles in disease and aging. Cell Res. 24 (2014), 92–104, 10.1038/cr.2013.153.
    • (2014) Cell Res. , vol.24 , pp. 92-104
    • Cuervo, A.M.1    Wong, E.2
  • 23
    • 74949127989 scopus 로고    scopus 로고
    • Protocols to detect senescence-associated beta-galactosidase (SA-βgal) activity, a biomarker of senescent cells in culture and in vivo
    • Debacq-Chainiaux, F., Erusalimsky, J.D., Campisi, J., Toussaint, O., Protocols to detect senescence-associated beta-galactosidase (SA-βgal) activity, a biomarker of senescent cells in culture and in vivo. Nat. Protoc. 4 (2009), 1798–1806, 10.1038/nprot.2009.191.
    • (2009) Nat. Protoc. , vol.4 , pp. 1798-1806
    • Debacq-Chainiaux, F.1    Erusalimsky, J.D.2    Campisi, J.3    Toussaint, O.4
  • 25
    • 56449090138 scopus 로고    scopus 로고
    • DNA damage response activation in mouse embryonic fibroblasts undergoing replicative senescence and following spontaneous immortalization
    • Di Micco, R., Cicalese, A., Fumagalli, M., Dobreva, M., Verrecchia, A., Pelicci, P.G., Di Fagagna, F.D.A., DNA damage response activation in mouse embryonic fibroblasts undergoing replicative senescence and following spontaneous immortalization. Cell Cycle 7 (2008), 3601–3606, 10.4161/cc.7.22.7152.
    • (2008) Cell Cycle , vol.7 , pp. 3601-3606
    • Di Micco, R.1    Cicalese, A.2    Fumagalli, M.3    Dobreva, M.4    Verrecchia, A.5    Pelicci, P.G.6    Di Fagagna, F.D.A.7
  • 26
    • 0020405985 scopus 로고
    • Altered degradation of proteins microinjected into senescent human fibroblasts
    • Dice, J.F., Altered degradation of proteins microinjected into senescent human fibroblasts. J. Biol. Chem. 257 (1982), 14624–14627.
    • (1982) J. Biol. Chem. , vol.257 , pp. 14624-14627
    • Dice, J.F.1
  • 28
    • 82455210868 scopus 로고    scopus 로고
    • Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1β
    • Dupont, N., Jiang, S., Pilli, M., Ornatowski, W., Bhattacharya, D., Deretic, V., Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1β. EMBO J. 30 (2011), 4701–4711, 10.1038/emboj.2011.398.
    • (2011) EMBO J. , vol.30 , pp. 4701-4711
    • Dupont, N.1    Jiang, S.2    Pilli, M.3    Ornatowski, W.4    Bhattacharya, D.5    Deretic, V.6
  • 29
    • 84884315657 scopus 로고    scopus 로고
    • STUB1/CHIP is required for HIF1A degradation by chaperone-mediated autophagy
    • Ferreira, J.V., Fofo, H., Bejarano, E., Bento, C.F., Ramalho, J.S., Girao, H., Pereira, P., STUB1/CHIP is required for HIF1A degradation by chaperone-mediated autophagy. Autophagy 9 (2013), 1349–1366, 10.4161/auto.25190.
    • (2013) Autophagy , vol.9 , pp. 1349-1366
    • Ferreira, J.V.1    Fofo, H.2    Bejarano, E.3    Bento, C.F.4    Ramalho, J.S.5    Girao, H.6    Pereira, P.7
  • 32
  • 33
    • 85020028464 scopus 로고    scopus 로고
    • Review senescence in health and disease
    • He, S., Sharpless, N.E., Review senescence in health and disease. Cell 169 (2017), 1000–1011, 10.1016/j.cell.2017.05.015.
    • (2017) Cell , vol.169 , pp. 1000-1011
    • He, S.1    Sharpless, N.E.2
  • 35
    • 84943750048 scopus 로고    scopus 로고
    • An essential role for chaperone-mediated autophagy in cell cycle progression
    • Hubbi, M.E., Semenza, G.L., An essential role for chaperone-mediated autophagy in cell cycle progression. Autophagy 11 (2015), 850–851, 10.1080/15548627.2015.1037063.
