The unfolded protein response pathway in Saccharomyces cerevisiae. Oligomerization and trans-phosphorylation of Ire1p (Ern1p) are required for kinase activation
In eukaryotic cells, accumulation of unfolded proteins in the endoplasmic reticulum (ER) results in a transcription induction of a number of ER chaperone proteins. In Saccharomyces cerevisiae, the putative transmembrane receptor kinase, Ire1P (Ern1p), has been implicated as the sensor of unfolded pr...
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| Veröffentlicht in: | The Journal of biological chemistry 1996-07, Vol.271 (30), p.18181-18187 |
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| container_end_page | 18187 |
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| container_issue | 30 |
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| container_title | The Journal of biological chemistry |
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| creator | Welihinda, A.A. (University of Michigan Medical Center, Ann Arbor.) Kaufman, R.J |
| description | In eukaryotic cells, accumulation of unfolded proteins in the endoplasmic reticulum (ER) results in a transcription induction of a number of ER chaperone proteins. In Saccharomyces cerevisiae, the putative transmembrane receptor kinase, Ire1P (Ern1p), has been implicated as the sensor of unfolded proteins in the ER that initiates transmittance of the unfolded protein signal from the ER to the nucleus. We have shown that the cytoplasmic domain of Ire1p receptor indeed has intrinsic Ser/Thr kinase activity and contains Ser/Thr phosphorylation sites as well. The cytoplasmic domain is also shown to form oligomers in vivo and in vitro. The ability to form oligomers primarily resides within the last 130 amino acids of the cytoplasmic domain, a region that is dispensable for in vitro kinase activity of the receptor. Oligomerization of the cytoplasmic domains is required for receptor trans-phosphorylation and subsequent activation of the kinase function. The activated kinase may transmit the unfolded protein signal from the ER to the nucleus to activate the transcription of the chaperone genes in the nucleus |
| doi_str_mv | 10.1074/jbc.271.30.18181 |
| format | Article |
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The activated kinase may transmit the unfolded protein signal from the ER to the nucleus to activate the transcription of the chaperone genes in the nucleus</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>CHIMIORECEPTEUR</subject><subject>COMPOSICION QUIMICA</subject><subject>COMPOSITION CHIMIQUE</subject><subject>Cytoplasm - metabolism</subject><subject>Enzyme Activation</subject><subject>FOSFORILACION</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Membrane Glycoproteins - genetics</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Peptide Fragments - genetics</subject><subject>Peptide Fragments - metabolism</subject><subject>PHOSPHORYLATION</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>QUIMIORECEPTORES</subject><subject>Receptors, Growth Factor - genetics</subject><subject>Receptors, Growth Factor - metabolism</subject><subject>Receptors, Transforming Growth Factor beta</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>RETICULO ENDOPLASMATICO</subject><subject>RETICULUM ENDOPLASMIQUE</subject><subject>SACCHAROMYCES CEREVISIAE</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Structure-Activity Relationship</subject><subject>TRANSCRIPCION</subject><subject>TRANSCRIPTION</subject><subject>TRANSFERASAS</subject><subject>TRANSFERASE</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNotUMFq3DAQFaUl3aS9l0JBp9IevJUsW5aOIaRpIJBDEujNjORRVqktOZKdsv2afmpFd2cYhpn3Zh48Qj5wtuWsa749GbutO74VZVYlX5ENZ0pUouU_X5MNYzWvdN2qt-Q05ydWotH8hJwoKUXTqg35e79DugYXxwEHOqe4oA80YZ5jyEhnWHa_YU_L7g6s3UGK095iphYTvvjsAbf0dvSPccLk_8DiY6AQBrokCLmadzGXSvvxgERHrxPymX65TIHPXykkLGLPq09F3cVEf_kARRfs4l_-37wjbxyMGd8f-xl5-H55f_Gjurm9ur44v6lcXbdLZUDVEhqrpWgbAKYsNlaBUVJJp1s5KGFarVkHauisk67WjamlEQwNdoaJM_L58Ld48LxiXvrJZ4vjCAHjmnveSq47Jgrx05G4mgmHfk5-grTvj5YW_OMBdxB7eEw-9w93umsU51L8A7e1hRQ</recordid><startdate>19960726</startdate><enddate>19960726</enddate><creator>Welihinda, A.A. 