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A novel class of cysteine protease receptors that mediate lysosomal transport
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- Kumiko Nakada‐Tsukui
- Department of Parasitology, National Institute of Infectious Diseases, 1‐23‐1 Toyama, Shinjuku, Tokyo 162‐8640, Japan
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- Kumiko Tsuboi
- Department of Parasitology, National Institute of Infectious Diseases, 1‐23‐1 Toyama, Shinjuku, Tokyo 162‐8640, Japan
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- Atsushi Furukawa
- Department of Parasitology, National Institute of Infectious Diseases, 1‐23‐1 Toyama, Shinjuku, Tokyo 162‐8640, Japan
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- Yoko Yamada
- Department of Parasitology, Gunma University Graduate School of Medicine, 3‐39‐22 Showa‐machi, Maebashi 371‐8511, Japan
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- Tomoyoshi Nozaki
- Department of Parasitology, National Institute of Infectious Diseases, 1‐23‐1 Toyama, Shinjuku, Tokyo 162‐8640, Japan
Description
The transport of lysosomal proteins is, in general, mediated by mannose 6-phosphate receptors via carbohydrate modifications. Here, we describe a novel class of receptors that regulate the transport of lysosomal hydrolases in the enteric protozoan Entamoeba histolytica, which is a good model organism to investigate membrane traffic. A novel 110 kDa cysteine protease (CP) receptor (CP-binding protein family 1, CPBF1) was initially discovered by affinity co-precipitation of the major CP (EhCP-A5), which plays a pivotal role in the pathogenesis of E. histolytica. We demonstrated that CPBF1 regulates EhCP-A5 transport from the endoplasmic reticulum to lysosomes and its binding to EhCP-A5 is independent of carbohydrate modifications. Repression of CPBF1 by gene silencing led to the accumulation of the unprocessed form of EhCP-A5 in the non-acidic compartment and the mis-secretion of EhCP-A5, suggesting that CPBF1 is involved in the trafficking and processing of EhCP-A5. The CPBF represents a new class of transporters that bind to lysosomal hydrolases in a carbohydrate-independent fashion and regulate their trafficking, processing and activation and, thus, regulate the physiology and pathogenesis of E. histolytica.
Journal
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- Cellular Microbiology
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Cellular Microbiology 14 (8), 1299-1317, 2012-05-14
Hindawi Limited
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Keywords
- Molecular Sequence Data
- Protozoan Proteins
- Gene Expression
- Receptors, Cell Surface
- CHO Cells
- Endoplasmic Reticulum
- Host-Parasite Interactions
- Cysteine Proteases
- Cricetinae
- Phagosomes
- Animals
- Protein Interaction Domains and Motifs
- Amino Acid Sequence
- Oligonucleotide Array Sequence Analysis
- Entamoeba histolytica
- Original Articles
- Kinetics
- Protein Transport
- Lysosomes
- Transcriptome
- Protein Binding
Details 詳細情報について
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- CRID
- 1360567185577366400
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- ISSN
- 14625822
- 14625814
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- PubMed
- 22486861
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- Article Type
- journal article
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- Data Source
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- Crossref
- KAKEN
- OpenAIRE
