Two Motifs in the Translational Repressor PHAS-I Required for Efficient Phosphorylation by Mammalian Target of Rapamycin and for Recognition by Raptor
Open Access
- 1 May 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (22) , 19667-19673
- https://doi.org/10.1074/jbc.m301142200
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- The C Terminus of Initiation Factor 4E-Binding Protein 1 Contains Multiple Regulatory Features That Influence Its Function and PhosphorylationMolecular and Cellular Biology, 2003
- The Rapamycin-Binding Domain Governs Substrate Selectivity by the Mammalian Target of RapamycinMolecular and Cellular Biology, 2002
- Raptor, a Binding Partner of Target of Rapamycin (TOR), Mediates TOR ActionCell, 2002
- mTOR Interacts with Raptor to Form a Nutrient-Sensitive Complex that Signals to the Cell Growth MachineryCell, 2002
- Caspase Cleavage of Initiation Factor 4E-Binding Protein 1 Yields a Dominant Inhibitor of Cap-Dependent Translation and Reveals a Novel Regulatory MotifMolecular and Cellular Biology, 2002
- Mammalian Target of Rapamycin-dependent Phosphorylation of PHAS-I in Four (S/T)P Sites Detected by Phospho-specific AntibodiesJournal of Biological Chemistry, 2000
- Multiple Mechanisms Control Phosphorylation of PHAS-I in Five (S/T)P Sites That Govern Translational RepressionMolecular and Cellular Biology, 2000
- Control of PHAS-I by Insulin in 3T3-L1 AdipocytesJournal of Biological Chemistry, 1995
- A mammalian protein targeted by G1-arresting rapamycin–receptor complexNature, 1994
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970