CoChat
Sign Up
Cited by 1,407

The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.

The coming of age of chaperone-mediated autophagy

Kaushik, Susmita, Cuervo, Ana Maria·2018·Nature Reviews Molecular Cell Biology
DOI 10.1038/s41580-018-0001-6PMC PMC6399518
Open this paper in CoChat — free account

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1038/s41580-018-0001-6

Cites

13 of 13 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Chaperone-mediated autophagy involves proteins exposing a KFERQ-like motif binding HSC70 and then LAMP2A, which facilitates translocation of the client protein into the lysosome lumen.

    “The degradation of proteins by the lysosome can be achieved in a specific fashion, through chaperone-mediated autophagy (CMA), wherein proteins exposing a pentapeptide motif resembling KFERQ first bind to heat shock protein HSC70, and then to lysosomeassociated membrane protein type 2A (LAMP2A), which facilitates the translocation of the client protein into the lumen of the”

    From Hallmarks of aging: An expanding universe (2023) · cites this paper as [87]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 124

  1. Green, D. R. & Levine, B. To be or not to be? How selective autophagy and cell death govern cell fate. Cell 157, 65–75 (2014). · DOI
  2. Galluzzi, L. et al. Molecular definitions of autophagy and related processes. EMBO J. 36, 1811–1836 (2017). · DOI · Paper page
  3. Marzella, L., Ahlberg, J. & Glaumann, H. Autophagy, heterophagy, microautophagy and crinophagy as the means for intracellular degradation. Virchows Archiv B Cell Pathol. Incl. Mol. Pathol. 36, 219–234 (1981). · DOI
  4. Roberts, P. et al. Piecemeal microautophagy of nucleus in Saccharomyces cerevisiae. Mol. Biol. Cell 14, 129–141 (2003). · DOI · Paper page
  5. Sakai, Y., Koller, A., Rangell, L., Keller, G. & Subramani, S. Peroxisome degradation by microautophagy in Pichia pastoris. Identification of specific steps and morphological intermediates. J. Cell Biol. 141, 625–636 (1998). · DOI
  6. Sahu, R. et al. Microautophagy of cytosolic proteins by late endosomes. Dev. Cell 20, 131–139 (2011). First report of endosomal microautophagy. · DOI · Paper page
  7. Dice, J. F. Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends Biochem. Sci. 15, 305–309 (1990). First characterization of the properties of the KFERQ-like signal. · DOI
  8. Terlecky, S. R., Chiang, H.-L., Olson, T. S. & Dice, J. F. Protein and peptide binding and stimulation of in vitro lysosomal proteolysis by the 73-kDa heat shock cognate protein. J. Biol. Chem. 267, 9202–9209 (1992). · DOI
  9. Cuervo, A. M., Terlecky, S. R., Dice, J. F. & Knecht, E. Selective binding and uptake of ribonuclease A and glyceraldehyde-3-phosphate dehydrogenase by isolated rat liver lysosomes. J. Biol. Chem. 269, 26374–26380 (1994). · DOI
  10. Eskelinen, E. L. et al. Unifying nomenclature for the isoforms of the lysosomal membrane protein LAMP-2. Traffic 6, 1058–1061 (2005). · DOI
  11. Massey, A. C., Kaushik, S., Sovak, G., Kiffin, R. & Cuervo, A. M. Consequences of the selective blockage of chaperone-mediated autophagy. Proc. Natl Acad. Sci. USA 103, 5805–5810 (2006). · DOI · Paper page
  12. Bandyopadhyay, U., Sridhar, S., Kaushik, S., Kiffin, R. & Cuervo, A. M. Identification of regulators of chaperone-mediated autophagy. Mol. Cell 39, 535–547 (2010). · DOI