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(University of Michigan Medical Center, Ann Arbor.) ; Kaufman, R.J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f225t-ba826a4c96354aa08ce4c8ab8686f956d83b59907a8d7cf6f294b26b30ebe7b03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>CHIMIORECEPTEUR</topic><topic>COMPOSICION QUIMICA</topic><topic>COMPOSITION CHIMIQUE</topic><topic>Cytoplasm - metabolism</topic><topic>Enzyme Activation</topic><topic>FOSFORILACION</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Membrane Glycoproteins - genetics</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Peptide Fragments - genetics</topic><topic>Peptide Fragments - metabolism</topic><topic>PHOSPHORYLATION</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein Folding</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>QUIMIORECEPTORES</topic><topic>Receptors, Growth Factor - genetics</topic><topic>Receptors, Growth Factor - metabolism</topic><topic>Receptors, Transforming Growth Factor beta</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>RETICULO ENDOPLASMATICO</topic><topic>RETICULUM ENDOPLASMIQUE</topic><topic>SACCHAROMYCES CEREVISIAE</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Structure-Activity Relationship</topic><topic>TRANSCRIPCION</topic><topic>TRANSCRIPTION</topic><topic>TRANSFERASAS</topic><topic>TRANSFERASE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Welihinda, A.A. (University of Michigan Medical Center, Ann Arbor.)</creatorcontrib><creatorcontrib>Kaufman, R.J</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Welihinda, A.A. (University of Michigan Medical Center, Ann Arbor.)</au><au>Kaufman, R.J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The unfolded protein response pathway in Saccharomyces cerevisiae. Oligomerization and trans-phosphorylation of Ire1p (Ern1p) are required for kinase activation</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1996-07-26</date><risdate>1996</risdate><volume>271</volume><issue>30</issue><spage>18181</spage><epage>18187</epage><pages>18181-18187</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>In eukaryotic cells, accumulation of unfolded proteins in the endoplasmic reticulum (ER) results in a transcription induction of a number of ER chaperone proteins. In Saccharomyces cerevisiae, the putative transmembrane receptor kinase, Ire1P (Ern1p), has been implicated as the sensor of unfolded proteins in the ER that initiates transmittance of the unfolded protein signal from the ER to the nucleus. We have shown that the cytoplasmic domain of Ire1p receptor indeed has intrinsic Ser/Thr kinase activity and contains Ser/Thr phosphorylation sites as well. The cytoplasmic domain is also shown to form oligomers in vivo and in vitro. The ability to form oligomers primarily resides within the last 130 amino acids of the cytoplasmic domain, a region that is dispensable for in vitro kinase activity of the receptor. Oligomerization of the cytoplasmic domains is required for receptor trans-phosphorylation and subsequent activation of the kinase function. The activated kinase may transmit the unfolded protein signal from the ER to the nucleus to activate the transcription of the chaperone genes in the nucleus</abstract><cop>United States</cop><pmid>8663458</pmid><doi>10.1074/jbc.271.30.18181</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | The Journal of biological chemistry, 1996-07, Vol.271 (30), p.18181-18187 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE CHIMIORECEPTEUR COMPOSICION QUIMICA COMPOSITION CHIMIQUE Cytoplasm - metabolism Enzyme Activation FOSFORILACION Fungal Proteins - genetics Fungal Proteins - metabolism Membrane Glycoproteins - genetics Membrane Glycoproteins - metabolism Peptide Fragments - genetics Peptide Fragments - metabolism PHOSPHORYLATION Protein Binding Protein Conformation Protein Folding Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism PROTEINAS PROTEINE QUIMIORECEPTORES Receptors, Growth Factor - genetics Receptors, Growth Factor - metabolism Receptors, Transforming Growth Factor beta Recombinant Fusion Proteins - metabolism RETICULO ENDOPLASMATICO RETICULUM ENDOPLASMIQUE SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins Structure-Activity Relationship TRANSCRIPCION TRANSCRIPTION TRANSFERASAS TRANSFERASE |
| title | The unfolded protein response pathway in Saccharomyces cerevisiae. Oligomerization and trans-phosphorylation of Ire1p (Ern1p) are required for kinase activation |
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