Inhibition of the protein kinase A alters the degradation of the high-affinity phosphate transporter Pho84 in Saccharomyces cerevisiae

2005 ◽  
Vol 48 (4) ◽  
pp. 226-234 ◽  
Author(s):  
Jean-Marie Mouillon ◽  
Bengt L. Persson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Phosphate Transporter ◽  
High Affinity ◽  
Kinase A

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.

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

scholarly journals Protein Kinase A and Sch9 Cooperatively Regulate Induction of Autophagy in Saccharomyces cerevisiae

2007 ◽  
Vol 18 (10) ◽  
pp. 4180-4189 ◽  
Author(s):  
Tomohiro Yorimitsu ◽  
Shadia Zaman ◽  
James R. Broach ◽  
Daniel J. Klionsky
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Transcription Factors ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Signaling Pathways ◽  
Nutrient Sensing ◽  
Regulatory Mechanisms ◽  
Eukaryotic Cells ◽  
Tor Kinase ◽  
Kinase A

Autophagy is a highly conserved, degradative process in eukaryotic cells. The rapamycin-sensitive Tor kinase complex 1 (TORC1) has a major role in regulating induction of autophagy; however, the regulatory mechanisms are not fully understood. Here, we find that the protein kinase A (PKA) and Sch9 signaling pathways regulate autophagy cooperatively in yeast. Autophagy is induced in cells when PKA and Sch9 are simultaneously inactivated. Mutant alleles of these kinases bearing a mutation that confers sensitivity to the ATP-analogue inhibitor C3-1′-naphthyl-methyl PP1 revealed that autophagy was induced independently of effects on Tor kinase. The PKA–Sch9-mediated autophagy depends on the autophagy-related 1 kinase complex, which is also essential for TORC1-regulated autophagy, the transcription factors Msn2/4, and the Rim15 kinase. The present results suggest that autophagy is controlled by the signals from at least three partly separate nutrient-sensing pathways that include PKA, Sch9, and TORC1.

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