  13. 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, 5747–5763 (2008). Identification of the CMA translocation complex at the lysosomal membrane. · DOI
  14. Arias, E. et al. Lysosomal mTORC2/PHLPP1/Akt regulate chaperone-mediated autophagy. Mol. Cell 59, 270–284 (2015). · DOI
  15. Kon, M. et al. Chaperone-mediated autophagy is required for tumor growth. Sci. Transl Med. 3, 109ra117 (2011). · DOI
  16. Schneider, J. L., Suh, Y. & Cuervo, A. M. Deficient chaperone-mediated autophagy in liver leads to metabolic dysregulation. Cell Metab. 20, 417–432 (2014). First mouse model with tissue-specific CMA blockage in vivo. · DOI · Paper page
  17. Schneider, J. L. et al. Loss of hepatic chaperone-mediated autophagy accelerates proteostasis failure in aging. Aging Cell 14, 249–264 (2015). · DOI
  18. Dice, J. F. Altered degradation of proteins microinjected into senescent human fibroblasts. J. Biol. Chem. 257, 14624–14627 (1982). · DOI · Paper page
  19. Kaushik, S. & Cuervo, A. M. AMPK-dependent phosphorylation of lipid droplet protein PLIN2 triggers its degradation by CMA. Autophagy 12, 432–438 (2016). · DOI
  20. Park, C., Suh, Y. & Cuervo, A. M. Regulated degradation of Chk1 by chaperone-mediated autophagy in response to DNA damage. Nat. Commun. 6, 6823 (2015). · DOI
  21. Quintavalle, C. et al. Phosphorylation-regulated degradation of the tumor-suppressor form of PED by chaperone-mediated autophagy in lung cancer cells. J. Cell. Physiol. 229, 1359–1368 (2014). · DOI
  22. Zhou, J. et al. Chaperone-mediated autophagy regulates proliferation by targeting RND3 in gastric cancer. Autophagy 12, 515–528 (2016). · DOI
  23. Lv, L. et al. Acetylation targets the M2 isoform of pyruvate kinase for degradation through chaperone-mediated autophagy and promotes tumor growth. Mol. Cell 42, 719–730 (2011). · DOI
  24. Bonhoure, A. et al. Acetylation of translationally controlled tumor protein promotes its degradation through chaperone-mediated autophagy. Eur. J. Cell Biol. 96, 83–98 (2017). · DOI
  25. Ferreira, J. V., Soares, A. R., Ramalho, J. S., Pereira, P. & Girao, H. K63 linked ubiquitin chain formation is a signal for HIF1A degradation by chaperone-mediated autophagy. Sci. Rep. 5, 10210 (2015). · DOI
  26. Li, L. et al. Deacetylation of tumor-suppressor MST1 in Hippo pathway induces its degradation through HBXIP-elevated HDAC6 in promotion of breast cancer growth. Oncogene 35, 4048–4057 (2016). · DOI
  27. Chiang, H., Terlecky, S., Plant, C. & Dice, J. F. A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 246, 382–385 (1989). Identification of HSC70 as the chaperone for CMA. · DOI
  28. Ferreira, J. V. et al. STUB1/CHIP is required for HIF1A degradation by chaperone-mediated autophagy. Autophagy 9, 1349–1366 (2013). · DOI
  29. Agarraberes, F. & Dice, J. F. A molecular chaperone complex at the lysosomal membrane is required for protein translocation. J. Cell Sci. 114, 2491–2499 (2001). · DOI
  30. Arndt, V. et al. Chaperone-assisted selective autophagy is essential for muscle maintenance. Curr. Biol. 20, 143–148 (2010). · DOI
  31. Cuervo, A. M., Dice, J. F. & Knecht, E. A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins. J. Biol. Chem. 272, 5606–5615 (1997). · DOI
