Regulation of translation initiation by FRAP/mTOR
Regulation of protein synthesis in eukaryotes plays a critical role in development, differentiation, cell cycle progression, cell growth, and apoptosis. Translational control allows for a more rapid response than transcriptional modulation because no mRNA synthesis, processing, or transport is requi...
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description | Regulation of protein synthesis in eukaryotes plays a critical role in development, differentiation, cell cycle progression, cell growth, and apoptosis. Translational control allows for a more rapid response than transcriptional modulation because no mRNA synthesis, processing, or transport is required, and can be used to coordinate gene expression in systems that lack transcriptional regulation, such as reticulocytes or platelets. Translational control plays a particularly important role in early developmental processes, when localized translation is utilized to establish polarity (Wickens et al. 2000), and localized translation in neurons may be critical for learning and memory (e.g., Casadio et al. 1999). Following transcription, processing, and nucleocytoplasmic export, mRNAs are competent for translation. However, two transcripts present in identical quantities may be translated at very different rates. This phenomenon is caused, in part, by the fact that the ribosome does not bind to mRNA directly, but must be recruited to mRNA by the concerted action of a large number of eukaryotic translation initiation factors (eIFs). This recruitment step, also referred to as the initiation phase, is a complex process that culminates in the positioning of a charged ribosome (that is, an 80S ribosome loaded with an initiator tRNA in its P site) at an initiation codon. As discussed further below, the recruitment process is rate-limiting for translation in many cases, and is subject to exquisite regulation. The structure m super(7)GpppN (or the cap, where m is a methyl group and N any nucleotide) is present at the 5' end of all nuclear transcribed mRNAs, and plays an important role in the initiation process. |
doi_str_mv | 10.1101/gad.887201 |
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Translational control allows for a more rapid response than transcriptional modulation because no mRNA synthesis, processing, or transport is required, and can be used to coordinate gene expression in systems that lack transcriptional regulation, such as reticulocytes or platelets. Translational control plays a particularly important role in early developmental processes, when localized translation is utilized to establish polarity (Wickens et al. 2000), and localized translation in neurons may be critical for learning and memory (e.g., Casadio et al. 1999). Following transcription, processing, and nucleocytoplasmic export, mRNAs are competent for translation. However, two transcripts present in identical quantities may be translated at very different rates. This phenomenon is caused, in part, by the fact that the ribosome does not bind to mRNA directly, but must be recruited to mRNA by the concerted action of a large number of eukaryotic translation initiation factors (eIFs). This recruitment step, also referred to as the initiation phase, is a complex process that culminates in the positioning of a charged ribosome (that is, an 80S ribosome loaded with an initiator tRNA in its P site) at an initiation codon. As discussed further below, the recruitment process is rate-limiting for translation in many cases, and is subject to exquisite regulation. The structure m super(7)GpppN (or the cap, where m is a methyl group and N any nucleotide) is present at the 5' end of all nuclear transcribed mRNAs, and plays an important role in the initiation process.</description><identifier>ISSN: 0890-9369</identifier><identifier>EISSN: 1549-5477</identifier><identifier>DOI: 10.1101/gad.887201</identifier><identifier>PMID: 11297505</identifier><language>eng</language><publisher>United States</publisher><subject>Androstadienes - pharmacology ; Animals ; Antineoplastic Agents - pharmacology ; Binding Sites ; Carrier Proteins - metabolism ; Cell Division - genetics ; Cell Division - physiology ; Chromones - pharmacology ; Drosophila melanogaster - genetics ; Drosophila melanogaster - metabolism ; Drosophila Proteins ; Energy Metabolism - genetics ; Enzyme Inhibitors - pharmacology ; Eukaryotic Cells - drug effects ; Eukaryotic Cells - metabolism ; Eukaryotic Initiation Factor-4G ; Eukaryotic Initiation Factors ; FRAP protein ; Fungal Proteins - metabolism ; Gene Expression Regulation - drug effects ; Gene Expression Regulation - physiology ; initiation factors ; Insect Proteins - genetics ; Insect Proteins - metabolism ; Insulin - pharmacology ; Macromolecular Substances ; Mammals - genetics ; Mammals - metabolism ; Mice ; Morpholines - pharmacology ; mTOR protein ; Neoplasm Proteins - antagonists & inhibitors ; Peptide Fragments - metabolism ; Peptide Initiation Factors - metabolism ; Phosphatidylinositol 3-Kinases - antagonists & inhibitors ; Phosphatidylinositol 3-Kinases - physiology ; Phosphoprotein Phosphatases - metabolism ; Phosphoric Monoester Hydrolases - metabolism ; Phosphorylation - drug effects ; Phosphotransferases (Alcohol Group Acceptor) - genetics ; Phosphotransferases (Alcohol Group Acceptor) - metabolism ; Protein Biosynthesis - drug effects ; Protein Biosynthesis - physiology ; Protein Kinase Inhibitors ; Protein Kinases - chemistry ; Protein Kinases - genetics ; Protein Kinases - physiology ; Protein Processing, Post-Translational - drug effects ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases ; Proto-Oncogene Proteins - metabolism ; Proto-Oncogene Proteins c-akt ; PTEN Phosphohydrolase ; RNA, Messenger - genetics ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins ; Signal Transduction - drug effects ; Sirolimus - pharmacology ; Species Specificity ; Structure-Activity Relationship ; Tacrolimus Binding Protein 1A - metabolism ; TOR Serine-Threonine Kinases ; Tumor Suppressor Proteins</subject><ispartof>Genes & development, 2001-04, Vol.15 (7), p.807-826</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c416t-2271e9b3b2498bb039ad386406b42f19a593030e19edb0a799a21f1cf9ee42e13</citedby><cites>FETCH-LOGICAL-c416t-2271e9b3b2498bb039ad386406b42f19a593030e19edb0a799a21f1cf9ee42e13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11297505$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gingras, A C</creatorcontrib><creatorcontrib>Raught, B</creatorcontrib><creatorcontrib>Sonenberg, N</creatorcontrib><title>Regulation of translation initiation by FRAP/mTOR</title><title>Genes & development</title><addtitle>Genes Dev</addtitle><description>Regulation of protein synthesis in eukaryotes plays a critical role in development, differentiation, cell cycle progression, cell growth, and apoptosis. Translational control allows for a more rapid response than transcriptional modulation because no mRNA synthesis, processing, or transport is required, and can be used to coordinate gene expression in systems that lack transcriptional regulation, such as reticulocytes or platelets. Translational control plays a particularly important role in early developmental processes, when localized translation is utilized to establish polarity (Wickens et al. 2000), and localized translation in neurons may be critical for learning and memory (e.g., Casadio et al. 1999). Following transcription, processing, and nucleocytoplasmic export, mRNAs are competent for translation. However, two transcripts present in identical quantities may be translated at very different rates. This phenomenon is caused, in part, by the fact that the ribosome does not bind to mRNA directly, but must be recruited to mRNA by the concerted action of a large number of eukaryotic translation initiation factors (eIFs). This recruitment step, also referred to as the initiation phase, is a complex process that culminates in the positioning of a charged ribosome (that is, an 80S ribosome loaded with an initiator tRNA in its P site) at an initiation codon. As discussed further below, the recruitment process is rate-limiting for translation in many cases, and is subject to exquisite regulation. The structure m super(7)GpppN (or the cap, where m is a methyl group and N any nucleotide) is present at the 5' end of all nuclear transcribed mRNAs, and plays an important role in the initiation process.</description><subject>Androstadienes - pharmacology</subject><subject>Animals</subject><subject>Antineoplastic Agents - pharmacology</subject><subject>Binding Sites</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Division - genetics</subject><subject>Cell Division - physiology</subject><subject>Chromones - pharmacology</subject><subject>Drosophila melanogaster - genetics</subject><subject>Drosophila melanogaster - metabolism</subject><subject>Drosophila Proteins</subject><subject>Energy Metabolism - genetics</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Eukaryotic Cells - drug effects</subject><subject>Eukaryotic Cells - metabolism</subject><subject>Eukaryotic Initiation Factor-4G</subject><subject>Eukaryotic Initiation Factors</subject><subject>FRAP protein</subject><subject>Fungal Proteins - metabolism</subject><subject>Gene Expression Regulation - drug effects</subject><subject>Gene Expression Regulation - physiology</subject><subject>initiation factors</subject><subject>Insect Proteins - genetics</subject><subject>Insect Proteins - metabolism</subject><subject>Insulin - pharmacology</subject><subject>Macromolecular Substances</subject><subject>Mammals - genetics</subject><subject>Mammals - metabolism</subject><subject>Mice</subject><subject>Morpholines - pharmacology</subject><subject>mTOR protein</subject><subject>Neoplasm Proteins - antagonists & inhibitors</subject><subject>Peptide Fragments - metabolism</subject><subject>Peptide Initiation Factors - metabolism</subject><subject>Phosphatidylinositol 3-Kinases - antagonists & inhibitors</subject><subject>Phosphatidylinositol 3-Kinases - physiology</subject><subject>Phosphoprotein Phosphatases - metabolism</subject><subject>Phosphoric Monoester Hydrolases - metabolism</subject><subject>Phosphorylation - drug effects</subject><subject>Phosphotransferases (Alcohol Group Acceptor) - genetics</subject><subject>Phosphotransferases (Alcohol Group Acceptor) - metabolism</subject><subject>Protein Biosynthesis - drug effects</subject><subject>Protein Biosynthesis - physiology</subject><subject>Protein Kinase Inhibitors</subject><subject>Protein Kinases - chemistry</subject><subject>Protein Kinases - genetics</subject><subject>Protein Kinases - physiology</subject><subject>Protein Processing, Post-Translational - drug effects</subject><subject>Protein Structure, Tertiary</subject><subject>Protein-Serine-Threonine Kinases</subject><subject>Proto-Oncogene Proteins - metabolism</subject><subject>Proto-Oncogene Proteins c-akt</subject><subject>PTEN Phosphohydrolase</subject><subject>RNA, Messenger - genetics</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Signal Transduction - drug effects</subject><subject>Sirolimus - pharmacology</subject><subject>Species Specificity</subject><subject>Structure-Activity Relationship</subject><subject>Tacrolimus Binding Protein 1A - metabolism</subject><subject>TOR Serine-Threonine Kinases</subject><subject>Tumor Suppressor Proteins</subject><issn>0890-9369</issn><issn>1549-5477</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1Lw0AURQdRbK1u_AHSlQsh7Xszk0zespRWhUKl1PUwk0xKJB81kyz6740k4NLVuw8Ol8th7BFhgQi4PJl0EceKA16xKYaSglAqdc2mEBMEJCKasDvvvwAggii6ZRNETiqEcMrw4E5dYdq8ruZ1Nm8bU_nxzau8zYdoL_PtYfWxLI_7wz27yUzh3cN4Z-xzuzmu34Ld_vV9vdoFicSoDThX6MgKyyXF1oIgk4o4khBZyTMkE5IAAQ7JpRaMIjIcM0wyck5yh2LGnofec1N_d863usx94orCVK7uvFYKJHEu_wVRxQr6OT34MoBJU3vfuEyfm7w0zUUj6F-TujepB5M9_DS2drZ06R86qhM_TXlsMA</recordid><startdate>20010401</startdate><enddate>20010401</enddate><creator>Gingras, A C</creator><creator>Raught, B</creator><creator>Sonenberg, N</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20010401</creationdate><title>Regulation of translation initiation by FRAP/mTOR</title><author>Gingras, A C ; Raught, B ; Sonenberg, N</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c416t-2271e9b3b2498bb039ad386406b42f19a593030e19edb0a799a21f1cf9ee42e13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Androstadienes - pharmacology</topic><topic>Animals</topic><topic>Antineoplastic Agents - pharmacology</topic><topic>Binding Sites</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Division - genetics</topic><topic>Cell Division - physiology</topic><topic>Chromones - pharmacology</topic><topic>Drosophila melanogaster - genetics</topic><topic>Drosophila melanogaster - metabolism</topic><topic>Drosophila Proteins</topic><topic>Energy Metabolism - genetics</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Eukaryotic Cells - drug effects</topic><topic>Eukaryotic Cells - metabolism</topic><topic>Eukaryotic Initiation Factor-4G</topic><topic>Eukaryotic Initiation Factors</topic><topic>FRAP protein</topic><topic>Fungal Proteins - metabolism</topic><topic>Gene Expression Regulation - drug effects</topic><topic>Gene Expression Regulation - physiology</topic><topic>initiation factors</topic><topic>Insect Proteins - genetics</topic><topic>Insect Proteins - metabolism</topic><topic>Insulin - pharmacology</topic><topic>Macromolecular Substances</topic><topic>Mammals - genetics</topic><topic>Mammals - metabolism</topic><topic>Mice</topic><topic>Morpholines - pharmacology</topic><topic>mTOR protein</topic><topic>Neoplasm Proteins - antagonists & inhibitors</topic><topic>Peptide Fragments - metabolism</topic><topic>Peptide Initiation Factors - metabolism</topic><topic>Phosphatidylinositol 3-Kinases - antagonists & inhibitors</topic><topic>Phosphatidylinositol 3-Kinases - physiology</topic><topic>Phosphoprotein Phosphatases - metabolism</topic><topic>Phosphoric Monoester Hydrolases - metabolism</topic><topic>Phosphorylation - drug effects</topic><topic>Phosphotransferases (Alcohol Group Acceptor) - genetics</topic><topic>Phosphotransferases (Alcohol Group Acceptor) - metabolism</topic><topic>Protein Biosynthesis - drug effects</topic><topic>Protein Biosynthesis - physiology</topic><topic>Protein Kinase Inhibitors</topic><topic>Protein Kinases - chemistry</topic><topic>Protein Kinases - genetics</topic><topic>Protein Kinases - physiology</topic><topic>Protein Processing, Post-Translational - drug effects</topic><topic>Protein Structure, Tertiary</topic><topic>Protein-Serine-Threonine Kinases</topic><topic>Proto-Oncogene Proteins - metabolism</topic><topic>Proto-Oncogene Proteins c-akt</topic><topic>PTEN Phosphohydrolase</topic><topic>RNA, Messenger - genetics</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Signal Transduction - drug effects</topic><topic>Sirolimus - pharmacology</topic><topic>Species Specificity</topic><topic>Structure-Activity Relationship</topic><topic>Tacrolimus Binding Protein 1A - metabolism</topic><topic>TOR Serine-Threonine Kinases</topic><topic>Tumor Suppressor Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gingras, A C</creatorcontrib><creatorcontrib>Raught, B</creatorcontrib><creatorcontrib>Sonenberg, N</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Genes & development</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gingras, A C</au><au>Raught, B</au><au>Sonenberg, N</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of translation initiation by FRAP/mTOR</atitle><jtitle>Genes & development</jtitle><addtitle>Genes Dev</addtitle><date>2001-04-01</date><risdate>2001</risdate><volume>15</volume><issue>7</issue><spage>807</spage><epage>826</epage><pages>807-826</pages><issn>0890-9369</issn><eissn>1549-5477</eissn><abstract>Regulation of protein synthesis in eukaryotes plays a critical role in development, differentiation, cell cycle progression, cell growth, and apoptosis. Translational control allows for a more rapid response than transcriptional modulation because no mRNA synthesis, processing, or transport is required, and can be used to coordinate gene expression in systems that lack transcriptional regulation, such as reticulocytes or platelets. Translational control plays a particularly important role in early developmental processes, when localized translation is utilized to establish polarity (Wickens et al. 2000), and localized translation in neurons may be critical for learning and memory (e.g., Casadio et al. 1999). Following transcription, processing, and nucleocytoplasmic export, mRNAs are competent for translation. However, two transcripts present in identical quantities may be translated at very different rates. This phenomenon is caused, in part, by the fact that the ribosome does not bind to mRNA directly, but must be recruited to mRNA by the concerted action of a large number of eukaryotic translation initiation factors (eIFs). This recruitment step, also referred to as the initiation phase, is a complex process that culminates in the positioning of a charged ribosome (that is, an 80S ribosome loaded with an initiator tRNA in its P site) at an initiation codon. As discussed further below, the recruitment process is rate-limiting for translation in many cases, and is subject to exquisite regulation. The structure m super(7)GpppN (or the cap, where m is a methyl group and N any nucleotide) is present at the 5' end of all nuclear transcribed mRNAs, and plays an important role in the initiation process.</abstract><cop>United States</cop><pmid>11297505</pmid><doi>10.1101/gad.887201</doi><tpages>20</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Androstadienes - pharmacology Animals Antineoplastic Agents - pharmacology Binding Sites Carrier Proteins - metabolism Cell Division - genetics Cell Division - physiology Chromones - pharmacology Drosophila melanogaster - genetics Drosophila melanogaster - metabolism Drosophila Proteins Energy Metabolism - genetics Enzyme Inhibitors - pharmacology Eukaryotic Cells - drug effects Eukaryotic Cells - metabolism Eukaryotic Initiation Factor-4G Eukaryotic Initiation Factors FRAP protein Fungal Proteins - metabolism Gene Expression Regulation - drug effects Gene Expression Regulation - physiology initiation factors Insect Proteins - genetics Insect Proteins - metabolism Insulin - pharmacology Macromolecular Substances Mammals - genetics Mammals - metabolism Mice Morpholines - pharmacology mTOR protein Neoplasm Proteins - antagonists & inhibitors Peptide Fragments - metabolism Peptide Initiation Factors - metabolism Phosphatidylinositol 3-Kinases - antagonists & inhibitors Phosphatidylinositol 3-Kinases - physiology Phosphoprotein Phosphatases - metabolism Phosphoric Monoester Hydrolases - metabolism Phosphorylation - drug effects Phosphotransferases (Alcohol Group Acceptor) - genetics Phosphotransferases (Alcohol Group Acceptor) - metabolism Protein Biosynthesis - drug effects Protein Biosynthesis - physiology Protein Kinase Inhibitors Protein Kinases - chemistry Protein Kinases - genetics Protein Kinases - physiology Protein Processing, Post-Translational - drug effects Protein Structure, Tertiary Protein-Serine-Threonine Kinases Proto-Oncogene Proteins - metabolism Proto-Oncogene Proteins c-akt PTEN Phosphohydrolase RNA, Messenger - genetics Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins Signal Transduction - drug effects Sirolimus - pharmacology Species Specificity Structure-Activity Relationship Tacrolimus Binding Protein 1A - metabolism TOR Serine-Threonine Kinases Tumor Suppressor Proteins |
title | Regulation of translation initiation by FRAP/mTOR |
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