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Chaperone-mediated autophagy. Molecular mechanisms and physiological relevance
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“CMA is a very specific lysosomal degradation pathway where proteins bound to Hsc70-containing chaperone and co-chaperone complexes are recognized by the LAMP-2A receptor via a specific consensus sequence and subsequently degraded in lysosomes (41)(42)(43).”
From A Unique Carboxyl-terminal Insert Domain in the Hematopoietic-specific, GTPase-deficient Rho GTPase RhoH Regulates Post-translational Processing (2013) · cites this paper as [42]
In the citing paper
“As LAMP-2A receptormediated lysosomal protein uptake requires a specific recognition sequence and substrate translocation occurs in a stoichiometric fashion in CMA”
From A Unique Carboxyl-terminal Insert Domain in the Hematopoietic-specific, GTPase-deficient Rho GTPase RhoH Regulates Post-translational Processing (2013) · cites this paper as [42]
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Citations
Cites
Autophagy fights disease through cellular self-digestion
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Self-citationRegulation mechanisms and signaling pathways of autophagy
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Protein degradation and protection against misfolded or damaged proteins.
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Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy
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Self-citationTau 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 · cited 2×
“As in the case of α-synuclein, the pathogenic forms of tau also organize into irreversible oligomeric structures at the lysosomal membrane that interfere with normal CMA, and in this case, also often result in destabilization of the lysosomal membrane and lysosomal enzyme leakage into the cytosol [48].”
BackgroundChaperone-mediated autophagy: selectivity pays off
Cuervo, A. M. (2010) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2009.10.003 · Cited by 260 · cited 4×
“CMA is a uniquely selective form of autophagy by which specific cytosolic proteins are transported one-by-one across the lysosomal membrane for degradation [10,11].”
BackgroundInfluentialSelf-citationKabuta, T., Furuta, A., Aoki, S., Furuta, K., & Wada, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801918200 · Cited by 227
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., Martinez-Vicente, M., & Cuervo, A. M. (2007) · Journal of Cell Science · doi:10.1242/jcs.001073 · Cited by 213
Self-citationCathepsin A regulates chaperone‐mediated autophagy through cleavage of the lysosomal receptor
Cuervo, A. M., Mann, L., Bonten, E. J., d'Azzo, A., & Dice, J. F. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg002 · Cited by 182
Self-citation
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Cited by
Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1
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
An Overview of Autophagy: Morphology, Mechanism, and Regulation
Parzych, K. R., & Klionsky, D. J. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5371 · Cited by 2,521
The pathways of mitophagy for quality control and clearance of mitochondria
Ashrafi, G., & Schwarz, T. L. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2012.81 · Cited by 1,900
Age and Age-Related Diseases: Role of Inflammation Triggers and Cytokines
Rea, I. M., Gibson, D. S., McGilligan, V., McNerlan, S. E., Alexander, H. D., & Ross, O. A. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00586 · Cited by 1,267
Autophagy during viral infection — a double-edged sword
Choi, Y., Bowman, J. W., & Jung, J. U. (2018) · Nature Reviews Microbiology · doi:10.1038/s41579-018-0003-6 · Cited by 838
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
Metadata
- Authors
- Orenstein, S. J., & Cuervo, A. M.
- Venue
- Seminars in Cell & Developmental Biology
- Publisher
- Elsevier BV
- Published
- 2010-09
- Volume
- 21
- Issue
- 7
- Pages
- 719-726
- ISSN
- 1084-9521
- PMC
- PMC2914824
- Cited by
- 260
- References
- 9
- Language
- en
- Funders
- NIA (AG021904, AG031782)
- NIDKK (DK041918)
- NINDS (NS038370)
- NIH/NIA (T32 AG023475)
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