The Role of Serine/Threonine Protein Phosphatases in Ceramide Signaling

Author(s):  
Charles E. Chalfant ◽  
Yusuf A. Hannun
Keyword(s):  
Author(s):  
Lekshmy Sathee ◽  
G. K. Krishna ◽  
Sandeep B. Adavi ◽  
Shailendra K. Jha ◽  
Vanita Jain

1995 ◽  
Vol 48 (1) ◽  
pp. 103-110 ◽  
Author(s):  
Johan Svennilson ◽  
Madeleine Durbeej ◽  
Gianni Celsi ◽  
Åsa Laestadius ◽  
Edgar F. da Cruz e Silva ◽  
...  
Keyword(s):  

1987 ◽  
Vol 43 ◽  
pp. 203
Author(s):  
Hideyuki Yamamoto ◽  
Yoshiki Saitoh ◽  
Eishichi Miyamoto

2020 ◽  
Vol 21 (2) ◽  
pp. 395 ◽  
Author(s):  
Ruth Martín ◽  
Vilte Stonyte ◽  
Sandra Lopez-Aviles

Eukaryotic cells make the decision to proliferate, to differentiate or to cease dividing during G1, before passage through the restriction point or Start. Keeping cyclin-dependent kinase (CDK) activity low during this period restricts commitment to a new cell cycle and is essential to provide the adequate timeframe for the sensing of environmental signals. Here, we review the role of protein phosphatases in the modulation of CDK activity and as the counteracting force for CDK-dependent substrate phosphorylation, in budding and fission yeast. Moreover, we discuss recent findings that place protein phosphatases in the interface between nutritional signalling pathways and the cell cycle machinery.


1988 ◽  
Vol 82 (1-2) ◽  
Author(s):  
EvangeliaG. Kranias ◽  
RameshC. Gupta ◽  
Gyorgyi Jakab ◽  
HaeWon Kim ◽  
NancyA.E. Steenaart ◽  
...  

1993 ◽  
Vol 13 (6) ◽  
pp. 349-358 ◽  
Author(s):  
Åke Sjöhom ◽  
Richard E. Honkanen ◽  
Per-Olof Berggren

This study investigates the occurrence and regulation of serine/threonine protein phosphatases (PPases) in insulin-secreting RINm5F insulinoma cells. PPases types 1 and 2A were identified in crude RINm5F cell homogenates by both enzymatic assay and Western blot analysis. We then characterized and compared the inhibitory actions of several compounds isolated from cyanobacteria, marine dinoflagellates and marine sponges, (viz. okadaic acid, microcystin-LR, calyculin-A and nodularin) cation-independent PPase activities in RINm5F cell homogenates. It was found that okadaic acid was the least potent inhibitor (IC50 ≈ 10−9M, IC100 ≈ 10−6M), while the other compounds exhibited IC50 values of ≈ 5·10−10 M and IC100 ≈ 5·10−9 M. The findings indicate that the inhibitory substances employed in this study may be used pharmacologically to investigate the role of serine/threonine PPases in RINm5F cell insulin secretion, a process that is likely to be regulated to a major extent by protein phosphorylation.


1998 ◽  
Vol 273 (45) ◽  
pp. 30039-30045 ◽  
Author(s):  
Sunil Mukhopadhyay ◽  
Cynthia R. L. Webster ◽  
M. Sawkat Anwer

1999 ◽  
Vol 32 (7) ◽  
pp. 835-839 ◽  
Author(s):  
A.M. da-Silva ◽  
P.D.A. Zapella ◽  
L.P.M. Andrioli ◽  
R.B. Campanhã ◽  
L.C. Fiorini ◽  
...  

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