Cathepsin L occupies a vacuolar compartment and is a protein maturase within the endo/exocytic system of Toxoplasma gondii
dc.contributor.author | Parussini, Fabiola | en_US |
dc.contributor.author | Coppens, Isabelle | en_US |
dc.contributor.author | Shah, Parag P. | en_US |
dc.contributor.author | Diamond, Scott L. | en_US |
dc.contributor.author | Carruthers, Vern B. | en_US |
dc.date.accessioned | 2011-01-31T17:52:26Z | |
dc.date.available | 2011-08-02T18:19:14Z | en_US |
dc.date.issued | 2010-06 | en_US |
dc.identifier.citation | Parussini, Fabiola; Coppens, Isabelle; Shah, Parag P.; Diamond, Scott L.; Carruthers, Vern B.; (2010). "Cathepsin L occupies a vacuolar compartment and is a protein maturase within the endo/exocytic system of Toxoplasma gondii ." Molecular Microbiology 76(6): 1340-1357. <http://hdl.handle.net/2027.42/79312> | en_US |
dc.identifier.issn | 0950-382X | en_US |
dc.identifier.issn | 1365-2958 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/79312 | |
dc.description.abstract | Regulated exocytosis allows the timely delivery of proteins and other macromolecules precisely when they are needed to fulfil their functions. The intracellular parasite Toxoplasma gondii has one of the most extensive regulated exocytic systems among all unicellular organisms, yet the basis of protein trafficking and proteolytic modification in this system is poorly understood. We demonstrate that a parasite cathepsin protease, TgCPL, occupies a newly recognized va cuolar c ompartment (VAC) that undergoes dynamic fragmentation during T. gondii replication. We also provide evidence that within the VAC or late endosome this protease mediates the proteolytic maturation of proproteins targeted to micronemes, regulated secretory organelles that deliver adhesive proteins to the parasite surface during cell invasion. Our findings suggest that processing of microneme precursors occurs within intermediate endocytic compartments within the exocytic system, indicating an extensive convergence of the endocytic and exocytic pathways in this human parasite. | en_US |
dc.format.extent | 2660280 bytes | |
dc.format.extent | 17212421 bytes | |
dc.format.extent | 3106 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Blackwell Publishing Ltd | en_US |
dc.title | Cathepsin L occupies a vacuolar compartment and is a protein maturase within the endo/exocytic system of Toxoplasma gondii | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Microbiology and Immunology | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Microbiology and Immunology, University of Michigan, Ann Arbor, MI 48109, USA. | en_US |
dc.contributor.affiliationother | Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT 05405, USA. | en_US |
dc.contributor.affiliationother | Department of Molecular Microbiology and Immunology, Johns Hopkins University, Bloomberg School of Public Health, Baltimore, MD 21205, USA. | en_US |
dc.contributor.affiliationother | Institute for Medicine and Engineering, Penn Center for Molecular Discovery, University of Pennsylvania, Philadelphia, PA 19104, USA. | en_US |
dc.identifier.pmid | 20444089 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/79312/1/j.1365-2958.2010.07181.x.pdf | |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/79312/2/MMI_7181_sm_FigS1-8.pdf | |
dc.identifier.doi | 10.1111/j.1365-2958.2010.07181.x | en_US |
dc.identifier.source | Molecular Microbiology | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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