    • (2015) Autophagy , vol.11 , pp. 850-851
    • Hubbi, M.E.1    Semenza, G.L.2
  • 36
    • 84905976385 scopus 로고    scopus 로고
    • Cyclin-dependent kinases regulate lysosomal degradation of hypoxia-inducible factor 1α to promote cell-cycle progression
    • Hubbi, M.E., Gilkes, D.M., Hu, H., Kshitiz Ahmed, I., Semenza, G.L., Cyclin-dependent kinases regulate lysosomal degradation of hypoxia-inducible factor 1α to promote cell-cycle progression. Proc. Natl. Acad. Sci. U. S. A. 111 (2014), E3325–34, 10.1073/pnas.1412840111.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. E3325-34
    • Hubbi, M.E.1    Gilkes, D.M.2    Hu, H.3    Kshitiz Ahmed, I.4    Semenza, G.L.5
  • 38
    • 0028984925 scopus 로고
    • Non-AP component of Alzheimer's disease amyloid (NAC) is amyloidogenid
    • Iwai, A., Yoshimoto, M., Masliah, E., Saitoh, T., Non-AP component of Alzheimer's disease amyloid (NAC) is amyloidogenid. Biochemistry, 1995, 10139–10145, 10.1021/bi00032a006.
    • (1995) Biochemistry , pp. 10139-10145
    • Iwai, A.1    Yoshimoto, M.2    Masliah, E.3    Saitoh, T.4
  • 39
    • 85013413636 scopus 로고    scopus 로고
    • Cellular proteostasis: degradation of misfolded proteins by lysosomes
    • Jackson, M.P., Hewitt, E.W., Cellular proteostasis: degradation of misfolded proteins by lysosomes. Essays Biochem. 60 (2016), 173–180, 10.1042/EBC20160005.
    • (2016) Essays Biochem. , vol.60 , pp. 173-180
    • Jackson, M.P.1    Hewitt, E.W.2
  • 41
    • 77951985216 scopus 로고    scopus 로고
    • Examination of the expanding pathways for the regulation of p21 expression and activity
    • Jung, Y., Qian, Y., Chen, X., Examination of the expanding pathways for the regulation of p21 expression and activity. Cell. Signal. 22 (2010), 1003–1012, 10.1016/j.cellsig.2010.01.013.
    • (2010) Cell. Signal. , vol.22 , pp. 1003-1012
    • Jung, Y.1    Qian, Y.2    Chen, X.3
  • 42
    • 84971568095 scopus 로고    scopus 로고
    • How autophagy both activates and inhibits cellular senescence
    • Kang, C., Elledge, S.J., How autophagy both activates and inhibits cellular senescence. Autophagy 12 (2016), 898–899, 10.1080/15548627.2015.1121361.
    • (2016) Autophagy , vol.12 , pp. 898-899
    • Kang, C.1    Elledge, S.J.2
  • 43
    • 79961194820 scopus 로고    scopus 로고
    • Autophagy impairment induces premature senescence in primary human fibroblasts
    • Kang, H.T., Lee, K.B., Kim, S.Y., Choi, H.R., Park, S.C., Autophagy impairment induces premature senescence in primary human fibroblasts. PLoS One 6 (2011), 1–12, 10.1371/journal.pone.0023367.
    • (2011) PLoS One , vol.6 , pp. 1-12
    • Kang, H.T.1    Lee, K.B.2    Kim, S.Y.3    Choi, H.R.4    Park, S.C.5
  • 44
    • 85033222941 scopus 로고    scopus 로고
    • The DNA damage response induces inflammation and senescence by inhibiting autophagy of GATA4
    • Kang, C., Xu, Q., Martin, T.D., Li, M.Z., Demaria, M., Aron, L., Elledge, S.J., The DNA damage response induces inflammation and senescence by inhibiting autophagy of GATA4. Science 16 (2015), 1–26, 10.1037/emo0000122.
