Protein Quality Control along the Route to the Plant Vacuole
To acquire information on the relationships between structural maturation of proteins in the endoplasmic reticulum (ER) and their transport along the secretory pathway, we have analyzed the destiny of an assembly-defective form of the trimeric vacuolar storage glycoprotein phaseolin. In leaves of tr...
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| Veröffentlicht in: | The Plant cell 1997-10, Vol.9 (10), p.1869-1880 |
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| container_end_page | 1880 |
|---|---|
| container_issue | 10 |
| container_start_page | 1869 |
| container_title | The Plant cell |
| container_volume | 9 |
| creator | Pedrazzini, Emanuela Giovinazzo, Giovanna Bielli, Anna de Virgilio, Maddalena Frigerio, Lorenzo Pesca, Michela Faoro, Franco Bollini, Roberto Ceriotti, Aldo Vitale, Alessandro |
| description | To acquire information on the relationships between structural maturation of proteins in the endoplasmic reticulum (ER) and their transport along the secretory pathway, we have analyzed the destiny of an assembly-defective form of the trimeric vacuolar storage glycoprotein phaseolin. In leaves of transgenic tobacco, where assembly-competent phaseolin is correctly targeted to the vacuole, defective phaseolin remains located in the ER or a closely related compartment where it represents a major ligand of the chaperone BiP. Defective phaseolin maintained susceptibility to endoglycosidase H and was slowly degraded by a process that is not inhibited by heat shock or brefeldin A, indicating that degradation does not involve transport along the secretory pathway. These results provide evidence for the presence of a quality control mechanism in the ER of plant cells that avoids intracellular trafficking of severely defective proteins and eventually leads to their degradation. |
| doi_str_mv | 10.1105/tpc.9.10.1869 |
| format | Article |
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In leaves of transgenic tobacco, where assembly-competent phaseolin is correctly targeted to the vacuole, defective phaseolin remains located in the ER or a closely related compartment where it represents a major ligand of the chaperone BiP. Defective phaseolin maintained susceptibility to endoglycosidase H and was slowly degraded by a process that is not inhibited by heat shock or brefeldin A, indicating that degradation does not involve transport along the secretory pathway. These results provide evidence for the presence of a quality control mechanism in the ER of plant cells that avoids intracellular trafficking of severely defective proteins and eventually leads to their degradation.</description><identifier>ISSN: 1040-4651</identifier><identifier>EISSN: 1532-298X</identifier><identifier>DOI: 10.1105/tpc.9.10.1869</identifier><identifier>PMID: 9368420</identifier><language>eng</language><publisher>England: American Society of Plant Physiologists</publisher><subject>Antiserum ; Biological Transport ; Cell Compartmentation ; Endoplasmic Reticulum - metabolism ; Golgi Apparatus - metabolism ; Hydrolysis ; Molecular Chaperones - metabolism ; Nicotiana - metabolism ; Plant cells ; Plant Proteins - chemistry ; Plant Proteins - metabolism ; Plants ; Plants, Genetically Modified ; Plants, Toxic ; Polysaccharides ; Protein Processing, Post-Translational ; Protoplasts ; Quality assurance ; Secretory pathway ; Storage proteins ; Transgenic plants ; Vacuoles ; Vacuoles - metabolism</subject><ispartof>The Plant cell, 1997-10, Vol.9 (10), p.1869-1880</ispartof><rights>Copyright 1997 American Society of Plant Physiologists</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c509t-371fd76f5f7ff9edd390f1f146179465ee4ecec25e3af895fc4caaef1d7b544b3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3870531$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3870531$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9368420$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pedrazzini, Emanuela</creatorcontrib><creatorcontrib>Giovinazzo, Giovanna</creatorcontrib><creatorcontrib>Bielli, Anna</creatorcontrib><creatorcontrib>de