  32. Salvador, N., Aguado, C., Horst, M. & Knecht, E. Import of a cytosolic protein into lysosomes by chaperone-mediated autophagy depends on its folding state. J. Biol. Chem. 275, 27447–27456 (2000). · DOI
  33. Agarraberes, F., Terlecky, S. & Dice, J. An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation. J. Cell Biol. 137, 825–834 (1997). · DOI
  34. Kaushik, S., Massey, A., Mizushima, N. & Cuervo, A. M. Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy. Mol. Biol. Cell 19, 2179–2192 (2008). · DOI
  35. Cuervo, A. M. & Dice, J. F. A receptor for the selective uptake and degradation of proteins by lysosomes. Science 273, 501–503 (1996). Identification of the lysosomal membrane receptor for CMA. · DOI · Paper page
  36. Cuervo, A. M., Knecht, E., Terlecky, S. R. & Dice, J. F. Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation. Am. J. Physiol. 269, C1200–C1208 (1995). · DOI
  37. Cuervo, A. M. & Dice, J. F. Unique properties of lamp2a compared to other lamp2 isoforms. J. Cell Sci. 113, 4441–4450 (2000). · DOI
  38. Li, J. & Pfeffer, S. R. Lysosomal membrane glycoproteins bind cholesterol and contribute to lysosomal cholesterol export. eLife 5, e21635 (2016). · DOI · Paper page
  39. Cuervo, A. M. & Dice, J. F. Regulation of lamp2a levels in the lysosomal membrane. Traffic 1, 570–583 (2000). · DOI
  40. Rout, A. K., Strub, M. P., Piszczek, G. & Tjandra, N. Structure of transmembrane domain of lysosome-associated membrane protein type 2a (LAMP-2A) reveals key features for substrate specificity in chaperone-mediated autophagy. J. Biol. Chem. 289, 35111–35123 (2014). · DOI
  41. Kiffin, R., Christian, C., Knecht, E. & Cuervo, A. M. Activation of chaperone-mediated autophagy during oxidative stress. Mol. Biol. Cell 15, 4829–4840 (2004). · DOI
  42. Hubbi, M. E. et al. Cyclin-dependent kinases regulate lysosomal degradation of hypoxia-inducible factor 1alpha to promote cell-cycle progression. Proc. Natl Acad. Sci. USA 111, E3325–E3334 (2014). · DOI
  43. Anguiano, J. et al. Chemical modulation of chaperone-mediated autophagy by retinoic acid derivatives. Nat. Chem. Biol. 9, 374–382 (2013). · DOI
  44. Sardiello, M. et al. A gene network regulating lysosomal biogenesis and function. Science 325, 473–477 (2009). · DOI · Paper page
  45. Kaushik, S., Massey, A. C. & Cuervo, A. M. Lysosome membrane lipid microdomains: novel regulators of chaperone-mediated autophagy. EMBO J. 25, 3921–3933 (2006). Identification of the mechanisms that determine LAMP2A stability in lysosomes. · DOI
  46. Wilke, S., Krausze, J. & Bussow, K. Crystal structure of the conserved domain of the DC lysosomal associated membrane protein: implications for the lysosomal glycocalyx. BMC Biol. 10, 62 (2012). · DOI
  47. Cuervo, A. M., Mann, L., Bonten, E. J., d’Azzo, A. & Dice, J. F. Cathepsin A regulates chaperone-mediated autophagy through cleavage of the lysosomal receptor. EMBO J. 22, 12–19 (2003). · DOI · Paper page
  48. Rodriguez-Navarro, J. A. et al. Inhibitory effect of dietary lipids on chaperone-mediated autophagy. Proc. Natl Acad. Sci. USA 109, E705–E714 (2012). · DOI
  49. Napolitano, G. et al. Impairment of chaperone-mediated autophagy leads to selective lysosomal degradation defects in the lysosomal storage disease cystinosis. EMBO Mol. Med. 7, 158–174 (2015). · DOI
