Inhibition of protein synthesis by the beta-subunit of spectrin.
The 220 kDa beta-subunit of erythroid cell spectrin is a potent inhibitor of protein synthesis in lysates from rabbit reticulocytes. On the basis of weight of protein added to a lysate reaction mixture, it has about half the inhibitory activity of highly purified heme-regulated eIF-2 alpha kinase. Inhibition appears to be at the level of peptide initiation but does not involve a kinase that phosphorylates eIF-2 on its alpha-subunit.
Kudlicki
W
W
Kramer
G
G
Hardesty
B
B
D000818:Animals; D015852:Eukaryotic Initiation Factor-2; D066298:In Vitro Techniques; D010448:Peptide Initiation Factors / Q000494:pharmacology; D014176:Protein Biosynthesis; D011494:Protein Kinases / Q000494:pharmacology; D011506:Proteins / Q000494:pharmacology; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism; D013049:Spectrin / Q000494:pharmacology*; D019892:eIF-2 Kinase
D015852:Eukaryotic Initiation Factor-2; D010448:Peptide Initiation Factors; D011506:Proteins; D013049:Spectrin; D011494:Protein Kinases; D019892:eIF-2 Kinase