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RACK1 mRNA translation is regulated via a rapamycin-sensitive pathway and coordinated with ribosomal protein synthesis.
- Source :
-
FEBS letters [FEBS Lett] 2005 Oct 24; Vol. 579 (25), pp. 5517-20. Date of Electronic Publication: 2005 Sep 27. - Publication Year :
- 2005
-
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.
- Subjects :
- Amino Acids pharmacology
GTP-Binding Proteins biosynthesis
Gene Expression Regulation
HeLa Cells
Humans
Neoplasm Proteins biosynthesis
Protein Biosynthesis drug effects
RNA, Messenger chemistry
Receptors for Activated C Kinase
Receptors, Cell Surface biosynthesis
Ribosomal Proteins genetics
Sirolimus pharmacology
GTP-Binding Proteins genetics
Neoplasm Proteins genetics
Protein Biosynthesis genetics
RNA, Messenger metabolism
Receptors, Cell Surface genetics
Ribosomal Proteins biosynthesis
Subjects
Details
- Language :
- English
- ISSN :
- 0014-5793
- Volume :
- 579
- Issue :
- 25
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 16212959
- Full Text :
- https://doi.org/10.1016/j.febslet.2005.09.016