  50. Zhang, J. et al. Cystinosin, the small GTPase Rab11, and the Rab7 effector RILP regulate intracellular trafficking of the chaperone-mediated autophagy receptor LAMP2A. J. Biol. Chem. 292, 10328–10346 (2017). · DOI
  51. Koga, H., Martinez-Vicente, M., Macian, F., Verkhusha, V. V. & Cuervo, A. M. A photoconvertible fluorescent reporter to track chaperone-mediated autophagy. Nat. Commun. 2, 386 (2011). · DOI
  52. Dohi, E. et al. Hypoxic stress activates chaperone-mediated autophagy and modulates neuronal cell survival. Neurochem. Int. 60, 431–442 (2012). · DOI
  53. Finn, P. F. & Dice, J. F. Ketone bodies stimulate chaperone-mediated autophagy. J. Biol. Chem. 280, 25864–25870 (2005). · DOI
  54. Cuervo, A. M., Hildebrand, H., Bomhard, E. M. & Dice, J. F. Direct lysosomal uptake of alpha 2-microglobulin contributes to chemically induced nephropathy. Kidney Int. 55, 529–545 (1999). · DOI
  55. Martinez-Vicente, M. et al. Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy. J. Clin. Invest. 118, 777–788 (2008).
  56. Zhang, C. & Cuervo, A. M. Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function. Nat. Med. 14, 959–965 (2008). · DOI · Paper page
  57. Mizushima, N., Yamamoto, A., Matsui, M., Yoshimori, T. & Ohsumi, Y. In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol. Biol. Cell 15, 1101–1111 (2004). · DOI · Paper page
  58. Singh, V. et al. Salmonella co-opts host cell chaperone-mediated autophagy for intracellular growth. J. Biol. Chem. 292, 1847–1864 (2017). · DOI
  59. Wang, B. et al. Essential control of mitochondrial morphology and function by chaperone-mediated autophagy through degradation of PARK7. Autophagy 12, 1215–1228 (2016). · DOI · Paper page
  60. Kaushik, S. & Cuervo, A. M. Degradation of lipid droplet-associated proteins by chaperone-mediated autophagy facilitates lipolysis. Nat. Cell Biol. 17, 759–770 (2015). Identification of the regulatory role of CMA in lipid metabolism. · DOI
  61. Lu, W. et al. Dual proteolytic pathways govern glycolysis and immune competence. Cell 159, 1578–1590 (2014). · DOI
  62. Cuervo, A. M., Hu, W., Lim, B. & Dice, J. F. IkappaB is a substrate for a selective pathway of lysosomal proteolysis. Mol. Biol. Cell 9, 1995–2010 (1998). · DOI
  63. Franch, H. A., Sooparb, S., Du, J. & Brown, N. S. A mechanism regulating proteolysis of specific proteins during renal tubular cell growth. J. Biol. Chem. 276, 19126–19131 (2001). · DOI
  64. Yang, Q. et al. Regulation of neuronal survival factor MEF2D by chaperone-mediated autophagy. Science 323, 124–127 (2009). · DOI
  65. Zhang, L. et al. Disruption of chaperone-mediated autophagy-dependent degradation of MEF2A by oxidative stress-induced lysosome destabilization. Autophagy 10, 1015–1035 (2014). · DOI
  66. Hu, M. M. et al. Sumoylation promotes the stability of the DNA sensor cGAS and the adaptor STING to regulate the kinetics of response to DNA virus. Immunity 45, 555–569 (2016). · DOI
  67. Cuervo, A. M. & Dice, J. F. Age-related decline in chaperone-mediated autophagy. J. Biol. Chem. 275, 31505–31513 (2000). · DOI · Paper page
  68. Rodriguez-Muela, N. et al. Balance between autophagic pathways preserves retinal homeostasis. Aging Cell 12, 478–488 (2013). · DOI
  69. Cai, Z. et al. Chaperone-mediated autophagy: roles in neuroprotection. Neurosci. Bull. 31, 452–458 (2015). · DOI
