| Regulation of protein phosphatase type 1 and cell cycle progression by PfLRR1, a novel leucine-rich repeat protein of the human malaria parasite Plasmodium falciparum. | |
| | |
MedLine Citation:
|
PMID: 16629662 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
The protein called 'suppressor of the dis2 mutant (sds22+)' is an essential regulator of cell division in fission and budding yeasts, where its deletion causes mitotic arrest. Its role in cell cycle control appears to be mediated through the activation of protein phosphatase type 1 (PP1) in Schizosaccharomyces pombe. We have identified the Plasmodium falciparum Sds22 orthologue, which we designated PfLRR1 as it belongs to the leucine-rich repeat protein family. We showed by glutathione-S-transferase pull-down assay that the PfLRR1 gene product interacts with PfPP1, that the PfLRR1-PfPP1 complex is present in parasite extracts and that PfLRR1 inhibits PfPP1 activity. Functional studies in Xenopus oocytes revealed that PfLRR1 interacted with endogenous PP1 and overcame the G2/M cell cycle checkpoint by promoting progression to germinal vesicle breakdown (GVBD). Confirmatory results showing the appearance of GVBD were observed when oocytes were treated with anti-PP1 antibodies or okadaic acid. Taken together, these observations suggest that PfLRR1 can regulate the cell cycle by binding to PP1 and regulating its activity. |
| | |
Authors:
|
Wassim Daher; Edith Browaeys; Christine Pierrot; Hélène Jouin; Daniel Dive; Edwige Meurice; Colette Dissous; Monique Capron; Stanislas Tomavo; Christian Doerig; Katia Cailliau; Jamal Khalife |
Publication Detail:
|
Type: Journal Article |
Journal Detail:
|
Title: Molecular microbiology Volume: 60 ISSN: 0950-382X ISO Abbreviation: Mol. Microbiol. Publication Date: 2006 May |
Date Detail:
|
Created Date: 2006-04-24 Completed Date: 2006-07-03 Revised Date: 2007-11-15 |
Medline Journal Info:
|
Nlm Unique ID: 8712028 Medline TA: Mol Microbiol Country: England |
Other Details:
|
Languages: eng Pagination: 578-90 Citation Subset: IM |
Affiliation:
|
Unité Inserm 547/IPL, Institut Pasteur, 1 rue du Pr Calmette, B.P. 245, 59019 Lille cedex, France. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Amino Acid Sequence Animals Cell Cycle / drug effects Cell Division / drug effects G2 Phase / drug effects Gene Expression Regulation* Humans Molecular Sequence Data Nuclear Proteins / chemistry, genetics Oocytes Phosphoprotein Phosphatases / genetics, metabolism* Plasmodium falciparum / cytology* Proteins / chemistry, genetics, metabolism*, pharmacology Schizosaccharomyces pombe Proteins / chemistry, genetics Sequence Homology, Amino Acid Xenopus |
| Chemical | |
Reg. No./Substance:
|
0/Nuclear Proteins; 0/Proteins; 0/Schizosaccharomyces pombe Proteins; 0/leucine-rich repeat proteins; 135316-05-1/sds22 protein, S pombe; EC 3.1.3.16/Phosphoprotein Phosphatases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Recombinant cytochromes c biogenesis systems I and II and analysis of haem delivery pathways in Esch...
Next Document: Two distinct regions of the large serine recombinase TnpX are required for DNA binding and biologica...