ArticleMolecular biology of the cell2014
Manganese induces oligomerization to promote down-regulation of the intracellular trafficking receptor used by Shiga toxin.
Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Shedding of GPP130 by PC7 and Furin: Potential Implication in Lung Cancer Progression.International journal of molecular sciences · 2025Article
- Review
- Isoform-dependent lysosomal degradation and internalization of apolipoprotein E requires autophagy proteins.Journal of cell science · 2022Article
- Therapeutic Strategies to Protect the Central Nervous System against Shiga Toxin from EnterohemorrhagicCurrent neuropharmacology · 2021Article
- Targeting the Early Endosome-to-Golgi Transport of Shiga Toxins as a Therapeutic Strategy.Toxins · 2020Review
- HHV-7 U21 exploits Golgi quality control carriers to reroute class I MHC molecules to lysosomes.Molecular biology of the cell · 2020Article
- Protein folding state-dependent sorting at the Golgi apparatus.Molecular biology of the cell · 2019Article
- Genome-wide siRNA screen identifies UNC50 as a regulator of Shiga toxin 2 trafficking.The Journal of cell biology · 2017Article
- Manganese-induced trafficking and turnover of GPP130 is mediated by sortilin.Molecular biology of the cell · 2017Article
- Protection against Shiga Toxins.Toxins · 2017Review
- Induced oligomerization targets Golgi proteins for degradation in lysosomes.Molecular biology of the cell · 2015Article
- Manganese Is Essential for Neuronal Health.Annual review of nutrition · 2015Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Manganese (Mn) protects cells against lethal doses of purified Shiga toxin by causing the degradation of the cycling transmembrane protein GPP130, which the toxin uses as a trafficking receptor. Mn-induced GPP130 down-regulation, in addition to being a potential therapeutic approach against Shiga toxicosis, is a model for the study of metal-regulated protein sorting. Significantly, however, the mechanism by which Mn regulates GPP130 trafficking is unknown. Here we show that a transferable trafficking determinant within GPP130 bound Mn and that Mn binding induced GPP130 oligomerization in the Golgi. Alanine substitutions blocking Mn binding abrogated both oligomerization of GPP130 and GPP130 sorting from the Golgi to lysosomes. Further, oligomerization was sufficient because forced aggregation, using a drug-controlled polymerization domain, redirected GPP130 to lysosomes in the absence of Mn. These experiments reveal metal-induced oligomerization as a Golgi sorting mechanism for a medically relevant receptor for Shiga toxin.
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Registered trials
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.