  70. Cuervo, A. M. & Wong, E. Chaperone-mediated autophagy: roles in disease and aging. Cell Res. 24, 92–104 (2014). · DOI
  71. Mak, S. K., McCormack, A. L., Manning-Bog, A. B., Cuervo, A. M. & Di Monte, D. A. Lysosomal degradation of alpha-synuclein in vivo. J. Biol. Chem. 285, 13621–13629 (2010). · DOI
  72. Malkus, K. A. & Ischiropoulos, H. Regional deficiencies in chaperone-mediated autophagy underlie alpha-synuclein aggregation and neurodegeneration. Neurobiol. Dis. 46, 732–744 (2012). · DOI
  73. Orenstein, S. J. et al. Interplay of LRRK2 with chaperone-mediated autophagy. Nat. Neurosci. 16, 394–406 (2013). · DOI · Paper page
  74. 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. 283, 23731–23738 (2008). · DOI · Paper page
  75. Andersson, F. I. et al. The effect of Parkinson’s-disease-associated mutations on the deubiquitinating enzyme UCH-L1. J. Mol. Biol. 407, 261–272 (2011). · DOI
  76. Huang, C. C. et al. Metabolism and mis-metabolism of the neuropathological signature protein TDP-43. J. Cell Sci. 127, 3024–3038 (2014). · DOI
  77. Koga, H. et al. Constitutive upregulation of chaperone-mediated autophagy in Huntington’s disease. J. Neurosci. 31, 18492–18505 (2011). · DOI
  78. Qi, L. et al. The role of chaperone-mediated autophagy in huntingtin degradation. PLoS ONE 7, e46834 (2012). · DOI
  79. Xilouri, M., Vogiatzi, T., Vekrellis, K., Park, D. & Stefanis, L. Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy. PLoS ONE 4, e5515 (2009). · DOI
  80. Xilouri, M. et al. Impairment of chaperone-mediated autophagy induces dopaminergic neurodegeneration in rats. Autophagy 12, 2230–2247 (2016). · DOI
  81. Xilouri, M. et al. Boosting chaperone-mediated autophagy in vivo mitigates alpha-synuclein-induced neurodegeneration. Brain 136, 2130–2146 (2013). First evidence of antidegenerative effect of genetic enhancement of CMA. · DOI
  82. Gan, L., Vargas, M. R., Johnson, D. A. & Johnson, J. A. Astrocyte-specific overexpression of Nrf2 delays motor pathology and synuclein aggregation throughout the CNS in the alpha-synuclein mutant (A53T) mouse model. J. Neurosci. 32, 17775–17787 (2012). · DOI
  83. Magalhaes, J. et al. Autophagic lysosome reformation dysfunction in glucocerebrosidase deficient cells: relevance to Parkinson disease. Hum. Mol. Genet. 25, 3432–3445 (2016). · DOI
  84. Alvarez-Erviti, L. et al. Chaperone-mediated autophagy markers in Parkinson disease brains. Arch. Neurol. 67, 1464–1472 (2010). · DOI
  85. Pang, S., Chen, D., Zhang, A., Qin, X. & Yan, B. Genetic analysis of the LAMP-2 gene promoter in patients with sporadic Parkinson’s disease. Neurosci. Lett. 526, 63–67 (2012). · DOI
  86. Alvarez-Erviti, L. et al. Influence of microRNA deregulation on chaperone-mediated autophagy and alpha-synuclein pathology in Parkinson’s disease. Cell Death Dis. 4, e545 (2013). · DOI
  87. Park, J. S., Kim, D. H. & Yoon, S. Y. Regulation of amyloid precursor protein processing by its KFERQ motif. BMB Rep. 49, 337–342 (2016). · DOI
  88. 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. 23, 3383–3392 (2009). · DOI
  89. Saha, T. LAMP2A overexpression in breast tumors promotes cancer cell survival via chaperone-mediated autophagy. Autophagy 8, 1643–1656 (2012). · DOI
