scholarly journals Protein Phosphatase 2A, a Negative Regulator of the ERK Signaling Pathway, Is Activated by Tyrosine Phosphorylation of Putative HLA Class II-associated Protein I (PHAPI)/pp32 in Response to the Antiproliferative Lectin, Jacalin

2004 ◽  
Vol 279 (40) ◽  
pp. 41377-41383 ◽  
Author(s):  
Lu-Gang Yu ◽  
Len C. Packman ◽  
Mike Weldon ◽  
Jane Hamlett ◽  
Jonathan M. Rhodes
Keyword(s):  
Signaling Pathway ◽  
Tyrosine Phosphorylation ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Class Ii ◽  
Hla Class Ii ◽  
Negative Regulator ◽  
Erk Signaling ◽  
Phosphatase 2A

Transgenic expression of protein phosphatase 2A regulatory subunit B56γ disrupts distal lung differentiation

2002 ◽  
Vol 282 (6) ◽  
pp. L1266-L1271 ◽  
Author(s):  
Allen D. Everett ◽  
Craig Kamibayashi ◽  
David L. Brautigan
Keyword(s):  
Signaling Pathway ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Wnt Signaling Pathway ◽  
Bronchial Epithelium ◽  
Surfactant Protein ◽  
Regulatory Subunit ◽  
Normal Lung ◽  
Transgenic Expression ◽  
Phosphatase 2A

The distal epithelium of the developing lung exhibits high-level expression of protein phosphatase 2A (PP2A), a vital signaling enzyme. Here we report the discovery that in the lung, the PP2A regulatory subunit B56γ is expressed in a discrete developmental period, with the highest protein levels at embryonic day (e) 17, but no detectable protein in the newborn or adult. By in situ hybridization, B56γ was highly expressed in the distal epithelium of newly forming airways and in mesenchymal cells. In contrast, expression of B56γ was quite low in the bronchial epithelium and vascular smooth muscle. Transgenic expression of B56γ using the lung-specific promoter for surfactant protein C (SP-C) resulted in neonatal death. Examination of lungs from SP-C-B56γ transgenic e18 fetuses revealed proximal airways and normal blood vessels, but the tissue was densely populated with epithelial-type cells and was devoid of normal peripheral lung structure. A component of the Wnt signaling pathway, β-catenin, was developmentally regulated in the normal lung and was absent in lung tissue from B-56γ transgenic fetuses. We propose that B56γ is expressed at a particular stage of lung development to modulate PP2A action on the Wnt/β-catenin signaling pathway during lung airway morphogenesis.

scholarly journals Suppression of Scant Identifies Endos as a Substrate of Greatwall Kinase and a Negative Regulator of Protein Phosphatase 2A in Mitosis

PLoS Genetics ◽  
2011 ◽  
Vol 7 (8) ◽  
pp. e1002225 ◽  
Author(s):  
Hélène Rangone ◽  
Eva Wegel ◽  
Melanie K. Gatt ◽  
Eirene Yeung ◽  
Alexander Flowers ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Negative Regulator ◽  
Phosphatase 2A ◽  
Greatwall Kinase

INH, a negative regulator of MPF, is a form of protein phosphatase 2A

Cell ◽  
1991 ◽  
Vol 64 (2) ◽  
pp. 415-423 ◽  
Author(s):  
Tina H Lee ◽  
Mark J Solomon ◽  
Marc C Mumby ◽  
Marc W Kirschner
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Negative Regulator ◽  
Phosphatase 2A

scholarly journals Protein Phosphatase 2A (PP2A) Regulatory Subunits ParA and PabA Orchestrate Septation and Conidiation and Are Essential for PP2A Activity in Aspergillus nidulans

2014 ◽  
Vol 13 (12) ◽  
pp. 1494-1506 ◽  
Author(s):  
Guo-wei Zhong ◽  
Ping Jiang ◽  
Wei-ran Qiao ◽  
Yuan-wei Zhang ◽  
Wen-fan Wei ◽  
...  
Keyword(s):  
Aspergillus Nidulans ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Hyphal Growth ◽  
Negative Regulator ◽  
Regulatory Subunit ◽  
Content Type ◽  
Regulatory Subunits ◽  
Pp2a Activity ◽  
Phosphatase 2A

ABSTRACTProtein phosphatase 2A (PP2A) is a major intracellular protein phosphatase that regulates multiple aspects of cell growth and metabolism. Different activities of PP2A and subcellular localization are determined by its regulatory subunits. Here we identified and characterized the functions of two protein phosphatase regulatory subunit homologs, ParA and PabA, inAspergillus nidulans. Our results demonstrate that ParA localizes to the septum site and that deletion ofparAcauses hyperseptation, while overexpression ofparAabolishes septum formation; this suggests that ParA may function as a negative regulator of septation. In comparison, PabA displays a clear colocalization pattern with 4′,6-diamidino-2-phenylindole (DAPI)-stained nuclei, and deletion ofpabAinduces a remarkable delayed-septation phenotype. BothparAandpabAare required for hyphal growth, conidiation, and self-fertilization, likely to maintain normal levels of PP2A activity. Most interestingly,parAdeletion is capable of suppressing septation defects inpabAmutants, suggesting that ParA counteracts PabA during the septation process. In contrast, double mutants ofparAandpabAled to synthetic defects in colony growth, indicating that ParA functions synthetically with PabA during hyphal growth. Moreover, unlike the case for PP2A-Par1 and PP2A-Pab1 in yeast (which are negative regulators that inactivate the septation initiation network [SIN]), loss of ParA or PabA fails to suppress defects of temperature-sensitive mutants of the SEPH kinase of the SIN. Thus, our findings support the previously unrealized evidence that the B-family subunits of PP2A have comprehensive functions as partners of heterotrimeric enzyme complexes of PP2A, both spatially and temporally, inA. nidulans.

Protein Phosphatase 2A Is Involved in the Regulation of Protein Kinase A Signaling Pathway during in Vitro Chondrogenesis

2002 ◽  
Vol 275 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Róza Zákány ◽  
Kornélia Szűcs ◽  
Éva Bakó ◽  
Szabolcs Felszeghy ◽  
Gabriella Czifra ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Signaling Pathway ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Phosphatase 2A ◽  
Kinase A
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