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J Biol Chem, Vol. 273, Issue 47, 30945-30953, November 20, 1998
From the Department of Cellular and Molecular Physiology, The
Pennsylvania State University, College of Medicine,
Hershey, Pennsylvania 17033
The present study was designed to investigate the
mechanism through which leucine and histidine regulate translation
initiation in L6 myoblasts. The results show that both amino acids
stimulate initiation and coordinately regulate the activity of
eukaryotic initiation factor eIF2B. The changes in eIF2B activity could
be explained in part by modulation of the phosphorylation state of the
Implication of eIF2B Rather Than eIF4E in the Regulation of
Global Protein Synthesis by Amino Acids in L6 Myoblasts
-subunit of eIF2. The activity changes might also be a result of
modulation of the phosphorylation state of the eIF2B 
-subunit, because deprivation of either amino acid caused a decrease in eIF2B
kinase activity. Leucine, but not histidine, additionally caused a
redistribution of eIF4E from the inactive eIF4E·4E-BP1 complex to the
active eIF4E·eIF4G complex. The redistribution was a result of
increased phosphorylation of 4E-BP1. The changes in 4E-BP1
phosphorylation and eIF4E redistribution associated with leucine
deprivation were not observed in the presence of insulin. However, the
leucine- and histidine-induced alterations in global protein synthesis
and eIF2B activity were maintained in the presence of the hormone.
Overall, the results suggest that both leucine and histidine regulate
global protein synthesis through modulation of eIF2B activity.
Furthermore, under the conditions employed herein, alterations in eIF4E
availability are not rate-controlling for global protein synthesis but
might be necessary for regulation of translation of specific mRNAs.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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 M. D. Sans, S. R. Kimball, and J. A. Williams Effect of CCK and intracellular calcium to regulate eIF2B and protein synthesis in rat pancreatic acinar cells Am J Physiol Gastrointest Liver Physiol, February 1, 2002; 282(2): G267 - G276. [Abstract] [Full Text] [PDF]
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