  90. Zhang, Y. et al. Acetylation targets HSD17B4 for degradation via the CMA pathway in response to estrone. Autophagy 13, 538–553 (2017). · DOI
  91. Du, C. et al. 5-Fluorouracil targets histone acetyltransferases p300/CBP in the treatment of colorectal cancer. Cancer Lett. 400, 183–193 (2017). · DOI
  92. Ding, Z. B. et al. Lamp2a is required for tumor growth and promotes tumor recurrence of hepatocellular carcinoma. Int. J. Oncol. 49, 2367–2376 (2016). · DOI
  93. Wu, J. H. et al. CMA down-regulates p53 expression through degradation of HMGB1 protein to inhibit irradiation-triggered apoptosis in hepatocellular carcinoma. World J. Gastroenterol. 23, 2308–2317 (2017). · DOI
  94. Chava, S. et al. Chaperone-mediated autophagy compensates for impaired macroautophagy in the cirrhotic liver to promote hepatocellular carcinoma. Oncotarget 8, 40019–40036 (2017). · DOI
  95. Guo, B. et al. M2 tumor-associated macrophages produce interleukin-17 to suppress oxaliplatin-induced apoptosis in hepatocellular carcinoma. Oncotarget 8, 44465–44476 (2017). · DOI
  96. Ali, A. B., Nin, D. S., Tam, J. & Khan, M. Role of chaperone mediated autophagy (CMA) in the degradation of misfolded N-CoR protein in non-small cell lung cancer (NSCLC) cells. PLoS ONE 6, e25268 (2011). · DOI
  97. Vakifahmetoglu-Norberg, H. et al. Chaperone-mediated autophagy degrades mutant p53. Genes Dev. 27, 1718–1730 (2013). · DOI
  98. Xie, W. et al. Chaperone-mediated autophagy prevents apoptosis by degrading BBC3/PUMA. Autophagy 11, 1623–1635 (2015). · DOI
  99. Suzuki, J., Nakajima, W., Suzuki, H., Asano, Y. & Tanaka, N. Chaperone-mediated autophagy promotes lung cancer cell survival through selective stabilization of the pro-survival protein, MCL1. Biochem. Biophys. Res. Commun. 482, 1334–1340 (2017). · DOI
  100. Xia, H. G. et al. Degradation of HK2 by chaperone-mediated autophagy promotes metabolic catastrophe and cell death. J. Cell Biol. 210, 705–716 (2015). · DOI · Paper page
  101. Galan-Acosta, L., Xia, H., Yuan, J. & Vakifahmetoglu-Norberg, H. Activation of chaperone-mediated autophagy as a potential anticancer therapy. Autophagy 11, 2370–2371 (2015). · DOI
  102. Gomes, L. R., Menck, C. F. M. & Cuervo, A. M. Chaperone-mediated autophagy prevents cellular transformation by regulating MYC proteasomal degradation. Autophagy 13, 928–940 (2017). · DOI
  103. Lu, T. L. et al. Hispolon promotes MDM2 downregulation through chaperone-mediated autophagy. Biochem. Biophys. Res. Commun. 398, 26–31 (2010). · DOI
  104. Garg, A. D., Dudek, A. M. & Agostinis, P. Calreticulin surface exposure is abrogated in cells lacking, chaperone-mediated autophagy-essential gene, LAMP2A. Cell Death Dis. 4, e826 (2013). · DOI
  105. Kaushik, S. & Cuervo, A. M. Methods to monitor chaperone-mediated autophagy. Methods Enzymol. 452, 297–324 (2009). · DOI
  106. Li, P. et al. Degradation of AF1Q by chaperone-mediated autophagy. Exp. Cell Res. 327, 48–56 (2014). · DOI
  107. Gao, L. et al. Oxidation of survival factor MEF2D in neuronal death and Parkinson’s disease. Antioxid. Redox Signal 20, 2936–2948 (2014). · DOI
  108. Li, G. et al. Targeted suppression of chaperone-mediated autophagy by miR-320a promotes alpha-synuclein aggregation. Int. J. Mol. Sci. 15, 15845–15857 (2014). · DOI
