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Chaperone-Mediated Autophagy
Open accessAbstract
Chaperone-mediated autophagy (CMA) is a lysosomal pathway of proteolysis that is responsible for the degradation of 30% of cytosolic proteins under conditions of prolonged nutrient deprivation. Molecular chaperones in the cytosol and in the lysosomal lumen stimulate this proteolytic pathway. The molecular chaperones in the cytosol unfold substrate proteins prior to their translocation across the lysosomal membrane, while the chaperone in the lysosomal lumen is probably required to pull the substrate protein across the lysosomal membrane. A critical component for CMA is a receptor in the lysosomal membrane, the lysosome-associated membrane protein (LAMP) type 2A. LAMP-2A levels in the lysosomal membrane can be increased by reduced degradation and/or redistribution from the lysosomal lumen to the lysosomal membrane. Recent results show that CMA is also activated by oxidative stress, and in this case LAMP-2A is increased due to transcriptional regulation. CMA can be reduced by inhibitors of glucose-6-phosphate dehydrogenase and of the heat shock protein of 90 kDa. Reduction of levels of LAMP-2A using RNAi strategies reduces CMA activity, but macroautophagy is activated as a result. The decrease in CMA causes cells to be more susceptibile to oxidative and other stresses. LAMP-2A in the lysosomal membrane can be sequestered into cholesterol-rich microdomains where it is inactive. When CMA is activated, LAMP-2A moves out of these domains. The reduced CMA in aging is due to reduced LAMP-2A in the lysosomal membrane. This reduction is caused by an age-related increased degradation of LAMP-2A and an age-related reduced ability of LAMP-2A to reinsert into the lysosomal membrane. These findings reveal a rich complexity of mechanisms to control CMA activity.
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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894
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Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,897
Ferroptosis: machinery and regulation
Chen, X., Li, J., Kang, R., Klionsky, D. J., & Tang, D. (2021) · Autophagy · doi:10.1080/15548627.2020.1810918 · Cited by 2,099
Zhao, J., Brault, J. J., Schild, A., Cao, P., Sandri, M., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.004 · Cited by 1,489
Matsunaga, K., Saitoh, T., Tabata, K., Omori, H., Satoh, T., Kurotori, N., Maejima, I., Shirahama-Noda, K., Ichimura, T., Isobe, T., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1846 · Cited by 1,235
Biological and Chemical Approaches to Diseases of Proteostasis Deficiency
Powers, E. T., Morimoto, R. I., Dillin, A., Kelly, J. W., & Balch, W. E. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052308.114844 · Cited by 1,149
Autophagy gone awry in neurodegenerative diseases
Wong, E., & Cuervo, A. M. (2010) · Nature Neuroscience · doi:10.1038/nn.2575 · Cited by 815
A Sensitive and Quantitative Technique for Detecting Autophagic Events Based on Lysosomal Delivery
Katayama, H., Kogure, T., Mizushima, N., Yoshimori, T., & Miyawaki, A. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.05.013 · Cited by 650
Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing
Wang, Y., Martinez-Vicente, M., Krüger, U., Kaushik, S., Wong, E., Mandelkow, E.-M., Cuervo, A. M., & Mandelkow, E. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp367 · Cited by 617
The Role of Autophagy in the Heart
Sciarretta, S., Maejima, Y., Zablocki, D., & Sadoshima, J. (2018) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021317-121427 · Cited by 547
Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction
Tai, H.-C., & Schuman, E. M. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2499 · Cited by 532
Autophagy and aging: keeping that old broom working
Cuervo, A. M. (2008) · Trends in Genetics · doi:10.1016/j.tig.2008.10.002 · Cited by 527
Zhang, C., & Cuervo, A. M. (2008) · Nature Medicine · doi:10.1038/nm.1851 · Cited by 520
Protein Homeostasis and Aging: the importance of exquisite quality control
Koga, H., Kaushik, S., & Cuervo, A. M. (2011) · Ageing research reviews · doi:10.1016/j.arr.2010.02.001 · Cited by 476
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Nedelsky, N. B., Todd, P. K., & Taylor, J. P. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.10.002 · Cited by 351
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Calderwood, S. K., Murshid, A., & Prince, T. (2009) · Gerontology · doi:10.1159/000225957 · Cited by 304
Chung, T., Phillips, A. R., & Vierstra, R. D. (2010) · The Plant Journal · doi:10.1111/j.1365-313x.2010.04166.x · Cited by 285
Poly(ADP-ribose) signaling in cell death
Virág, L., Robaszkiewicz, A., Rodriguez-Vargas, J. M., & Oliver, F. J. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2013.01.007 · Cited by 273
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Chaperone-mediated autophagy. Molecular mechanisms and physiological relevance
Orenstein, S. J., & Cuervo, A. M. (2010) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2010.02.005 · Cited by 260
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Schröder, B. A., Wrocklage, C., Hasilik, A., & Saftig, P. (2010) · PROTEOMICS · doi:10.1002/pmic.201000196 · Cited by 226
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Oehme, I., Linke, J.-P., Böck, B. C., Milde, T., Lodrini, M., Hartenstein, B., Wiegand, I., Eckert, C., Roth, W., Kool, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300113110 · Cited by 221
Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease.
