The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Regulation of Lamp2a Levels in the Lysosomal Membrane
Open accessAbstract
The selective degradation of cytosolic proteins in lysosomes by chaperone‐mediated autophagy depends, at least in part, on the levels of a substrate receptor at the lysosomal membrane. We have previously identified this receptor as the lysosome‐associated membrane protein type 2a (lamp2a) and showed that levels of lamp2a at the lysosomal membrane directly correlate with the activity of the proteolytic pathway. Here we show that levels of lamp2a at the lysosomal membrane are mainly controlled by changes in its half‐life and its distribution between the lysosomal membrane and the matrix. The lysosomal degradation of lamp2a requires the combined action of at least two different proteolytic activities at the lysosomal membrane. Lamp2a is released from the membrane by the action of these proteases, and then the truncated lamp2a is rapidly degraded within the lysosomal matrix. Membrane degradation of lamp2a is a regulated process that is inhibited in the presence of substrates for chaperone‐mediated autophagy and under conditions that activate that type of autophagy. Uptake of substrate proteins also results in transport of some intact lamp2a from the lysosomal membrane into the matrix. This fraction of lamp2a can be reinserted back into the lysosomal membrane. The traffic of lamp2a through the lysosomal matrix is not mediated by vesicles, and lamp2a reinsertion requires the lysosomal membrane potential and protein components of the lysosomal membrane. The distribution of lamp2a between the lysosomal membrane and matrix is a dynamic process that contributes to the regulation of lysosomal membrane levels of lamp2a and consequently to the activity of the chaperone‐mediated autophagic pathway.
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.
Integrity signals
Registry
Cites
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.
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
Carlsson, S. R., Roth, J., Piller, F., & Fukuda, M. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37369-1 · Cited by 345
Cited by
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 coming of age of chaperone-mediated autophagy
Kaushik, S., & Cuervo, A. M. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0001-6 · Cited by 1,407
Self-citationMolecular Mechanisms and Potential Therapeutical Targets in Huntington's Disease
Zuccato, C., Valenza, M., & Cattaneo, E. (2010) · Physiological Reviews · doi:10.1152/physrev.00041.2009 · Cited by 848
Lysosomal storage disorders: The cellular impact of lysosomal dysfunction
Platt, F. M., Boland, B., & van der Spoel, A. C. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201208152 · Cited by 689
Age-related decline in chaperone-mediated autophagy
Cuervo, A. M., & Dice, J. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002102200 · Cited by 665
Self-citationInterplay of LRRK2 with chaperone-mediated autophagy
Orenstein, S. J., Kuo, S.-H., Tasset, I., Arias, E., Koga, H., Fernandez-Carasa, I., Cortes, E., Honig, L. S., Dauer, W., Consiglio, A., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3350 · Cited by 588
Self-citationConsequences of the selective blockage of chaperone-mediated autophagy
Massey, A. C., Kaushik, S., Sovak, G., Kiffin, R., & Cuervo, A. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507436103 · Cited by 529
Self-citationNew insights into the role of mitochondria in aging: mitochondrial dynamics and more
Seo, A. Y., Joseph, A.-M., Dutta, D., Hwang, J. C. Y., Aris, J. P., & Leeuwenburgh, C. (2010) · Journal of Cell Science · doi:10.1242/jcs.070490 · Cited by 522
Reduced glucocerebrosidase is associated with increased α-synuclein in sporadic Parkinson’s disease
Murphy, K. E., Gysbers, A. M., Abbott, S. K., Tayebi, N., Kim, W. S., Sidransky, E., Cooper, A., Garner, B., & Halliday, G. M. (2014) · Brain · doi:10.1093/brain/awt367 · Cited by 475
Deficient Chaperone-Mediated Autophagy in Liver Leads to Metabolic Dysregulation
Schneider, J. L., Suh, Y., & Cuervo, A. M. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.06.009 · Cited by 340
Self-citationChaperone-mediated autophagy prevents collapse of the neuronal metastable proteome
Bourdenx, M., Martín-Segura, A., Scrivo, A., Rodriguez-Navarro, J. A., Kaushik, S., Tasset, I., Diaz, A., Storm, N. J., Xin, Q., Juste, Y. R., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.048 · Cited by 337
Self-citationRole of LAMP-2 in Lysosome Biogenesis and Autophagy
Eskelinen, E.-L., Illert, A. L., Tanaka, Y., Schwarzmann, G., Blanz, J., von Figura, K., & Saftig, P. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-02-0114 · Cited by 323
Chaperone-mediated autophagy in aging and disease
Massey, A. C., Zhang, C., & Cuervo, A. M. (2006) · Current Topics in Developmental Biology · doi:10.1016/s0070-2153(05)73007-6 · Cited by 315
Self-citationChaperone-mediated autophagy: selectivity pays off
Cuervo, A. M. (2010) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2009.10.003 · Cited by 260
“Conditions associated with enhanced CMA always require high LAMP-2A levels, which can be attained by transcriptional upregulation of the Lamp2 gene [28], but more often through changes in the degradation and lysosomal distribution of LAMP-2A [19].”
BackgroundSelf-citationChaperone-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
Self-citationValdor, R., Mocholi, E., Botbol, Y., Guerrero-Ros, I., Chandra, D., Koga, H., Gravekamp, C., Cuervo, A. M., & Macian, F. (2014) · Nature Immunology · doi:10.1038/ni.3003 · Cited by 244
Self-citationOtto, G. P., Wu, M. Y., Kazgan, N., Anderson, O. R., & Kessin, R. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212467200 · Cited by 221
Pajares, M., Rojo, A. I., Arias, E., Díaz-Carretero, A., Cuervo, A. M., & Cuadrado, A. (2018) · Autophagy · doi:10.1080/15548627.2018.1474992 · Cited by 218
Self-citationAltered 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-citationYou say lipofuscin, we say ceroid: Defining autofluorescent storage material
Seehafer, S. S., & Pearce, D. A. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.12.006 · Cited by 212
Cathepsin 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-citationThe aging lysosome: An essential catalyst for late-onset neurodegenerative diseases
Nixon, R. A. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140443 · Cited by 149
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
Lysosomal multienzyme complex: pros and cons of working together
Bonten, E. J., Annunziata, I., & d’Azzo, A. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1538-3 · Cited by 117
Autophagic response to exercise training in skeletal muscle with age
Kim, Y. A., Kim, Y. S., Oh, S. L., Kim, H.-J., & Song, W. (2013) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-013-0246-7 · Cited by 108
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
The physiology of the retinal pigment epithelium in Danon disease
Thompson, D. A., Constable, P. A., Liasis, A., Walters, B., & Esteban, M. T. (2016) · Retina · doi:10.1097/iae.0000000000000736 · Cited by 31
(2012) · PubMed
Metadata
- Authors
- Cuervo, A. M., & Dice, J. F.
- Venue
- Traffic
- Publisher
- Wiley
- Published
- 2000-07
- Volume
- 1
- Issue
- 7
- Pages
- 570-583
- ISSN
- 1398-9219 (ISSN-L)
- 1600-0854
- OpenAlex
- W2168445378
- Cited by
- 292
- References
- 1
- FWCI
- 2.83
- Type
- journal article
- Language
- en
- Open access
- bronze
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