    • (2015) Science , vol.16 , pp. 1-26
    • Kang, C.1    Xu, Q.2    Martin, T.D.3    Li, M.Z.4    Demaria, M.5    Aron, L.6    Elledge, S.J.7
  • 46
    • 84938072487 scopus 로고    scopus 로고
    • Autophagy at the crossroads of catabolism and anabolism
    • Kaur, J., Debnath, J., Autophagy at the crossroads of catabolism and anabolism. Nat. Rev. Mol. Cell Biol. 16 (2015), 461–472, 10.1038/nrm4024.
    • (2015) Nat. Rev. Mol. Cell Biol. , vol.16 , pp. 461-472
    • Kaur, J.1    Debnath, J.2
  • 47
    • 84864318195 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: a unique way to enter the lysosome world
    • Kaushik, S., Cuervo, A.M., Chaperone-mediated autophagy: a unique way to enter the lysosome world. Trends Cell Biol. 22 (2012), 407–417, 10.1016/j.tcb.2012.05.006.
    • (2012) Trends Cell Biol. , vol.22 , pp. 407-417
    • Kaushik, S.1    Cuervo, A.M.2
  • 48
    • 84930182353 scopus 로고    scopus 로고
    • Degradation of lipid droplet-associated proteins by chaperone-mediated autophagy facilitates lipolysis
    • Kaushik, S., Cuervo, A.M., Degradation of lipid droplet-associated proteins by chaperone-mediated autophagy facilitates lipolysis. Nat. Cell Biol. 17 (2015), 759–770, 10.1038/ncb3166.
    • (2015) Nat. Cell Biol. , vol.17 , pp. 759-770
    • Kaushik, S.1    Cuervo, A.M.2
  • 49
    • 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. 25 (2006), 3921–3933, 10.1038/sj.emboj.7601283.
    • (2006) EMBO J. , vol.25 , pp. 3921-3933
    • Kaushik, S.1    Massey, A.C.2    Cuervo, A.M.3
  • 50
    • 6344275803 scopus 로고    scopus 로고
    • Activation of chaperon-mediated autophagy during oxidative stress
    • Kiffin, R., Christian, C., Knecht, E., Cuervo, A., Activation of chaperon-mediated autophagy during oxidative stress. Mol. Biol. Cell 16 (2004), 4829–4840, 10.1091/mbc.E04.
    • (2004) Mol. Biol. Cell , vol.16 , pp. 4829-4840
    • Kiffin, R.1    Christian, C.2    Knecht, E.3    Cuervo, A.4
  • 52
    • 84898757170 scopus 로고    scopus 로고
    • Dynamic regulation of macroautophagy by distinctive ubiquitin-like proteins
    • Klionsky, D.J., Schulman, B.A., Dynamic regulation of macroautophagy by distinctive ubiquitin-like proteins. Nat. Struct. Mol. Biol. 21 (2014), 336–345, 10.1038/nsmb.2787.
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 336-345
    • Klionsky, D.J.1    Schulman, B.A.2
  • 53
    • 3142631736 scopus 로고    scopus 로고
    • HIF-1α induces cell cycle arrest by functionally counteracting Myc
    • Koshiji, M., Kageyama, Y., Pete, E.A., Horikawa, I., Barrett, J.C., Huang, L.E., HIF-1α induces cell cycle arrest by functionally counteracting Myc. EMBO J. 23 (2004), 1949–1956, 10.1038/sj.emboj.7600196.
    • (2004) EMBO J. , vol.23 , pp. 1949-1956
    • Koshiji, M.1    Kageyama, Y.2    Pete, E.A.3    Horikawa, I.4    Barrett, J.C.5    Huang, L.E.6
  • 54
    • 84939562025 scopus 로고    scopus 로고
    • Influence of lentiviral??-synuclein overexpression in the hippocampus of a transgenic mouse model of Alzheimer's disease on amyloid precursor protein metabolism and pathology
    • Krassnig, S., Schweinzer, C., Taub, N., Havas, D., Auer, E., Flunkert, S., Schreibmayer, W., Hutter-Paier, B., Windisch, M., Influence of lentiviral??-synuclein overexpression in the hippocampus of a transgenic mouse model of Alzheimer's disease on amyloid precursor protein metabolism and pathology. Neurodegener. Dis. 15 (2015), 243–257, 10.1159/000430952.
