scholarly journals The membrane localization of Ras2p and the association between Cdc25p and Ras2-GTP are regulated by protein kinase A (PKA) in the yeast Saccharomyces cerevisiae

FEBS Letters ◽  
2011 ◽  
Vol 585 (8) ◽  
pp. 1127-1134 ◽  
Author(s):  
Jian Dong ◽  
Xiaojia Bai
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Membrane Localization ◽  
Yeast Saccharomyces Cerevisiae ◽  
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.

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