  109. Wu, G. et al. Altered expression of autophagic genes in the peripheral leukocytes of patients with sporadic Parkinson’s disease. Brain Res. 1394, 105–111 (2011). · DOI
  110. Sala, G. et al. Reduced expression of the chaperone-mediated autophagy carrier hsc70 protein in lymphomonocytes of patients with Parkinson’s disease. Brain Res. 1546, 46–52 (2014). · DOI
  111. Wang, H. et al. Overexpression of PLK3 mediates the degradation of abnormal prion proteins dependent on chaperone-mediated autophagy. Mol. Neurobiol. 54, 4401–4413 (2017). · DOI
  112. Pedrozo, Z. et al. Cardiomyocyte ryanodine receptor degradation by chaperone-mediated autophagy. Cardiovasc. Res. 98, 277–285 (2013). · DOI
  113. Fidzianska, A., Walczak, E. & Walski, M. Abnormal chaperone-mediated autophagy (CMA) in cardiomyocytes of a boy with Danon disease. Folia Neuropathol. 45, 133–139 (2007).
  114. Metrailler, S., Schorderet, D. F. & Cottet, S. Early apoptosis of rod photoreceptors in Rpe65(−/−) mice is associated with the upregulated expression of lysosomal-mediated autophagic genes. Exp. Eye Res. 96, 70–81 (2012). · DOI
  115. Li, Y., Lu, L., Luo, N., Wang, Y. Q. & Gao, H. M. Inhibition of PI3K/AKt/mTOR signaling pathway protects against d-galactosamine/lipopolysaccharide-induced acute liver failure by chaperone-mediated autophagy in rats. Biomed. Pharmacother. 92, 544–553 (2017). · DOI
  116. Das, S. et al. Purinergic receptor X7 is a key modulator of metabolic oxidative stress-mediated autophagy and inflammation in experimental nonalcoholic steatohepatitis. Am. J. Physiol. Gastrointest. Liver Physiol. 305, G950–G963 (2013). · DOI
  117. Cai, Y. et al. The detrimental role played by lipocalin-2 in alcoholic fatty liver in mice. Am. J. Pathol. 186, 2417–2428 (2016). · DOI
  118. Lee, C. H., Lee, K. H., Jang, A. H. & Yoo, C. G. The impact of autophagy on the cigarette smoke extract-induced apoptosis of bronchial epithelial cells. Tuberc. Respir. Dis. 80, 83–89 (2017). · DOI
  119. 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. 65, 2135–2144 (2004). · DOI
  120. Cacciottolo, M., Nogalska, A., D’Agostino, C., Engel, W. K. & Askanas, V. Chaperone-mediated autophagy components are upregulated in sporadic inclusion-body myositis muscle fibres. Neuropathol. Appl. Neurobiol. 39, 750–761 (2013). · DOI
  121. Su, M. et al. HDAC6 regulates the chaperone-mediated autophagy to prevent oxidative damage in injured neurons after experimental spinal cord injury. Oxid. Med. Cell Longev. 2016, 7263736 (2016). · DOI
  122. Park, Y. et al. Chaperone-mediated autophagy after traumatic brain injury. J. Neurotrauma 32, 1449–1457 (2015). · DOI
  123. Macri, C. et al. Modulation of deregulated chaperone-mediated autophagy by a phosphopeptide. Autophagy 11, 472–486 (2015). · DOI
  124. Venugopal, B. et al. Chaperone-mediated autophagy is defective in mucolipidosis type IV. J. Cell. Physiol. 219, 344–353 (2009). · DOI

Cited by

Sorted by citations

Metadata

Authors
Kaushik, S., & Cuervo, A. M.
ORCID
Cuervo, Ana Maria
Venue
Nature Reviews Molecular Cell Biology
Publisher
Springer Science and Business Media LLC
Published
2018-04-06
Volume
19
Issue
6
Pages
365-381
ISSN
  • 1471-0072
  • 1471-0080
DOI
10.1038/s41580-018-0001-6
PMC
PMC6399518
Cited by
1,407
References
13
Language
en
Licence
www.springer.com/tdm (tdm)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review