    • (2015) Neurodegener. Dis. , vol.15 , pp. 243-257
    • Krassnig, S.1    Schweinzer, C.2    Taub, N.3    Havas, D.4    Auer, E.5    Flunkert, S.6    Schreibmayer, W.7    Hutter-Paier, B.8    Windisch, M.9
  • 55
    • 84878864199 scopus 로고    scopus 로고
    • Europe PMC funders group the hallmarks of aging
    • López-otín, C., Blasco, M.A., Partridge, L., Serrano, M., Europe PMC funders group the hallmarks of aging. Cell 153 (2013), 1194–1217, 10.1016/j.cell.2013.05.039.
    • (2013) Cell , vol.153 , pp. 1194-1217
    • López-otín, C.1    Blasco, M.A.2    Partridge, L.3    Serrano, M.4
  • 56
    • 84939000739 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy and neurodegeneration: connections, mechanisms, and therapeutic implications
    • Liu, X., Huang, S., Wang, X., Tang, B., Li, W., Mao, Z., Chaperone-mediated autophagy and neurodegeneration: connections, mechanisms, and therapeutic implications. Neurosci. Bull. 31 (2015), 407–415, 10.1007/s12264-015-1542-8.
    • (2015) Neurosci. Bull. , vol.31 , pp. 407-415
    • Liu, X.1    Huang, S.2    Wang, X.3    Tang, B.4    Li, W.5    Mao, Z.6
  • 57
    • 85014085851 scopus 로고    scopus 로고
    • Regulation of lipids is central to replicative senescence
    • Lizardo, D.Y., Lin, Y.-L., Gokcumen, O., Atilla-Gokcumen, G.E., Regulation of lipids is central to replicative senescence. Mol. BioSyst. 13 (2017), 498–509, 10.1039/C6MB00842A.
    • (2017) Mol. BioSyst. , vol.13 , pp. 498-509
    • Lizardo, D.Y.1    Lin, Y.-L.2    Gokcumen, O.3    Atilla-Gokcumen, G.E.4
  • 58
    • 43049163718 scopus 로고    scopus 로고
    • Free radicals and senescence
    • Lu, T., Finkel, T., Free radicals and senescence. Exp. Cell Res. 314 (2008), 1918–1922, 10.1016/j.yexcr.2008.01.011.
    • (2008) Exp. Cell Res. , vol.314 , pp. 1918-1922
    • Lu, T.1    Finkel, T.2
  • 60
    • 80054862730 scopus 로고    scopus 로고
    • Autophagy regulates ROS-induced cellular senescence via p21 in a p38 MAPK?? dependent manner
    • Luo, Y., Zou, P., Zou, J., Wang, J., Zhou, D., Liu, L., Autophagy regulates ROS-induced cellular senescence via p21 in a p38 MAPK?? dependent manner. Exp. Gerontol. 46 (2011), 860–867, 10.1016/j.exger.2011.07.005.
    • (2011) Exp. Gerontol. , vol.46 , pp. 860-867
    • Luo, Y.1    Zou, P.2    Zou, J.3    Wang, J.4    Zhou, D.5    Liu, L.6
  • 61
    • 79959371914 scopus 로고    scopus 로고
    • Acetylation targets the M2 isoform of pyruvate kinase for degradation through chaperone-mediated autophagy and promotes tumor growth
    • Lv, L., Li, D., Zhao, D., Lin, R., Chu, Y., Zhang, H., Zha, Z., Liu, Y., Li, Z., Xu, Y., Wang, G., Huang, Y., Xiong, Y., Guan, K.L., Lei, Q.Y., Acetylation targets the M2 isoform of pyruvate kinase for degradation through chaperone-mediated autophagy and promotes tumor growth. Mol. Cell 42 (2011), 719–730, 10.1016/j.molcel.2011.04.025.
