scholarly journals Identification and characterization of protein phosphatase 2C activation by ceramide

2012 ◽  
Vol 53 (8) ◽  
pp. 1513-1521 ◽  
Author(s):  
David M. Perry ◽  
Kazuyuki Kitatani ◽  
Patrick Roddy ◽  
Mohamad El-Osta ◽  
Yusuf A. Hannun
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 2C ◽  
Identification And Characterization

Identification and Characterization of the Human HCG V Gene Product as a Novel Inhibitor of Protein Phosphatase-1†

Biochemistry ◽  
1998 ◽  
Vol 37 (47) ◽  
pp. 16728-16734 ◽  
Author(s):  
Jun Zhang ◽  
Lifang Zhang ◽  
Sumin Zhao ◽  
Ernest Y. C. Lee
Keyword(s):  
Gene Product ◽  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
V Gene ◽  
Identification And Characterization

scholarly journals Calcineurin, a Calcium/Calmodulin-dependent Protein Phosphatase, Is Involved in Movement, Fertility, Egg Laying, and Growth inCaenorhabditis elegans

2002 ◽  
Vol 13 (9) ◽  
pp. 3281-3293 ◽  
Author(s):  
Jaya Bandyopadhyay ◽  
Jiyeon Lee ◽  
Jungsoo Lee ◽  
Jin Il Lee ◽  
Jae-Ran Yu ◽  
...  
Keyword(s):  
Signaling Pathways ◽  
Protein Phosphatase ◽  
Body Wall ◽  
Egg Laying ◽  
Α Subunit ◽  
C Elegans ◽  
Calcium Calmodulin Dependent ◽  
Dependent Protein ◽  
Identification And Characterization

Calcineurin is a Ca2+-calmodulin–dependent serine/threonine protein phosphatase that has been implicated in various signaling pathways. Here we report the identification and characterization of calcineurin genes in Caenorhabditis elegans (cna-1 and cnb-1), which share high homology with Drosophila and mammalian calcineurin genes. C. elegans calcineurin binds calcium and functions as a heterodimeric protein phosphatase establishing its biochemical conservation in the nematode. Calcineurin is expressed in hypodermal seam cells, body-wall muscle, vulva muscle, neuronal cells, and in sperm and the spermatheca. cnb-1 mutants showed pleiotropic defects including lethargic movement and delayed egg-laying. Interestingly, these characteristic defects resembled phenotypes observed in gain-of-function mutants ofunc-43/Ca2+-calmodulin–dependent protein kinase II (CaMKII) and goa-1/Go-protein α-subunit. Double mutants of cnb-1 andunc-43(gf) displayed an apparent synergistic severity of movement and egg-laying defects, suggesting that calcineurin may have an antagonistic role in CaMKII-regulated phosphorylation signaling pathways in C. elegans.

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