Virgilio, Maddalena</creatorcontrib><creatorcontrib>Frigerio, Lorenzo</creatorcontrib><creatorcontrib>Pesca, Michela</creatorcontrib><creatorcontrib>Faoro, Franco</creatorcontrib><creatorcontrib>Bollini, Roberto</creatorcontrib><creatorcontrib>Ceriotti, Aldo</creatorcontrib><creatorcontrib>Vitale, Alessandro</creatorcontrib><title>Protein Quality Control along the Route to the Plant Vacuole</title><title>The Plant cell</title><addtitle>Plant Cell</addtitle><description>To acquire information on the relationships between structural maturation of proteins in the endoplasmic reticulum (ER) and their transport along the secretory pathway, we have analyzed the destiny of an assembly-defective form of the trimeric vacuolar storage glycoprotein phaseolin. In leaves of transgenic tobacco, where assembly-competent phaseolin is correctly targeted to the vacuole, defective phaseolin remains located in the ER or a closely related compartment where it represents a major ligand of the chaperone BiP. Defective phaseolin maintained susceptibility to endoglycosidase H and was slowly degraded by a process that is not inhibited by heat shock or brefeldin A, indicating that degradation does not involve transport along the secretory pathway. These results provide evidence for the presence of a quality control mechanism in the ER of plant cells that avoids intracellular trafficking of severely defective proteins and eventually leads to their degradation.</description><subject>Antiserum</subject><subject>Biological Transport</subject><subject>Cell Compartmentation</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Golgi Apparatus - metabolism</subject><subject>Hydrolysis</subject><subject>Molecular Chaperones - metabolism</subject><subject>Nicotiana - metabolism</subject><subject>Plant cells</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - metabolism</subject><subject>Plants</subject><subject>Plants, Genetically Modified</subject><subject>Plants, Toxic</subject><subject>Polysaccharides</subject><subject>Protein Processing, Post-Translational</subject><subject>Protoplasts</subject><subject>Quality assurance</subject><subject>Secretory pathway</subject><subject>Storage proteins</subject><subject>Transgenic plants</subject><subject>Vacuoles</subject><subject>Vacuoles - metabolism</subject><issn>1040-4651</issn><issn>1532-298X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUE1LAzEUDKLUWj16FPbgdWuySTYb0IMUv6BgFRVvIc2-tFu2m5LNCv33pq2UenpvmJn3hkHokuAhIZjfhJUZyuEGFbk8Qn3CaZZmsvg-jjtmOGU5J6forG0XGGMiiOyhnqR5wTLcR7cT7wJUTfLW6boK62TkmuBdnejaNbMkzCF5d12AJLgtmNS6CcmXNp2r4RydWF23cPE3B-jz8eFj9JyOX59eRvfj1HAsQ0oFsaXILbfCWgllSSW2xBKWEyFjOgAGBkzGgWpbSG4NM1qDJaWYcsamdIDudndX3XQJpYEYUddq5aul9mvldKX-M001VzP3owgXOCuiP935jXdt68HurQSrTYkqlqjkFsUSo_7q8N9e_dda5K93_KINzh8eyygWihYCc0roL-faeyM</recordid><startdate>19971001</startdate><enddate>19971001</enddate><creator>Pedrazzini, Emanuela</creator><creator>Giovinazzo, Giovanna</creator><creator>Bielli, Anna</creator><creator>de Virgilio, Maddalena</creator><creator>Frigerio, Lorenzo</creator><creator>Pesca, Michela</creator><creator>Faoro, Franco</creator><creator>Bollini, Roberto</creator><creator>Ceriotti, Aldo</creator><creator>Vitale, Alessandro</creator><general>American Society of Plant Physiologists</general><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>5PM</scope></search><sort><creationdate>19971001</creationdate><title>Protein Quality Control along the Route to the Plant Vacuole</title><author>Pedrazzini, Emanuela ; Giovinazzo, Giovanna ; Bielli, Anna ; de Virgilio, Maddalena ; Frigerio, Lorenzo ; Pesca, Michela ; Faoro, Franco ; Bollini, Roberto ; Ceriotti, Aldo ; Vitale, Alessandro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c509t-371fd76f5f7ff9edd390f1f146179465ee4ecec25e3af895fc4caaef1d7b544b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Antiserum</topic><topic>Biological