    • (2011) Mol. Cell , vol.42 , pp. 719-730
    • Lv, L.1    Li, D.2    Zhao, D.3    Lin, R.4    Chu, Y.5    Zhang, H.6    Zha, Z.7    Liu, Y.8    Li, Z.9    Xu, Y.10    Wang, G.11    Huang, Y.12    Xiong, Y.13    Guan, K.L.14    Lei, Q.Y.15
  • 64
    • 44949127204 scopus 로고    scopus 로고
    • CHIP deficiency decreases longevity, with accelerated aging phenotypes accompanied by altered protein quality control
    • Min, J.-N., Whaley, R.A., Sharpless, N.E., Lockyer, P., Portbury, A.L., Patterson, C., CHIP deficiency decreases longevity, with accelerated aging phenotypes accompanied by altered protein quality control. Mol. Cell. Biol. 28 (2008), 4018–4025, 10.1128/MCB.00296-08.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4018-4025
    • Min, J.-N.1    Whaley, R.A.2    Sharpless, N.E.3    Lockyer, P.4    Portbury, A.L.5    Patterson, C.6
  • 65
    • 80054025654 scopus 로고    scopus 로고
    • The role of atg proteins in autophagosome formation
    • Mizushima, N., Yoshimori, T., Ohsumi, Y., The role of atg proteins in autophagosome formation. Annu. Rev. Cell Dev. Biol. 27 (2011), 107–132, 10.1146/annurev-cellbio-092910-154005.
    • (2011) Annu. Rev. Cell Dev. Biol. , vol.27 , pp. 107-132
    • Mizushima, N.1    Yoshimori, T.2    Ohsumi, Y.3
  • 66
    • 84904702784 scopus 로고    scopus 로고
    • Cellular senescence: from physiology to pathology
    • Muñoz-Espín, D., Serrano, M., Cellular senescence: from physiology to pathology. Nat. Rev. Mol. Cell Biol. 15 (2014), 482–496, 10.1038/nrm3823.
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 482-496
    • Muñoz-Espín, D.1    Serrano, M.2
  • 68
    • 0037401714 scopus 로고    scopus 로고
    • CHIP: A quality-control E3 ligase collaborating with molecular chaperones
    • Murata, S., Chiba, T., Tanaka, K., CHIP: A quality-control E3 ligase collaborating with molecular chaperones. Int. J. Biochem. Cell Biol. 35 (2003), 572–578, 10.1016/S1357-2725(02)00394-1.
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , pp. 572-578
    • Murata, S.1    Chiba, T.2    Tanaka, K.3
  • 69
  • 70
    • 0037667702 scopus 로고    scopus 로고
    • Rb-mediated heterochromatin formation and silencing of E2F target genes during cellular senescence
    • Narita, M., Nũnez, S., Heard, E., Narita, M., Lin, A.W., Hearn, S.A., Spector, D.L., Hannon, G.J., Lowe, S.W., Rb-mediated heterochromatin formation and silencing of E2F target genes during cellular senescence. Cell 113 (2003), 703–716, 10.1016/S0092-8674(03)00401-X.
    • (2003) Cell , vol.113 , pp. 703-716
    • Narita, M.1    Nũnez, S.2    Heard, E.3    Narita, M.4    Lin, A.W.5    Hearn, S.A.6    Spector, D.L.7    Hannon, G.J.8    Lowe, S.W.9
  • 72
    • 84891745088 scopus 로고    scopus 로고
    • Historical landmarks of autophagy research
    • Ohsumi, Y., Historical landmarks of autophagy research. Cell Res. 24 (2014), 9–23, 10.1038/cr.2013.169.
