Molecular Cloning of Novel Mouse and Human Putative Citrate Lyase β-Subunit

2001 ◽  
Vol 289 (5) ◽  
pp. 1282-1286 ◽  
Author(s):  
Joji Morikawa ◽  
Yuhei Nishimura ◽  
Atsumasa Uchida ◽  
Toshio Tanaka
PLoS ONE ◽  
2017 ◽  
Vol 12 (8) ◽  
pp. e0183545 ◽  
Author(s):  
Thais Sevilhano ◽  
Roberto Feitosa de Carvalho ◽  
Nélio Alessandro de Jesus Oliveira ◽  
João Ezequiel Oliveira ◽  
Vinicius Gonçalves Maltarollo ◽  
...  

Author(s):  
Tod A. Brown ◽  
Burton Horowitz ◽  
Richard P. Miller ◽  
Alicia A. McDonough ◽  
Robert A. Farley

1996 ◽  
Vol 224 (2) ◽  
pp. 318-326 ◽  
Author(s):  
Sunil K. Gupta ◽  
Kenneth Alves ◽  
Linda O'Neil Palladino ◽  
George E. Mark ◽  
Gregory F. Hollis
Keyword(s):  

1992 ◽  
Vol 288 (1) ◽  
pp. 309-314 ◽  
Author(s):  
K Hughes ◽  
S Ramakrishna ◽  
W B Benjamin ◽  
J R Woodgett

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.


2000 ◽  
Vol 30 (6) ◽  
pp. 729-733 ◽  
Author(s):  
Gao-De Li ◽  
Ji-Liang Li ◽  
Mathirut Mugthin ◽  
Stephen A Ward

FEBS Letters ◽  
1990 ◽  
Vol 269 (1) ◽  
pp. 233-238 ◽  
Author(s):  
Kalyan K. Bhattacharyya ◽  
Ellen E. Bergstrom ◽  
Lowell E. Hokin

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