Signal Transduction Dynamics of the Protein Kinase-A/Phosphofructokinase-2 System in Saccharomyces cerevisiae

2001 ◽  
Vol 3 (2) ◽  
pp. 163-172 ◽  
Author(s):  
Sam Vaseghi ◽  
Franz Macherhammer ◽  
Susanne Zibek ◽  
Matthias Reuss
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Signal Transduction ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Kinase A

Regulation of spontaneous and induced resumption of meiosis in mouse oocytes by different intracellular pathways

Reproduction ◽  
2000 ◽  
pp. 377-383 ◽  
Author(s):  
L Leonardsen ◽  
A Wiersma ◽  
M Baltsen ◽  
AG Byskov ◽  
CY Andersen
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Mitogen Activated Protein Kinase ◽  
Meiotic Maturation ◽  
Mouse Oocytes ◽  
Mitogen Activated Protein ◽  
Dependent Signal ◽  
Kinase Pathway ◽  
Kinase A

The mitogen-activated protein kinase-dependent and the cAMP-protein kinase A-dependent signal transduction pathways were studied in cultured mouse oocytes during induced and spontaneous meiotic maturation. The role of the mitogen-activated protein kinase pathway was assessed using PD98059, which specifically inhibits mitogen-activated protein kinase 1 and 2 (that is, MEK1 and MEK2), which activates mitogen-activated protein kinase. The cAMP-dependent protein kinase was studied by treating oocytes with the protein kinase A inhibitor rp-cAMP. Inhibition of the mitogen-activated protein kinase pathway by PD98059 (25 micromol l(-1)) selectively inhibited the stimulatory effect on meiotic maturation by FSH and meiosis-activating sterol (that is, 4,4-dimethyl-5alpha-cholest-8,14, 24-triene-3beta-ol) in the presence of 4 mmol hypoxanthine l(-1), whereas spontaneous maturation in the absence of hypoxanthine was unaffected. This finding indicates that different signal transduction mechanisms are involved in induced and spontaneous maturation. The protein kinase A inhibitor rp-cAMP induced meiotic maturation in the presence of 4 mmol hypoxanthine l(-1), an effect that was additive to the maturation-promoting effect of FSH and meiosis-activating sterol, indicating that induced maturation also uses the cAMP-protein kinase A-dependent signal transduction pathway. In conclusion, induced and spontaneous maturation of mouse oocytes appear to use different signal transduction pathways.

scholarly journals Regulation of maltose utilization in Saccharomyces cerevisiae by genes of the RAS/protein kinase A pathway 1

FEBS Letters ◽  
1997 ◽  
Vol 402 (2-3) ◽  
pp. 251-255 ◽  
Author(s):  
Valeria Wanke ◽  
Monica Vavassori ◽  
Johan M Thevelein ◽  
Paolo Tortora ◽  
Marco Vanoni
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Ras Protein ◽  
Maltose Utilization ◽  
Kinase A

scholarly journals p21-Activated Kinase 5 (Pak5) Localizes to Mitochondria and Inhibits Apoptosis by Phosphorylating BAD

2003 ◽  
Vol 23 (16) ◽  
pp. 5526-5539 ◽  
Author(s):  
Sophie Cotteret ◽  
Zahara M. Jaffer ◽  
Alexander Beeser ◽  
Jonathan Chernoff
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Kinase Activity ◽  
Independent Manner ◽  
Promote Neurite Outgrowth ◽  
P21 Activated Kinase ◽  
Kinase A ◽  
Apoptotic Cascade

ABSTRACT Pak5 is the most recently identified and least understood member of the p21-activated kinase (Pak) family. This kinase is known to promote neurite outgrowth in vitro, but its localization, substrates, and effects on cell survival have not been reported. We show here that Pak5 has unique properties that distinguish it from all other members of the Pak family. First, Pak5, unlike Pak1, cannot complement an STE20 mutation in Saccharomyces cerevisiae. Second, Pak5 binds to the GTPases Cdc42 and Rac, but these GTPases do not regulate Pak5 kinase activity, which is constitutive and stronger than any other Pak. Third, Pak5 prevents apoptosis induced by camptothecin and C2-ceramide by phosphorylating BAD on Ser-112 in a protein kinase A-independent manner and prevents the localization of BAD to mitochondria, thereby inhibiting the apoptotic cascade that leads to apoptosis. Finally, we show that Pak5 itself is constitutively localized to mitochondria, and that this localization is independent of kinase activity or Cdc42 binding. These features make Pak5 unique among the Pak family and suggest that it plays an important role in apoptosis through BAD phosphorylation.

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