Sequence of sites on ATP-citrate lyase and phosphatase inhibitor 2 phosphorylated by multifunctional protein kinase (a glycogen synthase kinase 3 like kinase)

Biochemistry ◽  
1990 ◽  
Vol 29 (33) ◽  
pp. 7617-7624 ◽  
Author(s):  
Seethala Ramakrishna ◽  
Guy D'Angelo ◽  
William B. Benjamin
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Atp Citrate Lyase ◽  
Multifunctional Protein ◽  
Phosphatase Inhibitor ◽  
Citrate Lyase ◽  
Kinase A

scholarly journals Identification of multifunctional ATP-citrate lyase kinase as the α-isoform of glycogen synthase kinase-3

1992 ◽  
Vol 288 (1) ◽  
pp. 309-314 ◽  
Author(s):  
K Hughes ◽  
S Ramakrishna ◽  
W B Benjamin ◽  
J R Woodgett
Keyword(s):  
Drosophila Melanogaster ◽  
Protein Kinase ◽  
Molecular Cloning ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Atp Citrate Lyase ◽  
Multifunctional Protein ◽  
Citrate Lyase ◽  
Biochemical Analyses

Multifunctional ATP-citrate lyase kinase (ACLK) exhibits several properties that are similar to glycogen-synthase kinase-3 (GSK-3). The molecular cloning of two distinct mammalian GSK-3 cDNAs and a Drosophila melanogaster (fruitfly) homologue, zeste-white3sgg, has established the existence of a GSK-3 subfamily. A multifunctional protein kinase first identified as an ACLK has recently been shown to exhibit several similarities to the alpha- and beta-forms of GSK-3. Here we have used immunological and biochemical analyses to directly compare these enzymes. Thus purified preparations of ACLK isolated from brain and liver preferentially cross-react with anti-GSK-3 alpha antisera and phosphorylate previously defined substrates of GSK-3 at identical sites. Conversely, both alpha- and beta-forms of GSK-3 phosphorylated ATP-citrate lyase at the same site(s) targeted by ACLK. These, and other similarities, demonstrate ACLK to be identical with, or highly related to, GSK-3 alpha, the implications of which are discussed.

scholarly journals Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A

2000 ◽  
Vol 97 (22) ◽  
pp. 11960-11965 ◽  
Author(s):  
X. Fang ◽  
S. X. Yu ◽  
Y. Lu ◽  
R. C. Bast ◽  
J. R. Woodgett ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Kinase A

scholarly journals FRAT1, a Substrate-specific Regulator of Glycogen Synthase Kinase-3 Activity, Is a Cellular Substrate of Protein Kinase A

2006 ◽  
Vol 281 (46) ◽  
pp. 35021-35029 ◽  
Author(s):  
Thilo Hagen ◽  
Darren A. E. Cross ◽  
Ainsley A. Culbert ◽  
Andrew West ◽  
Sheelagh Frame ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Kinase A

scholarly journals The In Vivo Activity of Ime1, the Key Transcriptional Activator of Meiosis-Specific Genes in Saccharomyces cerevisiae, Is Inhibited by the Cyclic AMP/Protein Kinase A Signal Pathway through the Glycogen Synthase Kinase 3-β Homolog Rim11

2004 ◽  
Vol 24 (16) ◽  
pp. 6967-6979 ◽  
Author(s):  
Ifat Rubin-Bejerano ◽  
Shira Sagee ◽  
Osnat Friedman ◽  
Lilach Pnueli ◽  
Yona Kassir
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Protein Kinase A ◽  
Glycogen Synthase ◽  
Transcriptional Activator ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Diploid Cells ◽  
Kinase A

ABSTRACT Phosphorylation is the main mode by which signals are transmitted to key regulators of developmental pathways. The glycogen synthase kinase 3 family plays pivotal roles in the development and well-being of all eukaryotic organisms. Similarly, the budding yeast homolog Rim11 is essential for the exit of diploid cells from the cell cycle and for entry into the meiotic developmental pathway. In this report we show that in vivo, in cells grown in a medium promoting vegetative growth with acetate as the sole carbon source (SA medium), Rim11 phosphorylates Ime1, the master transcriptional activator required for entry into the meiotic cycle and for the transcription of early meiosis-specific genes. We demonstrate that in the presence of glucose, the kinase activity of Rim11 is inhibited. This inhibition could be due to phosphorylation on Ser-5, Ser-8, and/or Ser-12 because in the rim11S5AS8AS12A mutant, Ime1 is incorrectly phosphorylated in the presence of glucose and cells undergo sporulation. We further show that this nutrient signal is transmitted to Rim11 and consequently to Ime1 by the cyclic AMP/protein kinase A signal transduction pathway. Ime1 is phosphorylated in SA medium on at least two residues, Tyr-359 and Ser-302 and/or Ser-306. Ser-302 and Ser-306 are part of a consensus site for the mammalian homolog of Rim11, glycogen synthase kinase 3-β. Phosphorylation on Tyr-359 but not Ser-302 or Ser-306 is essential for the transcription of early meiosis-specific genes and sporulation. We show that Tyr-359 is phosphorylated by Rim11.

Sign in / Sign up

Export Citation Format

Share Document