Calcium-mediated Association of a Putative Vacuolar Sorting Receptor PV72 with a Propeptide of 2S Albumin
PV72, a type I membrane protein with three epidermal-growth factor (EGF)-like motifs, was found to be localized on the membranes of the precursor-accumulating (PAC) vesicles that accumulated precursors of various seed storage proteins. To clarify the function of PV72 as a sorting receptor, we expres...
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| Veröffentlicht in: | The Journal of biological chemistry 2002-03, Vol.277 (10), p.8708-8715 |
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| container_title | The Journal of biological chemistry |
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| creator | Watanabe, Etsuko Shimada, Tomoo Kuroyanagi, Miwa Nishimura, Mikio Hara-Nishimura, Ikuko |
| description | PV72, a type I membrane protein with three epidermal-growth factor (EGF)-like motifs, was found to be localized on the membranes of the precursor-accumulating (PAC) vesicles that accumulated precursors of various seed storage proteins. To clarify the function of PV72 as a sorting receptor, we expressed four modified PV72s and analyzed their ability to bind the internal propeptide (the 2S-I peptide) of pro2S albumin by affinity chromatography and surface plasmon resonance. The recombinant PV72 specifically bound to the 2S-I peptide with a KD value of 0.2 μm, which was low enough for it to function as a receptor. The EGF-like motifs modulated the Ca2+-dependent conformational change of PV72 to form a functional pocket for the ligand binding. The binding of Ca2+ stabilizes the receptor-ligand complex even at pH 4.0. The association and dissociation of PV72 with the ligand is modulated by the Ca2+ concentration (EC50 value = 40 μm) rather than the environmental pH. Overall results suggest that Ca2+ regulates the vacuolar sorting mechanism in higher plants. |
| doi_str_mv | 10.1074/jbc.M109346200 |
| format | Article |
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To clarify the function of PV72 as a sorting receptor, we expressed four modified PV72s and analyzed their ability to bind the internal propeptide (the 2S-I peptide) of pro2S albumin by affinity chromatography and surface plasmon resonance. The recombinant PV72 specifically bound to the 2S-I peptide with a KD value of 0.2 μm, which was low enough for it to function as a receptor. The EGF-like motifs modulated the Ca2+-dependent conformational change of PV72 to form a functional pocket for the ligand binding. The binding of Ca2+ stabilizes the receptor-ligand complex even at pH 4.0. The association and dissociation of PV72 with the ligand is modulated by the Ca2+ concentration (EC50 value = 40 μm) rather than the environmental pH. Overall results suggest that Ca2+ regulates the vacuolar sorting mechanism in higher plants.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M109346200</identifier><identifier>PMID: 11748226</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>2S Albumins, Plant ; Amino Acid Motifs ; Antigens, Plant ; Calcium - metabolism ; Cucurbita - metabolism ; Electrophoresis, Polyacrylamide Gel ; Epidermal Growth Factor - metabolism ; Glycoproteins - metabolism ; Hydrogen-Ion Concentration ; Immunohistochemistry ; Kinetics ; Ligands ; Peptides - chemistry ; Plant Proteins - chemistry ; Protein Binding ; Protein Conformation ; Protein Precursors - chemistry ; Protein Structure, Tertiary ; Receptors, Cytoplasmic and Nuclear - chemistry ; Receptors, Cytoplasmic and Nuclear - metabolism ; Recombinant Proteins - metabolism ; Spectrometry, Fluorescence ; Surface Plasmon Resonance</subject><ispartof>The Journal of biological chemistry, 2002-03, Vol.277 (10), p.8708-8715</ispartof><rights>2002 © 2002 ASBMB. 