Phosphorylation and the control of protein synthesis.
This paper reviews the evidence that protein synthesis in rabbit reticulocytes is regulated by the reversible phosphorylation of the initiation factor eIF-2 by protein kinases under the control of the cytoplasmic haemin concentration on the one hand, and double-stranded RNA on the other. A molecular mechanism is proposed to account for the observation that inhibition of protein synthesis occurs when considerably less than half the eIF-2 present has been phosphorylated. The question of whether phosphorylation regulates protein synthesis in other types of cell is discussed.
D000818:Animals; D015852:Eukaryotic Initiation Factor-2; D006150:Guanine Nucleotides / Q000378:metabolism; D006427:Hemin / Q000378:metabolism; D010448:Peptide Initiation Factors / Q000378:metabolism; D010766:Phosphorylation; D014176:Protein Biosynthesis; D011494:Protein Kinases / Q000378:metabolism; D011506:Proteins / Q000378:metabolism; D012330:RNA, Double-Stranded / Q000378:metabolism; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism; D012269:Ribosomal Proteins / Q000378:metabolism
D015852:Eukaryotic Initiation Factor-2; D006150:Guanine Nucleotides; D010448:Peptide Initiation Factors; D011506:Proteins; D012330:RNA, Double-Stranded; D012269:Ribosomal Proteins; D006427:Hemin; D011494:Protein Kinases