Abstract
RACK1 has been shown to interact with several proteins, this suggesting that it may play a central role in cell growth regulation. Some recent articles have described RACK1 as a component of the small ribosomal subunit. To investigate the relationship between RACK1 and ribosome, we analyzed RACK1 mRNA structure and regulation. Translational regulation was studied in HeLa cells subjected to serum or amino acid deprivation and stimulation. The results show that RACK1 mRNA has a 5' terminal oligopyrimidine sequence and that its translation is dependent on the availability of serum and amino acids in exactly the same way as any other vertebrate ribosomal protein mRNA.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acids / pharmacology
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GTP-Binding Proteins / biosynthesis
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GTP-Binding Proteins / genetics*
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Gene Expression Regulation
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HeLa Cells
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Humans
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Neoplasm Proteins / biosynthesis
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Neoplasm Proteins / genetics*
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Protein Biosynthesis / drug effects
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Protein Biosynthesis / genetics*
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RNA, Messenger / chemistry
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RNA, Messenger / metabolism*
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Receptors for Activated C Kinase
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Receptors, Cell Surface / biosynthesis
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Receptors, Cell Surface / genetics*
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Ribosomal Proteins / biosynthesis*
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Ribosomal Proteins / genetics
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Sirolimus / pharmacology
Substances
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Amino Acids
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Neoplasm Proteins
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RACK1 protein, human
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RNA, Messenger
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Receptors for Activated C Kinase
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Receptors, Cell Surface
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Ribosomal Proteins
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GTP-Binding Proteins
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Sirolimus