ArticleThe Journal of cell biology1997
Aggregation as a determinant of protein fate in post-Golgi compartments: role of the luminal domain of furin in lysosomal targeting.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 67 citations in OpenAlex.
- Isoform-dependent lysosomal degradation and internalization of apolipoprotein E requires autophagy proteins.Journal of cell science · 2022Article
- HHV-7 U21 exploits Golgi quality control carriers to reroute class I MHC molecules to lysosomes.Molecular biology of the cell · 2020Article
- Unlocking Golgi: Why Does Morphology Matter?Biochemistry. Biokhimiia · 2019Review
- Protein quality control in the secretory pathway.The Journal of cell biology · 2019Review
- Protein folding state-dependent sorting at the Golgi apparatus.Molecular biology of the cell · 2019Article
- Segregation in the Golgi complex precedes export of endolysosomal proteins in distinct transport carriers.The Journal of cell biology · 2017Article
- Manganese-induced trafficking and turnover of GPP130 is mediated by sortilin.Molecular biology of the cell · 2017Article
- Induced oligomerization targets Golgi proteins for degradation in lysosomes.Molecular biology of the cell · 2015Article
- Manganese induces oligomerization to promote down-regulation of the intracellular trafficking receptor used by Shiga toxin.Molecular biology of the cell · 2014Article
- Human herpesvirus 7 U21 tetramerizes to associate with class I major histocompatibility complex molecules.Journal of virology · 2014Article
- Calpain inhibition promotes the rescue of F(508)del-CFTR in PBMC from cystic fibrosis patients.PloS one · 2013Article
- Functional Rescue of F508del-CFTR Using Small Molecule Correctors.Frontiers in pharmacology · 2012Article
- Sortilin associates with transforming growth factor-beta family proteins to enhance lysosome-mediated degradation.The Journal of biological chemistry · 2011Article
- Quality control for unfolded proteins at the plasma membrane.The Journal of cell biology · 2010Article
- Diacylglycerol enrichment of endoplasmic reticulum or lipid droplets recruits perilipin 3/TIP47 during lipid storage and mobilization.The Journal of biological chemistry · 2009Article
- Selective processing and metabolism of disease-causing mutant prion proteins.PLoS pathogens · 2009Article
- Kinesin adapter JLP links PIKfyve to microtubule-based endosome-to-trans-Golgi network traffic of furin.The Journal of biological chemistry · 2009Article
- Prions and retroviruses: an endosomal rendezvous?EMBO reports · 2006Review
- Identification of a pH sensor in the furin propeptide that regulates enzyme activation.The Journal of biological chemistry · 2006Article
- A lumenal domain-dependent pathway for sorting to intralumenal vesicles of multivesicular endosomes involved in organelle morphogenesis.Developmental cell · 2006Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mammalian endopeptidase furin is a type 1 integral membrane protein that is predominantly localized to the TGN and is degraded in lysosomes with a t1/2 = 2-4 h. Whereas the localization of furin to the TGN is largely mediated by sorting signals in the cytosolic tail of the protein, we show here that targeting of furin to lysosomes is a function of the luminal domain of the protein. Inhibition of lysosomal degradation results in the accumulation of high molecular weight aggregates of furin; aggregation is also dependent on the luminal domain of furin. Temperature and pharmacologic manipulations suggest that furin aggregation occurs in the TGN and thus precedes delivery to lysosomes. These findings are consistent with a model in which furin becomes progressively aggregated in the TGN, an event that leads to its transport to lysosomes. Our observations indicate that changes in the aggregation state of luminal domains can be potent determinants of biosynthetic targeting to lysosomes and suggest the possible existence of quality control mechanisms for disposal of aggregated proteins in compartments of the secretory pathway other than the endoplasmic reticulum.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.