A Receptor for the Selective Uptake and Degradation of Proteins by Lysosomes
Abstract
Multiple pathways of protein degradation operate within cells. A selective protein import pathway exists for the uptake and degradation of particular cytosolic proteins by lysosomes. Here, the lysosomal membrane glycoprotein LGP96 was identified as a receptor for the selective import and degradation of proteins within lysosomes. Specific substrates of this proteolytic pathway bound to the cytosolic tail of a 96-kilodalton lysosomal membrane protein in two different binding assays. Overexpression of human LGP96 in Chinese hamster ovary cells increased the activity of the selective lysosomal proteolytic pathway in vivo and in vitro.
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- Authors
- Cuervo, A. M., & Dice, J. F.
- Affiliations
- Department of Physiology, Tufts University School of Medicine, 136 Harrison Avenue, Boston, MA 02111, USA.
- Tufts University (US)
- Corresponding author
- Dice, J. Fred
- Venue
- Science
- Published
- 1996-07-26
- Volume
- 273
- Issue
- 5274
- Pages
- 501-503
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1968322176
- Cited by
- 979
- References
- 0
- Citations by year
- 2026: 28 · 2025: 37 · 2024: 49 · 2023: 41 · 2022: 53 · 2021: 54 · 2020: 49 · 2019: 53 · 2018: 56 · 2017: 43 · 2016: 50 · 2015: 49 · 2014: 27 · 2013: 46 · 2012: 37
- FWCI
- 14.92
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (AG-06116)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- lysosomal membrane glycoprotein, lysosomal protein degradation, selective autophagy, receptor identification, lysosomal proteolysis, protein binding
- MeSH terms
- Amino Acid Sequence, Animals, Glyceraldehyde-3-Phosphate Dehydrogenases, Cricetinae, Heat-Shock Proteins, Humans, Intracellular Membranes, Lysosomes, Membrane Glycoproteins, Molecular Sequence Data, Proteins, Ribonuclease, Pancreatic, Transfection, Antigens, CD, CHO Cells, HSP70 Heat-Shock Proteins, HSC70 Heat-Shock Proteins, Rats, Lysosomal Membrane Proteins, Lysosomal-Associated Membrane Protein 2
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