Transport</topic><topic>Cell Compartmentation</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Golgi Apparatus - metabolism</topic><topic>Hydrolysis</topic><topic>Molecular Chaperones - metabolism</topic><topic>Nicotiana - metabolism</topic><topic>Plant cells</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - metabolism</topic><topic>Plants</topic><topic>Plants, Genetically Modified</topic><topic>Plants, Toxic</topic><topic>Polysaccharides</topic><topic>Protein Processing, Post-Translational</topic><topic>Protoplasts</topic><topic>Quality assurance</topic><topic>Secretory pathway</topic><topic>Storage proteins</topic><topic>Transgenic plants</topic><topic>Vacuoles</topic><topic>Vacuoles - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pedrazzini, Emanuela</creatorcontrib><creatorcontrib>Giovinazzo, Giovanna</creatorcontrib><creatorcontrib>Bielli, Anna</creatorcontrib><creatorcontrib>de Virgilio, Maddalena</creatorcontrib><creatorcontrib>Frigerio, Lorenzo</creatorcontrib><creatorcontrib>Pesca, Michela</creatorcontrib><creatorcontrib>Faoro, Franco</creatorcontrib><creatorcontrib>Bollini, Roberto</creatorcontrib><creatorcontrib>Ceriotti, Aldo</creatorcontrib><creatorcontrib>Vitale, Alessandro</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Plant cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pedrazzini, Emanuela</au><au>Giovinazzo, Giovanna</au><au>Bielli, Anna</au><au>de Virgilio, Maddalena</au><au>Frigerio, Lorenzo</au><au>Pesca, Michela</au><au>Faoro, Franco</au><au>Bollini, Roberto</au><au>Ceriotti, Aldo</au><au>Vitale, Alessandro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein Quality Control along the Route to the Plant Vacuole</atitle><jtitle>The Plant cell</jtitle><addtitle>Plant Cell</addtitle><date>1997-10-01</date><risdate>1997</risdate><volume>9</volume><issue>10</issue><spage>1869</spage><epage>1880</epage><pages>1869-1880</pages><issn>1040-4651</issn><eissn>1532-298X</eissn><abstract>To acquire information on the relationships between structural maturation of proteins in the endoplasmic reticulum (ER) and their transport along the secretory pathway, we have analyzed the destiny of an assembly-defective form of the trimeric vacuolar storage glycoprotein phaseolin. In leaves of transgenic tobacco, where assembly-competent phaseolin is correctly targeted to the vacuole, defective phaseolin remains located in the ER or a closely related compartment where it represents a major ligand of the chaperone BiP. Defective phaseolin maintained susceptibility to endoglycosidase H and was slowly degraded by a process that is not inhibited by heat shock or brefeldin A, indicating that degradation does not involve transport along the secretory pathway. These results provide evidence for the presence of a quality control mechanism in the ER of plant cells that avoids intracellular trafficking of severely defective proteins and eventually leads to their degradation.</abstract><cop>England</cop><pub>American Society of Plant Physiologists</pub><pmid>9368420</pmid><doi>10.1105/tpc.9.10.1869</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Plant cell, 1997-10, Vol.9 (10), p.1869-1880 |
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| language | eng |
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| source | Jstor Complete Legacy; Oxford University Press Journals All Titles (1996-Current); MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Antiserum Biological Transport Cell Compartmentation Endoplasmic Reticulum - metabolism Golgi Apparatus - metabolism Hydrolysis Molecular Chaperones - metabolism Nicotiana - metabolism Plant cells Plant Proteins - chemistry Plant Proteins - metabolism Plants Plants, Genetically Modified Plants, Toxic Polysaccharides Protein Processing, Post-Translational Protoplasts Quality assurance Secretory pathway Storage proteins Transgenic plants Vacuoles Vacuoles - metabolism |
| title | Protein Quality Control along the Route to the Plant Vacuole |
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