    • (2014) Cell Res. , vol.24 , pp. 9-23
    • Ohsumi, Y.1
  • 73
    • 24744441497 scopus 로고    scopus 로고
    • Autophagy is required for maintenance of amino acid levels and protein synthesis under nitrogen starvation
    • Onodera, J., Ohsumi, Y., Autophagy is required for maintenance of amino acid levels and protein synthesis under nitrogen starvation. J. Biol. Chem. 280 (2005), 31582–31586, 10.1074/jbc.M506736200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31582-31586
    • Onodera, J.1    Ohsumi, Y.2
  • 74
    • 84928023582 scopus 로고    scopus 로고
    • Regulated degradation of Chk1 by chaperone-mediated autophagy in response to DNA damage
    • Park, C., Suh, Y., Cuervo, A.M., Regulated degradation of Chk1 by chaperone-mediated autophagy in response to DNA damage. Nat. Commun., 6, 2015, 6823, 10.1038/ncomms7823.
    • (2015) Nat. Commun. , vol.6 , pp. 6823
    • Park, C.1    Suh, Y.2    Cuervo, A.M.3
  • 75
    • 84991380022 scopus 로고    scopus 로고
    • Regulation of amyloid precursor protein processing by its KFERQ motif
    • Park, J.S., Kim, D.H., Yoon, S.Y., Regulation of amyloid precursor protein processing by its KFERQ motif. BMB Rep. 49 (2016), 337–342, 10.5483/BMBRep.2016.49.6.212.
    • (2016) BMB Rep. , vol.49 , pp. 337-342
    • Park, J.S.1    Kim, D.H.2    Yoon, S.Y.3
  • 76
    • 33750703909 scopus 로고    scopus 로고
    • Oxygen free radicals in cell senescence: are they signal transducers?
    • Passos, J.F., Von Zglinicki, T., Oxygen free radicals in cell senescence: are they signal transducers?. Free Radic. Res. 40 (2006), 1277–1283, 10.1080/10715760600917151.
    • (2006) Free Radic. Res. , vol.40 , pp. 1277-1283
    • Passos, J.F.1    Von Zglinicki, T.2
  • 78
    • 79951912532 scopus 로고    scopus 로고
    • Four faces of cellular senescence
    • Rodier, F., Campisi, J., Four faces of cellular senescence. J. Cell Biol. 192 (2011), 547–556, 10.1083/jcb.201009094.
    • (2011) J. Cell Biol. , vol.192 , pp. 547-556
    • Rodier, F.1    Campisi, J.2
  • 80
    • 85017330629 scopus 로고    scopus 로고
    • LAMP -2 deficiency leads to hippocampal dysfunction but normal clearance of neuronal substrates of chaperone-mediated autophagy in a mouse model for Danon disease
    • Rothaug, M., Stroobants, S., Schweizer, M., Peters, J., Zunke, F., Allerding, M., Hooge, R.D., Saftig, P., Blanz, J., LAMP -2 deficiency leads to hippocampal dysfunction but normal clearance of neuronal substrates of chaperone-mediated autophagy in a mouse model for Danon disease. Acta Neuropathol Commun, 2015, 1–17, 10.1186/s40478-014-0182-y.
    • (2015) Acta Neuropathol Commun , pp. 1-17
    • Rothaug, M.1    Stroobants, S.2    Schweizer, M.3    Peters, J.4    Zunke, F.5    Allerding, M.6    Hooge, R.D.7    Saftig, P.8    Blanz, J.9
  • 81
    • 84869428389 scopus 로고    scopus 로고
    • LAMP2A overexpression in breast tumors promotes cancer cell survival via chaperone-mediated autophagy
    • Saha, T., LAMP2A overexpression in breast tumors promotes cancer cell survival via chaperone-mediated autophagy. Autophagy 8 (2012), 1643–1656, 10.4161/auto.21654.
    • (2012) Autophagy , vol.8 , pp. 1643-1656
    • Saha, T.1
  • 83
    • 85021792527 scopus 로고    scopus 로고
    • Shaping proteostasis at the cellular, tissue, and organismal level
    • Sala, A.J., Bott, L.C., Morimoto, R.I., Shaping proteostasis at the cellular, tissue, and organismal level. J. Cell Biol., 2017, 201612111, 10.1083/jcb.201612111.
