A novel class of cysteine protease receptors that mediate lysosomal transport.
Cell Microbiol, 2012/8;14(8):1299-317.
Nakada-Tsukui K[1], Tsuboi K, Furukawa A, Yamada Y, Nozaki T
Affiliations
PMID: 22486861DOI: 10.1111/j.1462-5822.2012.01800.x
Impact factor: 4.115
Abstract
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.
MeSH terms
Amino Acid Sequence; Animals; CHO Cells; Cricetinae; Cysteine Proteases; Endoplasmic Reticulum; Entamoeba histolytica; Gene Expression; Host-Parasite Interactions; Kinetics; Lysosomes; Molecular Sequence Data; Oligonucleotide Array Sequence Analysis; Phagosomes; Protein Binding; Protein Interaction Domains and Motifs; Protein Transport; Protozoan Proteins; Receptors, Cell Surface; Transcriptome
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