ArticleExperimental parasitology2007
Characterization of glycosomal RING finger proteins of trypanosomatids.
Article in Experimental parasitology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Ultrastructural expansion microscopy reveals unexpected levels of glycosome heterogeneity in African trypanosomes.Journal of microscopy · 2026Article
- Glycosome heterogeneity in kinetoplastids.Biochemical Society transactions · 2021Review
- Environmentally regulated glycosome protein composition in the African trypanosome.Eukaryotic cell · 2013Article
- Conservation of PEX19-binding motifs required for protein targeting to mammalian peroxisomal and trypanosome glycosomal membranes.Eukaryotic cell · 2007Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
The glycosomes of trypanosomatids are essential organelles that are evolutionarily related to peroxisomes of other eukaryotes. The peroxisomal RING proteins-PEX2, PEX10 and PEX12-comprise a network of integral membrane proteins that function in the matrix protein import cycle. Here, we describe PEX10 and PEX12 in Trypanosoma brucei, Leishmania major, and Trypanosoma cruzi. We expressed GFP fusions of each T. brucei coding region in procyclic form T. brucei, where they localized to glycosomes and behaved as integral membrane proteins. Despite the weak transmembrane predictions for TbPEX12, protease protection assays demonstrated that both the N and C termini are cytosolic, similar to mammalian PEX12. GFP fusions of T. cruzi PEX10 and L. major PEX12 also localized to glycosomes in T. brucei indicating that glycosomal membrane protein targeting is conserved across trypanosomatids.
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