    • (2017) J. Cell Biol. , pp. 201612111
    • Sala, A.J.1    Bott, L.C.2    Morimoto, R.I.3
  • 84
    • 0034282931 scopus 로고    scopus 로고
    • Impor of cytosolic portein into lysosomes by chaperone-mediated autophagy depends on its folding state
    • Salvador, N., Aguado, C., Horst, M., Knecht, E., Impor of cytosolic portein into lysosomes by chaperone-mediated autophagy depends on its folding state. J. Biol. Chem. 275 (2000), 27447–27456.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27447-27456
    • Salvador, N.1    Aguado, C.2    Horst, M.3    Knecht, E.4
  • 85
    • 77954601195 scopus 로고    scopus 로고
    • Autophagy mediates the process of cellular senescence characterizing bile duct damages in primary biliary cirrhosis
    • Sasaki, M., Miyakoshi, M., Sato, Y., Nakanuma, Y., Autophagy mediates the process of cellular senescence characterizing bile duct damages in primary biliary cirrhosis. Lab. Invest. 90 (2010), 835–843, 10.1038/labinvest.2010.56.
    • (2010) Lab. Invest. , vol.90 , pp. 835-843
    • Sasaki, M.1    Miyakoshi, M.2    Sato, Y.3    Nakanuma, Y.4
  • 86
    • 38749103066 scopus 로고    scopus 로고
    • P21 inhibits cdk1 in the absence of cdk2 to maintain the G1/S phase DNA damage checkpoint
    • Satyanarayana, A., Hilton, M.B., Kaldis, P., P21 inhibits cdk1 in the absence of cdk2 to maintain the G1/S phase DNA damage checkpoint. Mol. Biol. Cell 19 (2008), 65–77, 10.1091/mbc.E07.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 65-77
    • Satyanarayana, A.1    Hilton, M.B.2    Kaldis, P.3
  • 88
    • 0030944985 scopus 로고    scopus 로고
    • Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16(INK4a)
    • Serrano, M., Lin, A.W., McCurrach, M.E., Beach, D., Lowe, S.W., Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16(INK4a). Cell 88 (1997), 593–602, 10.1016/S0092-8674(00)81902-9.
    • (1997) Cell , vol.88 , pp. 593-602
    • Serrano, M.1    Lin, A.W.2    McCurrach, M.E.3    Beach, D.4    Lowe, S.W.5
  • 89
    • 0034682721 scopus 로고    scopus 로고
    • Cellular senescence: minireview mitotic clock or culture shock?
    • Sherr, C.J., DePinho, R.A., Cellular senescence: minireview mitotic clock or culture shock?. Cell 102 (2000), 407–410, 10.1016/S0092-8674(00)00046-5.
    • (2000) Cell , vol.102 , pp. 407-410
    • Sherr, C.J.1    DePinho, R.A.2
  • 94
    • 84901288438 scopus 로고    scopus 로고
    • The role of senescent cells in ageing
    • van Deursen, J.M., The role of senescent cells in ageing. Nature 509 (2014), 439–446, 10.1038/nature13193.
    • (2014) Nature , vol.509 , pp. 439-446
    • van Deursen, J.M.1
  • 96
    • 66149167336 scopus 로고    scopus 로고
    • DNA damage response and cellular senescence in tissues of aging mice
    • Wang, C., Jurk, D., Maddick, M., Nelson, G., Martin-ruiz, C., Von Zglinicki, T., DNA damage response and cellular senescence in tissues of aging mice. Aging Cell 8 (2009), 311–323, 10.1111/j.1474-9726.2009.00481.x.
