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ATP Citrate Lyase

The Experts below are selected from a list of 177 Experts worldwide ranked by ideXlab platform

James R Woodgett – 1st expert on this subject based on the ideXlab platform

  • identification of multifunctional ATP Citrate Lyase kinase as the α isoform of glycogen synthase kinase 3
    Biochemical Journal, 1992
    Co-Authors: K Hughes, W B Benjamin, S Ramakrishna, James R Woodgett

    Abstract:

    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.

  • Identification of multifunctional ATP–Citrate Lyase kinase as the alpha-isoform of glycogen synthase kinase-3.
    The Biochemical journal, 1992
    Co-Authors: K Hughes, W B Benjamin, S Ramakrishna, James R Woodgett

    Abstract:

    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.

K Hughes – 2nd expert on this subject based on the ideXlab platform

  • identification of multifunctional ATP Citrate Lyase kinase as the α isoform of glycogen synthase kinase 3
    Biochemical Journal, 1992
    Co-Authors: K Hughes, W B Benjamin, S Ramakrishna, James R Woodgett

    Abstract:

    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.

  • Identification of multifunctional ATP–Citrate Lyase kinase as the alpha-isoform of glycogen synthase kinase-3.
    The Biochemical journal, 1992
    Co-Authors: K Hughes, W B Benjamin, S Ramakrishna, James R Woodgett

    Abstract:

    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.

S Ramakrishna – 3rd expert on this subject based on the ideXlab platform

  • Identification of multifunctional ATP–Citrate Lyase kinase as the alpha-isoform of glycogen synthase kinase-3.
    The Biochemical journal, 1992
    Co-Authors: K Hughes, W B Benjamin, S Ramakrishna, James R Woodgett

    Abstract:

    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.

  • identification of multifunctional ATP Citrate Lyase kinase as the α isoform of glycogen synthase kinase 3
    Biochemical Journal, 1992
    Co-Authors: K Hughes, W B Benjamin, S Ramakrishna, James R Woodgett

    Abstract:

    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.

  • An insulin-sensitive cytosolic protein kinase accounts for the regulation of ATP Citrate–Lyase phosphorylation
    Biochemical Journal, 1990
    Co-Authors: Kin-tak Yu, W B Benjamin, S Ramakrishna, Nazer Khalaf, Michael P. Czech

    Abstract:

    Purified rat liver ATP Citrate–Lyase is phosphorylated on serine residues by an insulin-stimulated cytosolic kinase activity partially purified from rat adipocytes [Yu, Khalaf & Czech (1987) J. Biol. Chem. 262, 16677-16685]. The Km for Lyase phosphorylation by this hormone-sensitive kinase activity is approx. 3 microM. Two-dimensional tryptic-peptide mapping of the 32P-labelled Lyase reveals that the kinase-catalysed phosphorylation occurs primarily on a specific peptide. In intact 32P-labelled adipocytes, insulin enhances the serine phosphorylation of ATP Citrate–Lyase by 2-3-fold. Tryptic digestion of the 32P-labelled Lyase immunopurified from insulin-treated adipocytes also yields one major phosphopeptide. 32P-labelled Lyase tryptic peptides derived from labelling experiments in vitro and in vivo exhibit identical electrophoretic and chromatographic migration profiles. Furthermore, radio-sequencing of the phosphopeptide from Lyase 32P-labelled in vitro indicates that serine-3 from the N-terminus is phosphorylated by the insulin-stimulated cytosolic kinase, in agreement with previous studies on the position of the phosphoserine residue in ATP Citrate–Lyase isolated from insulin-treated cells. Taken together, the similarity in site-specific phosphorylation of ATP Citrate–Lyase from insulin-treated adipocytes to that catalysed by the hormone-activated cytosolic kinase in vitro strongly suggests that this kinase mediates insulin action on Lyase phosphorylation in intact cells.