Eukaryotic translation initiation (Homo sapiens)

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<?xml version="1.0" encoding="UTF-8"?> <Pathway xmlns="http://pathvisio.org/GPML/2013a" Name="Eukaryotic Translation Initiation" Data-Source="Reactome - http://www.reactome.org" Version="54" Organism="Homo sapiens"> <Comment Source="WikiPathways-description">Initiation of translation in the majority of eukaryotic cellular mRNAs depends on the 5'-cap (m7GpppN) and involves ribosomal scanning of the 5' untranslated region (5'-UTR) for an initiating AUG start codon. Therefore, this mechanism is often called cap-dependent translation initiation. Proximity to the cap, as well as the nucleotides surrounding an AUG codon, influence the efficiency of the start site recognition during the scanning process. However, if the recognition site is poor enough, scanning ribosomal subunits will ignore and skip potential starting AUGs, a phenomenon called leaky scanning. Leaky scanning allows a single mRNA to encode several proteins that differ in their amino-termini. Merrick (2010) provides an overview of this process and hghlights several features of it that remain incompletely understood.&lt;p&gt;Several eukaryotic cell and viral mRNAs initiate translation by an alternative mechanism that involves internal initiation rather than ribosomal scanning. These mRNAs contain complex nucleotide sequences, called internal ribosomal entry sites, where ribosomes bind in a cap-independent manner and start translation at the closest downstream AUG codon.&lt;br&gt; Initiation on several viral and cellular mRNAs is cap-independent and is mediated by binding of the ribosome to internal ribosome entry site (IRES) elements. These elements are often found in characteristically long structured regions on the 5'-UTR of an mRNA that may or may not have regulatory upstream open reading frames (uORFs). Both of these features on the 5'-end of the mRNA hinder ribosomal scanning, and thus promote a cap-independent translation initiation mechanism. IRESs act as specific translational enhancers that allow translation initiation to occur in response to specific stimuli and under the control of different trans-acting factors, as for example when cap-dependent protein synthesis is shut off during viral infection. Such regulatory elements have been identified in the mRNAs of growth factors, protooncogenes, angiogenesis factors, and apoptosis regulators, which are translated under a variety of stress conditions, including hypoxia, serum deprivation, irradiation and apoptosis. Thus, cap-independent translational control might have evolved to regulate cellular responses in acute but transient stress conditions that would otherwise lead to cell death, while the same mechanism is of major importance for viral mRNAs to bypass the shutting-off of host protein synthesis after infection. Encephalomyocarditis virus (EMCV) and hepatitis C virus exemplify two distinct mechanisms of IRES-mediated initiation. In contrast to cap-dependent initiation, the eIF4A and eIF4G subunits of eIF4F bind immediately upstream of the EMCV initiation codon and promote binding of a 43S complex. Accordingly, EMCV initiation does not involve scanning and does not require eIF1, eIF1A, and the eIF4E subunit of eIF4F. Nonetheless, initiation on some EMCV-like IRESs requires additional non-canonical initiation factors, which alter IRES conformation and promote binding of eIF4A/eIF4G. Initiation on the hepatitis C virus IRES is simpler: a 43S complex containing only eIF2 and eIF3 binds directly to the initiation codon as a result of specific interaction of the IRES and the 40S subunit. View original pathway at:[http://www.reactome.org/PathwayBrowser/#DIAGRAM=72613 Reactome].</Comment> <BiopaxRef>f6c</BiopaxRef> <Attribute Key="reactome_id" Value="72613" /> <Graphics BoardWidth="2140.0" BoardHeight="2936.0" /> <DataNode TextLabel="EIF1AX" GraphId="ffa08" Type="Protein"> <BiopaxRef>f8f</BiopaxRef> <BiopaxRef>ad8</BiopaxRef> <Attribute Key="cellular_location" Value="cytosol" /> <Graphics CenterX="302.5" CenterY="472.5" Width="51.0" Height="23.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P47813" /> </DataNode> <DataNode TextLabel="80S ribosome" GraphId="c6d86" Type="Complex"> <Attribute Key="cellular_location" Value="cytosol" /> <Graphics CenterX="232.0" CenterY="379.0" Width="88.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-72500" /> </DataNode> <DataNode TextLabel="RPS10 " GraphId="d25a8" Type="Protein" GroupRef="d06e8"> <Attribute 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ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P50914" /> </DataNode> <DataNode TextLabel="RPL15 " GraphId="bae0c" Type="Protein" GroupRef="d32b1"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-72499" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="1196.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P61313" /> </DataNode> <DataNode TextLabel="RPL17 " GraphId="d2555" Type="Protein" GroupRef="d32b1"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-72499" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="1216.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P18621" /> </DataNode> <DataNode TextLabel="RPL18 " GraphId="d0bca" Type="Protein" GroupRef="d32b1"> <Attribute 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Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P84098" /> </DataNode> <DataNode TextLabel="RPL21 " GraphId="a9453" Type="Protein" GroupRef="d32b1"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-72499" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="1296.