ArticleThe Journal of cell biology1995
Transferrin-binding protein complex is the receptor for transferrin uptake in Trypanosoma brucei.
Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 169 citations in OpenAlex.
- Article
- Article
- Comparative genomics and transcriptomics of theResearch square · 2025Article
- A transferrin receptor's guide to African trypanosomes.Cell surface (Amsterdam, Netherlands) · 2023Review
- A receptor for the complement regulator factor H increases transmission of trypanosomes to tsetse flies.Nature communications · 2020Article
- Steric constraints control processing of glycosylphosphatidylinositol anchors inThe Journal of biological chemistry · 2020Article
- The Trypanosomal Transferrin Receptor of Trypanosoma Brucei-A Review.Tropical medicine and infectious disease · 2019Review
- Endoplasmic reticulum-associated degradation and disposal of misfolded GPI-anchored proteins in Trypanosoma brucei.Molecular biology of the cell · 2018Article
- Rab11 mediates selective recycling and endocytic trafficking in Trypanosoma brucei.Traffic (Copenhagen, Denmark) · 2018Article
- Dynamic regulation of the Trypanosoma brucei transferrin receptor in response to iron starvation is mediated via the 3'UTR.PloS one · 2018Article
- Controlling transferrin receptor trafficking with GPI-valence in bloodstream stage African trypanosomes.PLoS pathogens · 2017Article
- Surface proteins, ERAD and antigenic variation in Trypanosoma brucei.Cellular microbiology · 2016Article
- Trypanocidal and cysteine protease inhibitory activity of isopentyl caffeate is not linked in Trypanosoma brucei.Parasitology research · 2016Article
- Glycogen Synthase Kinase 3β Promotes the Endocytosis of Transferrin in the African Trypanosome.ACS infectious diseases · 2016Article
- A Gene of the β3-Glycosyltransferase Family Encodes N-Acetylglucosaminyltransferase II Function in Trypanosoma brucei.The Journal of biological chemistry · 2016Article
- Development of a quantitative fluorescence-based ligand-binding assay.Scientific reports · 2016Article
- Loss of the BBSome perturbs endocytic trafficking and disrupts virulence of Trypanosoma brucei.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Identification of a glycosylphosphatidylinositol anchor-modifying β1-3 galactosyltransferase in Trypanosoma brucei.Glycobiology · 2015Article
- ATG24 Represses Autophagy and Differentiation and Is Essential for Homeostasy of the Flagellar Pocket in Trypanosoma brucei.PloS one · 2015Article
- Iron Homeostasis and Trypanosoma brucei Associated Immunopathogenicity Development: A Battle/Quest for Iron.BioMed research international · 2015Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Trypanosoma brucei, the products of two genes, ESAG 6 and ESAG 7, located upstream of the variant surface glycoprotein gene in a polycistronic expression site form a glycosylphosphatidylinositol-anchored transferrin-binding protein (TFBP) complex. It is shown by gel filtration and membrane-binding experiments that the TFBP complex is heterodimeric and binds one molecule of transferrin with high affinity (2,300 binding sites per cell; KD = 2.1 nM for the dominant expression site from T. brucei strain 427 and KD = 131 nM for ES1.3A of the EATRO 1125 stock). The ternary transferrin-TFBP complexes with iron-loaded or iron-free ligand are stable between pH 5 and 8. Cellular transferrin uptake can be inhibited by 90% with Fab fragments from anti-TFBP antibodies. After uptake, the TFBP complex and its ligand are routed to lysosomes where transferrin is proteolytically degraded. While the degradation products are released from the cells, iron remains cell associated and the TFBP complex is probably recycled to the membrane of the flagellar pocket, the only site for exo- and endocytosis in this organism. It is concluded that the TFBP complex serves as the receptor for the uptake of transferrin in T. brucei by a mechanism distinct from that in mammalian cells.
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