scholarly journals Identification of Plasmodium falciparum Translation Initiation eIF2β Subunit: Direct Interaction with Protein Phosphatase Type 1

2016 ◽  
Vol 7 ◽  
Author(s):  
Géraldine Tellier ◽  
Astrid Lenne ◽  
Katia Cailliau-Maggio ◽  
Alejandro Cabezas-Cruz ◽  
James J. Valdés ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Translation Initiation ◽  
Protein Phosphatase ◽  
Direct Interaction ◽  
Protein Phosphatase Type 1 ◽  
Protein Phosphatase Type

scholarly journals Plasmodium falciparum encodes a conserved active inhibitor-2 for Protein Phosphatase type 1: perspectives for novel anti-plasmodial therapy

BMC Biology ◽  
2013 ◽  
Vol 11 (1) ◽  
pp. 80 ◽  
Author(s):  
Aline Fréville ◽  
Katia Cailliau-Maggio ◽  
Christine Pierrot ◽  
Géraldine Tellier ◽  
Hadidjatou Kalamou ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Protein Phosphatase ◽  
Active Inhibitor ◽  
Protein Phosphatase Type 1 ◽  
Protein Phosphatase Type

scholarly journals Analysis of the interactome of the Ser/Thr Protein Phosphatase type 1 in Plasmodium falciparum

BMC Genomics ◽  
2016 ◽  
Vol 17 (1) ◽  
Author(s):  
Thomas Hollin ◽  
Caroline De Witte ◽  
Astrid Lenne ◽  
Christine Pierrot ◽  
Jamal Khalife
Keyword(s):  
Plasmodium Falciparum ◽  
Protein Phosphatase ◽  
Protein Phosphatase Type 1 ◽  
Protein Phosphatase Type

scholarly journals Characterization of a Protein Phosphatase Type-1 and a Kinase Anchoring Protein in Plasmodium falciparum

2018 ◽  
Vol 9 ◽  
Author(s):  
Astrid Lenne ◽  
Caroline De Witte ◽  
Géraldine Tellier ◽  
Thomas Hollin ◽  
El Moukhtar Aliouat ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Protein Phosphatase ◽  
Protein Phosphatase Type 1 ◽  
Anchoring Protein ◽  
Protein Phosphatase Type

scholarly journals Ectopic Expression of Inhibitors of Protein Phosphatase Type 1 (PP1) Can Be Used to Analyze Roles of PP1 in Drosophila Development

Genetics ◽  
2003 ◽  
Vol 164 (1) ◽  
pp. 235-245
Author(s):  
Daimark Bennett ◽  
Balázs Szöőr ◽  
Sascha Gross ◽  
Natalia Vereshchagina ◽  
Luke Alphey
Keyword(s):  
Protein Phosphatase ◽  
Muscle Development ◽  
Ectopic Expression ◽  
High Specificity ◽  
Type I ◽  
Protein Phosphatase Type 1 ◽  
Mitotic Figures ◽  
Protein Phosphatase Type

Abstract We have identified two proteins that bind with high specificity to type 1 serine/threonine protein phosphatase (PP1) and have exploited their inhibitory properties to develop an efficient and flexible strategy for conditional inactivation of PP1 in vivo. We show that modest overexpression of Drosophila homologs of I-2 and NIPP1 (I-2Dm and NIPP1Dm) reduces the level of PP1 activity and phenotypically resembles known PP1 mutants. These phenotypes, which include lethality, abnormal mitotic figures, and defects in muscle development, are suppressed by coexpression of PP1, indicating that the effect is due specifically to loss of PP1 activity. Reactivation of I-2Dm:PP1c complexes suggests that inhibition of PP1 activity in vivo does not result in a compensating increase in synthesis of active PP1. PP1 mutants enhance the wing overgrowth phenotype caused by ectopic expression of the type II TGFβ superfamily signaling receptor Punt. Using I-2Dm, which has a less severe effect than NIPP1Dm, we show that lowering the level of PP1 activity specifically in cells overexpressing Punt is sufficient for wing overgrowth and that the interaction between PP1 and Punt requires the type I receptor Thick-veins (Tkv) but is not strongly sensitive to the level of the ligand, Decapentaplegic (Dpp), nor to that of the other type I receptors. This is consistent with a role for PP1 in antagonizing Punt by preventing phosphorylation of Tkv. These studies demonstrate that inhibitors of PP1 can be used in a tissue- and developmental-specific manner to examine the developmental roles of PP1.

Differential expression of protein phosphatase type 1 isotypes and nucleolin during cell cycle arrest

2007 ◽  
Vol 25 (4) ◽  
pp. 369-375 ◽  
Author(s):  
Hiroyuki Morimoto ◽  
Akiko Ozaki ◽  
Hirohiko Okamura ◽  
Kaya Yoshida ◽  
Bruna Rabelo Amorim ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Cell Cycle Arrest ◽  
Differential Expression ◽  
Protein Phosphatase ◽  
Cycle Arrest ◽  
Protein Phosphatase Type 1 ◽  
Protein Phosphatase Type

Phosphorylation of the Protein Phosphatase Type 1 Inhibitor Protein CPI-17 by Protein Kinase C

2007 ◽  
pp. 209-224 ◽  
Author(s):  
Michael P. Walsh ◽  
Marija Susnjar ◽  
Jingti Deng ◽  
Cindy Sutherland ◽  
Eniko Kiss ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Phosphatase ◽  
Inhibitor Protein ◽  
Kinase C ◽  
Protein Phosphatase Type 1 ◽  
Protein Phosphatase Type

scholarly journals Ypi1, a Positive Regulator of Nuclear Protein Phosphatase Type 1 Activity in Saccharomyces cerevisiae

2008 ◽  
Vol 19 (3) ◽  
pp. 1032-1045 ◽  
Author(s):  
Jennifer P. Bharucha ◽  
Jennifer R. Larson ◽  
Lu Gao ◽  
Lisa K. Daves ◽  
Kelly Tatchell
Keyword(s):  
Protein Phosphatase ◽  
Nuclear Protein ◽  
Spindle Checkpoint ◽  
Regulatory Subunit ◽  
Aurora B ◽  
Binding Partner ◽  
Protein Phosphatase Type 1 ◽  
Positive Regulators ◽  
Protein Phosphatase Type

The catalytic subunit of protein phosphatase type 1 (PP1) has an essential role in mitosis, acting in opposition to the Ipl1/Aurora B protein kinase to ensure proper kinetochore-microtubule interactions. However, the regulatory subunit(s) that completes the PP1 holoenzyme that functions in this capacity is not known. We show here that the budding yeast Ypi1 protein is a nuclear protein that functions with PP1 (Glc7) in this mitotic role. Depletion of cellular Ypi1 induces mitotic arrest due to activation of the spindle checkpoint. Ypi1 depletion is accompanied by a reduction of nuclear PP1 and by loss of nuclear Sds22, a Glc7 binding partner that is found in a ternary complex with Ypi1 and Glc7. Expression of a Ypi1 variant that binds weakly to PP1 also activates the spindle checkpoint and suppresses the temperature sensitivity of an ipl1-2 mutant. These results, together with genetic interactions among YPI1, GLC7, and SDS22 mutants, indicate that Ypi1 and Sds22 are positive regulators of the nuclear Glc7 activity that is required for mitosis.

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