Loading…

Vacuolar sorting receptor for seed storage proteins in Arabidopsis thaliana

The seeds of higher plants accumulate large quantities of storage protein. During seed maturation, storage protein precursors synthesized on rough endoplasmic reticulum are sorted to protein storage vacuoles, where they are converted into the mature forms and accumulated. Previous attempts to determ...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2003-12, Vol.100 (26), p.16095-16100
Main Authors: Shimada, T, Fuji, K, Tamura, K, Kondo, M, Nishimura, M, Hara-Nishimura, I
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c519t-3bce4277f8280f1391bed36db3dff3395510493ac5dd90017d9a0527ff60537f3
cites cdi_FETCH-LOGICAL-c519t-3bce4277f8280f1391bed36db3dff3395510493ac5dd90017d9a0527ff60537f3
container_end_page 16100
container_issue 26
container_start_page 16095
container_title Proceedings of the National Academy of Sciences - PNAS
container_volume 100
creator Shimada, T
Fuji, K
Tamura, K
Kondo, M
Nishimura, M
Hara-Nishimura, I
description The seeds of higher plants accumulate large quantities of storage protein. During seed maturation, storage protein precursors synthesized on rough endoplasmic reticulum are sorted to protein storage vacuoles, where they are converted into the mature forms and accumulated. Previous attempts to determine the sorting machinery for storage proteins have not been successful. Here we show that a type I membrane protein, AtVSR1/AtELP, of Arabidopsis functions as a sorting receptor for storage proteins. The atvsr1 mutant missorts storage proteins by secreting them from cells, resulting in an enlarged and electron-dense extracellular space in the seeds. The atvsr1 seeds have distorted cells and smaller protein storage vacuoles than do WT seeds, and atvsr1 seeds abnormally accumulate the precursors of two major storage proteins, 12S globulin and 2S albumin, together with the mature forms of these proteins. AtVSR1 was found to bind to the C-terminal peptide of 12S globulin in a Ca2+-dependent manner. These findings demonstrate a receptor-mediated transport of seed storage proteins to protein storage vacuoles in higher plants.
doi_str_mv 10.1073/pnas.2530568100
format article
fullrecord <record><control><sourceid>jstor_proqu</sourceid><recordid>TN_cdi_proquest_journals_201346013</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>3149136</jstor_id><sourcerecordid>3149136</sourcerecordid><originalsourceid>FETCH-LOGICAL-c519t-3bce4277f8280f1391bed36db3dff3395510493ac5dd90017d9a0527ff60537f3</originalsourceid><addsrcrecordid>eNqFkcFvFCEUxonR2G317MUo8eZh2gcMMBw8NI1VYxMPWq-EGWDLZjqMwBj972Wym66ePAB5eb_vy-N7CL0gcE5Asot5MvmccgZcdATgEdoQUKQRrYLHaANAZdO1tD1BpznvAEDxDp6iE9IKLhmjG_T5uxmWOJqEc0wlTFuc3ODmEhP29WTnLM61MluH5xSLC1PGYcKXyfTBxjmHjMudGYOZzDP0xJsxu-eH9wzdXr__dvWxufny4dPV5U0zcKJKw_rBtVRK39EOPGGK9M4yYXtmvWdMcU6gVcwM3FoFQKRVBjiV3gvgTHp2ht7tfeelv3d2cFNJZtRzCvcm_dbRBP1vZwp3eht_agZSqK7q3xz0Kf5YXC56F5c01ZE1BcJaUa8KXeyhIcWck_MP_gT0mr1es9fH7Kvi1d9jHflD2BXAB2BVHu1AU6GJqMupyNv_INov41jcr1LZl3t2ty7oAWakVYSJ2n69b3sTtdmmkPXt1_V_QECsAPsDIJSr6Q</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>201346013</pqid></control><display><type>article</type><title>Vacuolar sorting receptor for seed storage proteins in Arabidopsis thaliana</title><source>Open Access: PubMed Central</source><source>JSTOR Archival Journals and Primary Sources Collection</source><creator>Shimada, T ; Fuji, K ; Tamura, K ; Kondo, M ; Nishimura, M ; Hara-Nishimura, I</creator><creatorcontrib>Shimada, T ; Fuji, K ; Tamura, K ; Kondo, M ; Nishimura, M ; Hara-Nishimura, I</creatorcontrib><description>The seeds of higher plants accumulate large quantities of storage protein. During seed maturation, storage protein precursors synthesized on rough endoplasmic reticulum are sorted to