    • (2009) Aging Cell , vol.8 , pp. 311-323
    • Wang, C.1    Jurk, D.2    Maddick, M.3    Nelson, G.4    Martin-ruiz, C.5    Von Zglinicki, T.6
  • 98
    • 84978646178 scopus 로고    scopus 로고
    • Amyloid?? protein aggravates neuronal senescence and cognitive deficits in 5XFAD mouse model of Alzheimer???s disease
    • Wei, Z., Chen, X.C., Song, Y., Pan, X.D., Dai, X.M., Zhang, J., Cui, X.L., Wu, X.L., Zhu, Y.G., Amyloid?? protein aggravates neuronal senescence and cognitive deficits in 5XFAD mouse model of Alzheimer???s disease. Chin. Med. J. (Engl.) 129 (2016), 1835–1844, 10.4103/0366-6999.186646.
    • (2016) Chin. Med. J. (Engl.) , vol.129 , pp. 1835-1844
    • Wei, Z.1    Chen, X.C.2    Song, Y.3    Pan, X.D.4    Dai, X.M.5    Zhang, J.6    Cui, X.L.7    Wu, X.L.8    Zhu, Y.G.9
  • 99
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: core machinery and adaptations
    • Xie, Z., Klionsky, D.J., Autophagosome formation: core machinery and adaptations. Nat. Cell Biol. 9 (2007), 1102–1109, 10.1038/ncb1007-1102.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 100
    • 84929707134 scopus 로고    scopus 로고
    • Molecular and Cellular Neuroscience Chaperone mediated autophagy to the rescue: a new-fangled target for the treatment of neurodegenerative diseases
    • Xilouri, M., Stefanis, L., Molecular and Cellular Neuroscience Chaperone mediated autophagy to the rescue: a new-fangled target for the treatment of neurodegenerative diseases. Mol. Cell. Neurosci. 66 (2015), 29–36, 10.1016/j.mcn.2015.01.003.
    • (2015) Mol. Cell. Neurosci. , vol.66 , pp. 29-36
    • Xilouri, M.1    Stefanis, L.2
  • 101
    • 84999046809 scopus 로고    scopus 로고
    • Chaperone mediated autophagy in aging: starve to prosper
    • Xilouri, M., Stefanis, L., Chaperone mediated autophagy in aging: starve to prosper. Ageing Res. Rev. 32 (2016), 13–21, 10.1016/j.arr.2016.07.001.
    • (2016) Ageing Res. Rev. , vol.32 , pp. 13-21
    • Xilouri, M.1    Stefanis, L.2
  • 102
    • 84990234698 scopus 로고    scopus 로고
    • Impairment of chaperone-mediated autophagy induces dopaminergic neurodegeneration in rats
    • Xilouri, M., Brekk, O.R., Polissidis, A., Chrysanthou-Piterou, M., Kloukina, I., Stefanis, L., Impairment of chaperone-mediated autophagy induces dopaminergic neurodegeneration in rats. Autophagy 12 (2016), 2230–2247, 10.1080/15548627.2016.1214777.
    • (2016) Autophagy , vol.12 , pp. 2230-2247
    • Xilouri, M.1    Brekk, O.R.2    Polissidis, A.3    Chrysanthou-Piterou, M.4    Kloukina, I.5    Stefanis, L.6
  • 103
    • 84903590343 scopus 로고    scopus 로고
    • Disruption of chaperone-mediated autophagydependent degradation of MEF2A by oxidative stress-induced lysosome destabilization
    • Zhang, L., Sun, Y., Fei, M., Tan, C., Wu, J., Zheng, J., Tang, J., Sun, W., Lv, Z., Bao, J., Xu, Q., Yu, H., Disruption of chaperone-mediated autophagydependent degradation of MEF2A by oxidative stress-induced lysosome destabilization. Autophagy 10 (2014), 1015–1035, 10.4161/auto.28477.
    • (2014) Autophagy , vol.10 , pp. 1015-1035
    • Zhang, L.1    Sun, Y.2    Fei, M.3    Tan, C.4    Wu, J.5    Zheng, J.6    Tang, J.7    Sun, W.8    Lv, Z.9    Bao, J.10    Xu, Q.11    Yu, H.12


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