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Fatty acid acylation regulates trafficking of the unusual Plasmodium falciparum calpain to the nucleolus

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Title: Fatty acid acylation regulates trafficking of the unusual Plasmodium falciparum calpain to the nucleolus
Authors: Russo, Ilaria, Oksman, Anna, Goldberg, Daniel E.
Source: Mol Microbiol
Russo, I, Oksman, A & Goldberg, D E 2009, 'Fatty acid acylation regulates trafficking of the unusual Plasmodium falciparum calpain to the nucleolus', Molecular Microbiology, vol. 72, no. 1, pp. 229-245. https://doi.org/10.1111/j.1365-2958.2009.06639.x
Publisher Information: Wiley, 2009.
Publication Year: 2009
Subject Terms: 0301 basic medicine, Calpain, QH, Acylation, Lipoylation, Fatty Acids, Nuclear Localization Signals, Plasmodium falciparum, Protozoan Proteins, Fatty Acids/*metabolism, Transfection, Plasmodium falciparum/genetics/*metabolism, Protozoan Proteins/genetics/*metabolism, 3. Good health, Calpain/genetics/*metabolism, Cell Line, QH301, Protein Transport, 03 medical and health sciences, Animals, Humans, Cell Nucleolus/*metabolism, Research Articles, Cell Nucleolus, Phylogeny
Description: SummaryThe Plasmodium falciparum genome encodes a single calpain. By generating P. falciparum clones expressing C‐terminally tagged calpain, we localized this protein to the nucleolus. Pf_calpain possesses an unusual and long N‐terminal domain in which we identified three subregions that are highly conserved among Plasmodium species. Two have putative targeting signals: a myristoylation motif and a nuclear localization sequence. We assessed their functionality. Our data show that the nuclear localization sequence is an active nuclear import motif that contains an embedded signal conferring nucleolar localization on various chimeras. The N‐terminus is myristoylated at Gly2 and palmitoylated at Cys3 and Cys22. Palmitoylation status has an important role in dictating P. falciparum calpain localization. The targeting signals function in mammalian cells as well as in the parasite. P. falciparum calpain is a unique nucleolar protein with an interesting mechanism of targeting.
Document Type: Article
Other literature type
File Description: application/pdf
Language: English
ISSN: 1365-2958
0950-382X
DOI: 10.1111/j.1365-2958.2009.06639.x
Access URL: https://onlinelibrary.wiley.com/doi/pdfdirect/10.1111/j.1365-2958.2009.06639.x
https://pubmed.ncbi.nlm.nih.gov/19239622
http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2009.06639.x/full
https://www.research.manchester.ac.uk/portal/en/publications/fatty-acid-acylation-regulates-trafficking-of-the-unusual-plasmodium-falciparum-calpain-to-the-nucleolus(e1d40041-5837-4be8-86cc-f82900836255).html
https://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2009.06639.x
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2746569/pdf
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2746569/
https://www.cabdirect.org/cabdirect/abstract/20093110123
Rights: Wiley Online Library User Agreement
CC BY
Accession Number: edsair.doi.dedup.....54d2d003524f68076a11e72e8ea9fab2
Database: OpenAIRE
Description
Abstract:SummaryThe Plasmodium falciparum genome encodes a single calpain. By generating P. falciparum clones expressing C‐terminally tagged calpain, we localized this protein to the nucleolus. Pf_calpain possesses an unusual and long N‐terminal domain in which we identified three subregions that are highly conserved among Plasmodium species. Two have putative targeting signals: a myristoylation motif and a nuclear localization sequence. We assessed their functionality. Our data show that the nuclear localization sequence is an active nuclear import motif that contains an embedded signal conferring nucleolar localization on various chimeras. The N‐terminus is myristoylated at Gly2 and palmitoylated at Cys3 and Cys22. Palmitoylation status has an important role in dictating P. falciparum calpain localization. The targeting signals function in mammalian cells as well as in the parasite. P. falciparum calpain is a unique nucleolar protein with an interesting mechanism of targeting.
ISSN:13652958
0950382X
DOI:10.1111/j.1365-2958.2009.06639.x