protein storage vacuoles, where they are converted into the mature forms and accumulated. Previous attempts to determine the sorting machinery for storage proteins have not been successful. Here we show that a type I membrane protein, AtVSR1/AtELP, of Arabidopsis functions as a sorting receptor for storage proteins. The atvsr1 mutant missorts storage proteins by secreting them from cells, resulting in an enlarged and electron-dense extracellular space in the seeds. The atvsr1 seeds have distorted cells and smaller protein storage vacuoles than do WT seeds, and atvsr1 seeds abnormally accumulate the precursors of two major storage proteins, 12S globulin and 2S albumin, together with the mature forms of these proteins. AtVSR1 was found to bind to the C-terminal peptide of 12S globulin in a Ca2+-dependent manner. These findings demonstrate a receptor-mediated transport of seed storage proteins to protein storage vacuoles in higher plants.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.2530568100</identifier><identifier>PMID: 14657332</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Albumins ; Arabidopsis - genetics ; Arabidopsis - growth &amp; development ; Arabidopsis - physiology ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - physiology ; Arabidopsis thaliana ; Base Sequence ; binding proteins ; Biological Sciences ; Botany ; DNA Primers ; DNA, Bacterial - genetics ; Extracellular space ; Flowers &amp; plants ; Gene Deletion ; Germination ; Globulins ; knockout mutants ; membrane proteins ; Mutagenesis ; Plant cells ; plant proteins ; Protein precursors ; protein transport ; Proteins ; Receptors ; Seeds ; Seeds - genetics ; Seeds - physiology ; Storage proteins ; Vacuoles ; Vacuoles - physiology</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2003-12, Vol.100 (26), p.16095-16100</ispartof><rights>Copyright 1993-2003 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Dec 23, 2003</rights><rights>Copyright © 2003, The National Academy of Sciences 2003</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c519t-3bce4277f8280f1391bed36db3dff3395510493ac5dd90017d9a0527ff60537f3</citedby><cites>FETCH-LOGICAL-c519t-3bce4277f8280f1391bed36db3dff3395510493ac5dd90017d9a0527ff60537f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/100/26.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3149136$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3149136$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,725,778,782,883,27911,27912,53778,53780,58225,58458</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14657332$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shimada, T</creatorcontrib><creatorcontrib>Fuji, K</creatorcontrib><creatorcontrib>Tamura, K</creatorcontrib><creatorcontrib>Kondo, M</creatorcontrib><creatorcontrib>Nishimura, M</creatorcontrib><creatorcontrib>Hara-Nishimura, I</creatorcontrib><title>Vacuolar sorting receptor for seed storage proteins in Arabidopsis thaliana</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The seeds of higher plants accumulate large quantities of storage protein. During seed maturation, storage protein precursors synthesized on rough endoplasmic reticulum are sorted to protein storage vacuoles, where they are converted into the mature forms and accumulated. Previous attempts to determine the sorting machinery for storage proteins have not been successful. Here we show that a type I membrane protein, AtVSR1/AtELP, of Arabidopsis functions as a sorting receptor for storage proteins. The atvsr1 mutant missorts storage proteins by secreting them from cells, resulting in an enlarged and electron-dense extracellular space in the seeds. The atvsr1 seeds have distorted cells and smaller protein storage vacuoles than do WT seeds, and atvsr1 seeds abnormally accumulate the precursors of two major storage proteins, 12S globulin and 2S albumin, together with the mature forms of these proteins. AtVSR1 was found to bind to the C-terminal peptide of 12S globulin in a Ca2+-dependent manner. These findings demonstrate a receptor-mediated transport of seed storage proteins to protein storage vacuoles in higher plants.