scholarly journals Modulation of Abscisic Acid Signaling in Vivo by an Engineered Receptor-Insensitive Protein Phosphatase Type 2C Allele

2011 ◽  
Vol 156 (1) ◽  
pp. 106-116 ◽  
Author(s):  
Florine Dupeux ◽  
Regina Antoni ◽  
Katja Betz ◽  
Julia Santiago ◽  
Miguel Gonzalez-Guzman ◽  
...  
Genetics ◽  
2003 ◽  
Vol 164 (1) ◽  
pp. 235-245
Author(s):  
Daimark Bennett ◽  
Balázs Szöőr ◽  
Sascha Gross ◽  
Natalia Vereshchagina ◽  
Luke Alphey

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.


2007 ◽  
Vol 50 (6) ◽  
pp. 935-949 ◽  
Author(s):  
Noriyuki Nishimura ◽  
Tomo Yoshida ◽  
Nobutaka Kitahata ◽  
Tadao Asami ◽  
Kazuo Shinozaki ◽  
...  

2013 ◽  
Vol 163 (1) ◽  
pp. 441-455 ◽  
Author(s):  
Gaston A. Pizzio ◽  
Lesia Rodriguez ◽  
Regina Antoni ◽  
Miguel Gonzalez-Guzman ◽  
Cristina Yunta ◽  
...  

Gene ◽  
2014 ◽  
Vol 549 (1) ◽  
pp. 179-185 ◽  
Author(s):  
Ying-Ge Wang ◽  
Hao-Qiang Yu ◽  
Yuan-Yuan Zhang ◽  
Cong-Xian Lai ◽  
Yue-Hui She ◽  
...  

2002 ◽  
Vol 368 (3) ◽  
pp. 789-797 ◽  
Author(s):  
Louise PARKER ◽  
Sascha GROSS ◽  
Monique BEULLENS ◽  
Mathieu BOLLEN ◽  
Daimark BENNETT ◽  
...  

The catalytic subunit of type 1 Ser/Thr protein phosphatases (PP1c) forms complexes with many proteins that target it to particular subcellular locations and regulate its activity towards specific substrates. We report the identification of a Drosophila orthologue of nuclear inhibitor of PP1 (NIPP1Dm) through interaction with PP1c in the yeast two-hybrid system. NIPP1Dm shares many properties with mammalian NIPP1 including inhibition of PP1c in vitro, binding to RNA and PP1c, and localization to nuclear speckles. However, the mechanism controlling interaction of PP1c with NIPP1 is not conserved in Drosophila. NIPP1 can function independently of PP1c as a splicing factor, but the relative importance of this function is unknown. Over-expression of NIPP1Dm in Drosophila is cell-lethal in a range of tissues and developmental stages. The effects of ectopic NIPP1Dm are suppressed by co-expression of PP1c, indicating that the only effect of ectopic NIPP1Dm is to affect PP1c function. Co-expression of NIPP1Dm and PP1c does not have any detectable physiological effect in vivo, suggesting that the NIPP1Dm—PP1c holoenzyme is not normally limiting in Drosophila. These data show that NIPP1Dm and PP1c interact in vivo and suggest that NIPP1's role as a phosphatase regulator is conserved in Drosophila.


1999 ◽  
Vol 11 (10) ◽  
pp. 1897-1909 ◽  
Author(s):  
Françoise Gosti ◽  
Nathalie Beaudoin ◽  
Carine Serizet ◽  
Alex A. R. Webb ◽  
Nicole Vartanian ◽  
...  

Plant Science ◽  
2012 ◽  
Vol 187 ◽  
pp. 83-88 ◽  
Author(s):  
Chae Woo Lim ◽  
Jung-Hyun Kim ◽  
Woonhee Baek ◽  
Beom Seok Kim ◽  
Sung Chul Lee

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