Chesser, A. S., Pritchard, S. M., & Johnson, G. V. W. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00122 · Cited by 219
Autophagy modulates SNCA/α-synuclein release, thereby generating a hostile microenvironment
Poehler, A.-M., Xiang, W., Spitzer, P., May, V. E. L., Meixner, H., Rockenstein, E., Chutna, O., Outeiro, T. F., Winkler, J., Masliah, E., et al. (2014) · Autophagy · doi:10.4161/auto.36436 · Cited by 212
Specific iron chelators determine the route of ferritin degradation
De Domenico, I., Ward, D. M., & Kaplan, J. (2009) · Blood · doi:10.1182/blood-2009-05-224188 · Cited by 176
Caccamo, A., Majumder, S., Deng, J. J., Bai, Y., Thornton, F. B., & Oddo, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.031278 · Cited by 169
Ordered Organelle Degradation during Starvation-induced Autophagy
Kristensen, A. R., Schandorff, S., Høyer-Hansen, M., Nielsen, M. O., Jaüaüttelaü, M., Dengjel, J., & Andersen, J. S. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800184-mcp200 · Cited by 165
Chaperone-mediated autophagy. Machinery, regulation and biological consequences
Li, W., Yang, Q., & Mao, Z. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0565-6 · Cited by 119
Chaperone‐mediated autophagy: Molecular mechanisms, biological functions, and diseases
Yao, R., & Shen, J. (2023) · MedComm · doi:10.1002/mco2.347 · Cited by 111
Wang, B., Cai, Z., Tao, K., Zeng, W., Lu, F., Yang, R., Feng, D., Gao, G., & Yang, Q. (2016) · Autophagy · doi:10.1080/15548627.2016.1179401 · Cited by 107
Chaperone mediated autophagy degrades TDP-43 protein and is affected by TDP-43 aggregation
Ormeño, F., Hormazabal, J., Moreno, J., Riquelme, F., Rios, J., Criollo, A., Albornoz, A., Alfaro, I. E., & Budini, M. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00019 · Cited by 80
Liu, B., Wang, T., Wang, H., Zhang, L., Xu, F., Fang, R., Li, L., Cai, X., Wu, Y., Zhang, W., et al. (2018) · Journal of Hematology & Oncology · doi:10.1186/s13045-018-0577-5 · Cited by 73
Chaperone-Mediated Autophagy and Its Emerging Role in Hematological Malignancies
Robert, G., Jacquel, A., & Auberger, P. (2019) · Cells · doi:10.3390/cells8101260 · Cited by 45
Bhattacharya, K., Maiti, S., Zahoran, S., Weidenauer, L., Hany, D., Wider, D., Bernasconi, L., Quadroni, M., Collart, M., & Picard, D. (2022) · Nature Communications · doi:10.1038/s41467-022-33916-3 · Cited by 40
Brown, C. R., Dunton, D., & Chiang, H.-L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.028241 · Cited by 29
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Zimmermann, A. C., Zarei, M., Eiselein, S., & Dengjel, J. (2010) · Autophagy · doi:10.4161/auto.6.8.12786 · Cited by 28
A selective autophagy pathway that degrades gluconeogenic enzymes during catabolite inactivation
Brown, C. R., & Chiang, H.-L. (2009) · Communicative & Integrative Biology · doi:10.4161/cib.7711 · Cited by 22
Troeger, A., Chae, H.-D., Senturk, M., Wood, J., & Williams, D. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.505727 · Cited by 15
(2012) · PubMed
Metadata
- Authors
- Dice, J. F.
- Venue
- Autophagy
- Publisher
- Informa UK Limited
- Published
- 2007-07-16
- Volume
- 3
- Issue
- 4
- Pages
- 295-299
- ISSN
- 1554-8627 (ISSN-L)
- 1554-8635
- OpenAlex
- W2112693824
- Cited by
- 569
- References
- 0
- FWCI
- 25.96
- Type
- journal article
- Language
- en
- Open access
- bronze
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