</description><subject>Albumins</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - growth &amp; development</subject><subject>Arabidopsis - physiology</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - physiology</subject><subject>Arabidopsis thaliana</subject><subject>Base Sequence</subject><subject>binding proteins</subject><subject>Biological Sciences</subject><subject>Botany</subject><subject>DNA Primers</subject><subject>DNA, Bacterial - genetics</subject><subject>Extracellular space</subject><subject>Flowers &amp; plants</subject><subject>Gene Deletion</subject><subject>Germination</subject><subject>Globulins</subject><subject>knockout mutants</subject><subject>membrane proteins</subject><subject>Mutagenesis</subject><subject>Plant cells</subject><subject>plant proteins</subject><subject>Protein precursors</subject><subject>protein transport</subject><subject>Proteins</subject><subject>Receptors</subject><subject>Seeds</subject><subject>Seeds - genetics</subject><subject>Seeds - physiology</subject><subject>Storage proteins</subject><subject>Vacuoles</subject><subject>Vacuoles - physiology</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><recordid>eNqFkcFvFCEUxonR2G317MUo8eZh2gcMMBw8NI1VYxMPWq-EGWDLZjqMwBj972Wym66ePAB5eb_vy-N7CL0gcE5Asot5MvmccgZcdATgEdoQUKQRrYLHaANAZdO1tD1BpznvAEDxDp6iE9IKLhmjG_T5uxmWOJqEc0wlTFuc3ODmEhP29WTnLM61MluH5xSLC1PGYcKXyfTBxjmHjMudGYOZzDP0xJsxu-eH9wzdXr__dvWxufny4dPV5U0zcKJKw_rBtVRK39EOPGGK9M4yYXtmvWdMcU6gVcwM3FoFQKRVBjiV3gvgTHp2ht7tfeelv3d2cFNJZtRzCvcm_dbRBP1vZwp3eht_agZSqK7q3xz0Kf5YXC56F5c01ZE1BcJaUa8KXeyhIcWck_MP_gT0mr1es9fH7Kvi1d9jHflD2BXAB2BVHu1AU6GJqMupyNv_INov41jcr1LZl3t2ty7oAWakVYSJ2n69b3sTtdmmkPXt1_V_QECsAPsDIJSr6Q</recordid><startdate>20031223</startdate><enddate>20031223</enddate><creator>Shimada, T</creator><creator>Fuji, K</creator><creator>Tamura, K</creator><creator>Kondo, M</creator><creator>Nishimura, M</creator><creator>Hara-Nishimura, I</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</scope><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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>20031223</creationdate><title>Vacuolar sorting receptor for seed storage proteins in Arabidopsis thaliana</title><author>Shimada, T ; Fuji, K ; Tamura, K ; Kondo, M ; Nishimura, M ; Hara-Nishimura, I</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c519t-3bce4277f8280f1391bed36db3dff3395510493ac5dd90017d9a0527ff60537f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Albumins</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis - growth &amp; development</topic><topic>Arabidopsis - physiology</topic><topic>Arabidopsis Proteins - genetics</topic><topic>Arabidopsis Proteins - physiology</topic><topic>Arabidopsis thaliana</topic><topic>Base Sequence</topic><topic>binding proteins</topic><topic>Biological Sciences</topic><topic>Botany</topic><topic>DNA Primers</topic><topic>DNA, Bacterial - genetics</topic><topic>Extracellular space</topic><topic>Flowers &amp; plants</topic><topic>Gene Deletion</topic><topic>Germination</topic><topic>Globulins</topic><topic>knockout mutants</topic><topic>membrane proteins</topic><topic>Mutagenesis</topic><topic>Plant cells</topic><topic>plant proteins</topic><topic>Protein precursors</topic><topic>protein transport</topic><topic>Proteins</topic><topic>Receptors</topic><topic>Seeds</topic><topic>Seeds - genetics</topic><topic>Seeds - physiology</topic><topic>Storage proteins</topic><topic>Vacuoles</topic><topic>Vacuoles - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shimada, T</creatorcontrib><creatorcontrib>Fuji, K</creatorcontrib><creatorcontrib>Tamura, K</creatorcontrib><creatorcontrib>Kondo, M</creatorcontrib><creatorcontrib>Nishimura, M</creatorcontrib><creatorcontrib>Hara-Nishimura, I</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shimada, T</au><au>Fuji, K</au><au>Tamura, K</au><au>Kondo, M</au><au>Nishimura, M</au><au>Hara-Nishimura, I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Vacuolar sorting receptor for seed storage proteins in Arabidopsis thaliana</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2003-12-23</date><risdate>2003</risdate><volume>100</volume><issue>26</issue><spage>16095</spage><epage>16100</epage><pages>16095-16100</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The seeds of higher plants accumulate large quantities of storage protein. During seed maturation, storage protein precursors synthesized on rough endoplasmic reticulum are sorted to protein storage vacuoles, where they are converted into the mature forms and accumulated. Previous attempts to determine the sorting machinery for storage proteins have not been successful. Here we show that a type I membrane protein, AtVSR1/AtELP, of Arabidopsis functions as a sorting receptor for storage proteins. The atvsr1 mutant missorts storage proteins by secreting them from cells, resulting in an enlarged and electron-dense extracellular space in the seeds. The atvsr1 seeds have distorted cells and smaller protein storage vacuoles than do WT seeds, and atvsr1 seeds abnormally accumulate the precursors of two major storage proteins, 12S globulin and 2S albumin, together with the mature forms of these proteins. AtVSR1 was found to bind to the C-terminal peptide of 12S globulin in a Ca2+-dependent manner. These findings demonstrate a receptor-mediated transport of seed storage proteins to protein storage vacuoles in higher plants.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>14657332</pmid><doi>10.1073/pnas.2530568100</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0027-8424
ispartof Proceedings of the National Academy of Sciences - PNAS, 2003-12, Vol.100 (26), p.16095-16100
issn 0027-8424
1091-6490
language eng
recordid cdi_proquest_journals_201346013
source Open Access: PubMed Central; JSTOR Archival Journals and Primary Sources Collection
subjects Albumins
Arabidopsis - genetics
Arabidopsis - growth & development
Arabidopsis - physiology
Arabidopsis Proteins - genetics
Arabidopsis Proteins - physiology
Arabidopsis thaliana
Base Sequence
binding proteins
Biological Sciences
Botany
DNA Primers
DNA, Bacterial - genetics
Extracellular space
Flowers & plants
Gene Deletion
Germination
Globulins
knockout mutants
membrane proteins
Mutagenesis
Plant cells
plant proteins
Protein precursors
protein transport
Proteins
Receptors
Seeds
Seeds - genetics
Seeds - physiology
Storage proteins
Vacuoles
Vacuoles - physiology
title Vacuolar sorting receptor for seed storage proteins in Arabidopsis thaliana
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-16T00%3A07%3A12IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Vacuolar%20sorting%20receptor%20for%20seed%20storage%20proteins%20in%20Arabidopsis%20thaliana&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Shimada,%20T&rft.date=2003-12-23&rft.volume=100&rft.issue=26&rft.spage=16095&rft.epage=16100&rft.pages=16095-16100&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.2530568100&rft_dat=%3Cjstor_proqu%3E3149136%3C/jstor_proqu%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c519t-3bce4277f8280f1391bed36db3dff3395510493ac5dd90017d9a0527ff60537f3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=201346013&rft_id=info:pmid/14657332&rft_jstor_id=3149136&rfr_iscdi=true