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Updated: Jul 18, 2026

Using Fluorescent Proteins to Monitor Glycosome Dynamics in the African Trypanosome
Published on: August 19, 2014
Characterization of glycosomal RING finger proteins of trypanosomatids
Tracy Saveria1, Peter Kessler, Bryan C Jensen
1Seattle Biomedical Research Institute, 307 Westlake Avenue N., Seattle, WA 98109, USA.
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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