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P46778" /> </DataNode> <DataNode TextLabel="RPL22 " GraphId="fcaad" Type="Protein" GroupRef="d32b1"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-72499" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="1316.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P35268" /> </DataNode> <DataNode TextLabel="RPL23 " GraphId="b169c" Type="Protein" GroupRef="d32b1"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-72499" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="1336.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P62829" /> </DataNode> <DataNode TextLabel="RPL23A " GraphId="eb700" Type="Protein" GroupRef="d32b1"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-72499" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="1356.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P62750" /> </DataNode> <DataNode TextLabel="RPL24 " GraphId="a3b8a" Type="Protein" GroupRef="d32b1"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-72499" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" 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<Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1116.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P62249" /> </DataNode> <DataNode TextLabel="RPS17 " GraphId="db51c" Type="Protein" GroupRef="ac276"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-72392" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1136.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P08708" /> </DataNode> <DataNode TextLabel="RPS18 " GraphId="d9c1d" Type="Protein" GroupRef="ac276"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-72392" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1156.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P62269" /> </DataNode> <DataNode TextLabel="RPS19 " GraphId="e0a46" Type="Protein" GroupRef="ac276"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-72392" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1176.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P39019" /> </DataNode> <DataNode TextLabel="RPS15A " GraphId="d3796" Type="Protein" GroupRef="ac276"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-72392" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1196.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P62244" /> </DataNode> <DataNode TextLabel="RPS2 " GraphId="d18e0" Type="Protein" GroupRef="ac276"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" 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<Attribute Key="complex_id" Value="R-HSA-72570" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="520.0" CenterY="1436.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P39019" /> </DataNode> <DataNode TextLabel="RPS15A " GraphId="a10a9" Type="Protein" GroupRef="fdb52"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-72570" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="520.0" CenterY="1456.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P62244" /> </DataNode> <DataNode TextLabel="RPS2 " GraphId="e9f9e" Type="Protein" GroupRef="fdb52"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-72570" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="520.0" CenterY="1476.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" 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<Graphics CenterX="1500.0" CenterY="1356.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P60866" /> </DataNode> <DataNode TextLabel="RPS21 " GraphId="dcb69" Type="Protein" GroupRef="efb31"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-72504" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="1500.0" CenterY="1376.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P63220" /> </DataNode> <DataNode TextLabel="RPS23 " GraphId="f2a41" Type="Protein" GroupRef="efb31"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-72504" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="1500.0" CenterY="1396.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P62266" /> </DataNode> <DataNode 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Here the association of PABP with the poly (A) mRNA and the association of PABP with eIF4F are represented as occuring simultaneously after formation of the initiation complex. However, it is also possible that these interactions occur during the formation of the translation initiation complex. The binding of eIF4F to the cap and binding of PABP to the poly (A) tail, for example, may occur at the same time. In fact, the eIF4G-PABP interaction helps eIF4F to bind tighter to the cap (Borman et al. 2000.) 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initiation complex, eIF5B hydrolyzes its GTP and is released from the now 80S monosome. 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rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Imataka H, Gradi A, Sonenberg N.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="de7"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">1095581</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Purification and characterization of homogeneous initiation factor M2A from rabbit reticulocytes.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Merrick WC, Kemper WM, Anderson WF.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="f8f"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">8106356</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Determination of the amino acid sequence of rabbit, human, and wheat germ protein synthesis factor eIF-4C by cloning and chemical sequencing.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Dever TE, Wei CL, Benkowski LA, Browning K, Merrick WC, Hershey JW.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="ca8"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">592399</bp:ID> <bp:DB 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