molecular specificity code for the three mammalian KDEL receptors
AC-terminal KDEL-like motif prevents secretion of soluble endoplasmic reticulum (ER)-resident proteins. This motif interacts with KDEL receptors localized in the intermediate compartment and Golgi apparatus. Such binding triggers retrieval back to the ER via a coat protein I-dependent pathway. To da...
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| Veröffentlicht in: | The Journal of cell biology 2007-12, Vol.179 (6), p.1193-1204 |
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| container_issue | 6 |
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| container_title | The Journal of cell biology |
| container_volume | 179 |
| creator | Raykhel, Irina Alanen, Heli Salo, Kirsi Jurvansuu, Jaana Nguyen, Van Dat Latva-Ranta, Maria Ruddock, Lloyd |
| description | AC-terminal KDEL-like motif prevents secretion of soluble endoplasmic reticulum (ER)-resident proteins. This motif interacts with KDEL receptors localized in the intermediate compartment and Golgi apparatus. Such binding triggers retrieval back to the ER via a coat protein I-dependent pathway. To date, two human KDEL receptors have been reported. Here, we report the Golgi localization of a third human KDEL receptor. Using a reporter construct system from a screen of 152 variants, we identified 35 KDEL-like variants that result in efficient ER localization but do not match the current Prosite motif for ER localization ([KRHQSA]-[DENQ]-E-L). We cloned 16 human proteins with one of these motifs and all were found in the ER. A subsequent screen by bimolecular fluorescence complementation determined the specificities of the three human KDEL receptors. Each KDEL receptor has a unique pattern of motifs with which it interacts. This suggests a specificity in the retrieval of human proteins that contain different KDEL variants. |
| doi_str_mv | 10.1083/jcb.200705180 |
| format | Article |
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This motif interacts with KDEL receptors localized in the intermediate compartment and Golgi apparatus. Such binding triggers retrieval back to the ER via a coat protein I-dependent pathway. To date, two human KDEL receptors have been reported. Here, we report the Golgi localization of a third human KDEL receptor. Using a reporter construct system from a screen of 152 variants, we identified 35 KDEL-like variants that result in efficient ER localization but do not match the current Prosite motif for ER localization ([KRHQSA]-[DENQ]-E-L). We cloned 16 human proteins with one of these motifs and all were found in the ER. A subsequent screen by bimolecular fluorescence complementation determined the specificities of the three human KDEL receptors. Each KDEL receptor has a unique pattern of motifs with which it interacts. This suggests a specificity in the retrieval of human proteins that contain different KDEL variants.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.200705180</identifier><identifier>PMID: 18086916</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: The Rockefeller University Press</publisher><subject>Amino Acid Motifs ; Animals ; Antibodies ; Biochemistry ; Cells ; Cercopithecus aethiops ; Cloning, Molecular ; COS Cells ; Endoplasmic Reticulum - metabolism ; Fluorescence ; Fluorescent antibody techniques ; Genes, Reporter ; Golgi Apparatus - metabolism ; HeLa Cells ; Humans ; Mammals ; Molecular Sequence Data ; Molecules ; Plasmids ; Protein Sorting Signals ; Proteins ; Receptors ; Receptors, Peptide - analysis ; Receptors, Peptide - chemistry ; Secretory pathway ; Sequence Alignment ; Social interaction ; Transfection</subject><ispartof>The Journal of cell biology, 2007-12, Vol.179 (6), p.1193-1204</ispartof><rights>Copyright 2007 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Dec 17, 2007</rights><rights>Copyright © 2007, The Rockefeller University Press 2007</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c524t-2abdae1997d6fae0cbd6ad3fcf7a57b4c55947b332973870b49650a557f637ab3</citedby><cites>FETCH-LOGICAL-c524t-2abdae1997d6fae0cbd6ad3fcf7a57b4c55947b332973870b49650a557f637ab3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18086916$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Raykhel, Irina</creatorcontrib><creatorcontrib>Alanen, Heli</creatorcontrib><creatorcontrib>Salo, Kirsi</creatorcontrib><creatorcontrib>Jurvansuu, Jaana</creatorcontrib><creatorcontrib>Nguyen, Van Dat</creatorcontrib><creatorcontrib>Latva-Ranta, Maria</creatorcontrib><creatorcontrib>Ruddock, Lloyd</creatorcontrib><title>molecular specificity code for the three mammalian KDEL receptors</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>AC-terminal KDEL-like motif prevents secretion of soluble endoplasmic reticulum (ER)-resident proteins. This motif interacts with KDEL receptors localized in the intermediate compartment and Golgi apparatus. Such binding triggers retrieval back to the ER via a coat protein I-dependent pathway. To date, two human KDEL receptors have been reported. Here, we report the Golgi localization of a third human KDEL receptor. Using a reporter construct system from a screen of 152 variants, we identified 35 KDEL-like variants that result in efficient ER localization but do not match the current Prosite motif for ER localization ([KRHQSA]-[DENQ]-E-L). We cloned 16 human proteins with one of these motifs and all were found in the ER. A subsequent screen by bimolecular fluorescence complementation determined the specificities of the three human KDEL receptors. Each KDEL receptor has a unique pattern of motifs with which it interacts. 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This motif interacts with KDEL receptors localized in the intermediate compartment and Golgi apparatus. Such binding triggers retrieval back to the ER via a coat protein I-dependent pathway. To date, two human KDEL receptors have been reported. Here, we report the Golgi localization of a third human KDEL receptor. Using a reporter construct system from a screen of 152 variants, we identified 35 KDEL-like variants that result in efficient ER localization but do not match the current Prosite motif for ER localization ([KRHQSA]-[DENQ]-E-L). We cloned 16 human proteins with one of these motifs and all were found in the ER. A subsequent screen by bimolecular fluorescence complementation determined the specificities of the three human KDEL receptors. Each KDEL receptor has a unique pattern of motifs with which it interacts. 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| subjects | Amino Acid Motifs Animals Antibodies Biochemistry Cells Cercopithecus aethiops Cloning, Molecular COS Cells Endoplasmic Reticulum - metabolism Fluorescence Fluorescent antibody techniques Genes, Reporter Golgi Apparatus - metabolism HeLa Cells Humans Mammals Molecular Sequence Data Molecules Plasmids Protein Sorting Signals Proteins Receptors Receptors, Peptide - analysis Receptors, Peptide - chemistry Secretory pathway Sequence Alignment Social interaction Transfection |
| title | molecular specificity code for the three mammalian KDEL receptors |
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