ArticleMolecular biology of the cell2004
Adaptor protein complex 1 mediates the transport of lysosomal proteins from a Golgi-like organelle to peripheral vacuoles in the primitive eukaryote Giardia lamblia.
Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 64 citations in OpenAlex.
- Subunits of adaptor protein complex-1 make distinct contributions to the virulence ofInfection and immunity · 2026Article
- The history of giardiasis.Parasitology research · 2025Review
- Genomic survey maps differences in the molecular complement of vesicle formation machinery between Giardia intestinalis assemblages.PLoS neglected tropical diseases · 2023Article
- ADAPTOR PROTEIN-1 complex-mediated post-Golgi trafficking is critical for pollen wall development in Arabidopsis.The New phytologist · 2022Article
- Article
- Exosome Biogenesis in the Protozoa ParasiteCells · 2019Article
- Article
- Lactoferrin and lactoferricin endocytosis halt Giardia cell growth and prevent infective cyst production.Scientific reports · 2018Article
- Membrane-Associated Proteins inGenes · 2018Review
- Receptor-mediated endocytosis generates nanomechanical force reflective of ligand identity and cellular property.Journal of cellular physiology · 2018Article
- Myosin-independent cytokinesis inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
- Keeping Wnt signalosome in check by vesicular traffic.Journal of cellular physiology · 2015Review
- Article
- The giardial VPS35 retromer subunit is necessary for multimeric complex assembly and interaction with the vacuolar protein sorting receptor.Biochimica et biophysica acta · 2013Article
- Lysosomal protein trafficking in Giardia lamblia: common and distinct features.Frontiers in bioscience (Elite edition) · 2012Review
- Vacuolar protein sorting receptor in Giardia lamblia.PloS one · 2012Article
- Giardia lamblia low-density lipoprotein receptor-related protein is involved in selective lipoprotein endocytosis and parasite replication.Molecular microbiology · 2011Article
- Long double-stranded RNA produces specific gene downregulation in Giardia lamblia.The Journal of parasitology · 2010Article
- Adaptor protein 2 regulates receptor-mediated endocytosis and cyst formation in Giardia lamblia.The Biochemical journal · 2010Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Giardia lamblia is an early branching protist that possesses peripheral vacuoles (PVs) with characteristics of lysosome-like organelles, located underneath the plasma membrane. In more evolved cells, lysosomal protein trafficking is achieved by cargo recognition involving adaptor protein (AP) complexes that recognize specific amino acid sequences (tyrosine and/or dileucine motifs) within the cytoplasmic tail of membrane proteins. Previously, we reported that Giardia has a tyrosine-based sorting system, which mediates the targeting of a membrane-associated cysteine protease (encystation-specific cysteine protease, ESCP) to the PVs. Here, we show that Giardia AP1 mediates the transport of ESCP and the soluble acid phosphatase (AcPh) to the PVs. By using the yeast two-hybrid assay we found that the ESCP tyrosine-based motif interacts specifically with the medium subunit of AP1 (Gimicroa). Hemagglutinin-tagged Gimicroa colocalizes with ESCP and AcPh and coimmunoprecipitates with clathrin, suggesting that protein trafficking toward the PVs is clathrin-adaptin dependent. Targeted disruption of Gimicroa results in mislocalization of ESCP and AcPh but not of variant-specific surface proteins. Our results suggest that, unlike mammalian cells, only AP1 is involved in anterograde protein trafficking to the PVs in Giardia. Moreover, even though Giardia trophozoites lack a morphologically discernible Golgi apparatus, the presence of a clathrin-adaptor system suggests that this parasite possess a primitive secretory organelle capable of sorting proteins similar to that of more evolved cells.
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