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To clarify the function of PV72 as a sorting receptor, we expressed four modified PV72s and analyzed their ability to bind the internal propeptide (the 2S-I peptide) of pro2S albumin by affinity chromatography and surface plasmon resonance. The recombinant PV72 specifically bound to the 2S-I peptide with a KD value of 0.2 μm, which was low enough for it to function as a receptor. The EGF-like motifs modulated the Ca2+-dependent conformational change of PV72 to form a functional pocket for the ligand binding. The binding of Ca2+ stabilizes the receptor-ligand complex even at pH 4.0. The association and dissociation of PV72 with the ligand is modulated by the Ca2+ concentration (EC50 value = 40 μm) rather than the environmental pH. Overall results suggest that Ca2+ regulates the vacuolar sorting mechanism in higher plants.</description><subject>2S Albumins, Plant</subject><subject>Amino Acid Motifs</subject><subject>Antigens, Plant</subject><subject>Calcium - metabolism</subject><subject>Cucurbita - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Epidermal Growth Factor - metabolism</subject><subject>Glycoproteins - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Immunohistochemistry</subject><subject>Kinetics</subject><subject>Ligands</subject><subject>Peptides - chemistry</subject><subject>Plant Proteins - chemistry</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Precursors - chemistry</subject><subject>Protein Structure, Tertiary</subject><subject>Receptors, Cytoplasmic and Nuclear - chemistry</subject><subject>Receptors, Cytoplasmic and Nuclear - metabolism</subject><subject>Recombinant Proteins - metabolism</subject><subject>Spectrometry, Fluorescence</subject><subject>Surface Plasmon Resonance</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFrHCEUxqWkNNtNrz0WIdDbbH06s-pxWZK2kNLQNKE3cfVN1jAzbnQmof99XXYhp1A96JPf-_B9HyEfgS2AyfrLw8YtfgDTol5yxt6QGTAlKtHAnxMyY4xDpXmjTsn7nB9YWbWGd-QUQNaK8-WMhLXtXJj6qkcf7IiernKOrlxDHGhsqaXX01iqJ6R31k2xs4nexDSG4Z7-Qoe7MSZ6fSc5fQ7jdo-nuCuvweO-nd_QVbeZ-jCckbet7TJ-OJ5zcnt58Xv9rbr6-fX7enVVuVrosWpaIVrdyoZrsAJq28iytfLaM481gvMauUDlQfum9pZZtFYt2yVgmc-KOfl80N2l-DhhHk0fssOuswPGKRsJTeG4_C8IqpHFSF3AxQF0KeacsDW7FHqb_hpgZp-CKSmYlxRKw6ej8rQpvr7gR9sLcH4AtuF--xwSmk2Ibou94VLuVZUsMc6JOlBY7HoKmEx2AQdXkkroRuNjeO0H_wAnpKCx</recordid><startdate>20020308</startdate><enddate>20020308</enddate><creator>Watanabe, Etsuko</creator><creator>Shimada, Tomoo</creator><creator>Kuroyanagi, Miwa</creator><creator>Nishimura, Mikio</creator><creator>Hara-Nishimura, Ikuko</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>7QP</scope><scope>7X8</scope></search><sort><creationdate>20020308</creationdate><title>Calcium-mediated Association of a Putative Vacuolar Sorting Receptor PV72 with a Propeptide of 2S Albumin</title><author>Watanabe, Etsuko ; Shimada, Tomoo ; Kuroyanagi, Miwa ; Nishimura, Mikio ; Hara-Nishimura, Ikuko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c439t-5f33f9f75291a314a5757598d9d0de4e1cd9e23e8d19d54da0aeaa86f61e000a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>2S Albumins, Plant</topic><topic>Amino Acid Motifs</topic><topic>Antigens, Plant</topic><topic>Calcium - metabolism</topic><topic>Cucurbita - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Epidermal Growth Factor - metabolism</topic><topic>Glycoproteins - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Immunohistochemistry</topic><topic>Kinetics</topic><topic>Ligands</topic><topic>Peptides - chemistry</topic><topic>Plant Proteins - chemistry</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein Precursors - chemistry</topic><topic>Protein Structure, Tertiary</topic><topic>Receptors, Cytoplasmic and Nuclear - chemistry</topic><topic>Receptors, Cytoplasmic and Nuclear - metabolism</topic><topic>Recombinant Proteins - metabolism</topic><topic>Spectrometry, Fluorescence</topic><topic>Surface Plasmon Resonance</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Watanabe, Etsuko</creatorcontrib><creatorcontrib>Shimada, Tomoo</creatorcontrib><creatorcontrib>Kuroyanagi, Miwa</creatorcontrib><creatorcontrib>Nishimura, Mikio</creatorcontrib><creatorcontrib>Hara-Nishimura, Ikuko</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Watanabe, Etsuko</au><au>Shimada, Tomoo</au><au>Kuroyanagi, Miwa</au><au>Nishimura, Mikio</au><au>Hara-Nishimura, Ikuko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Calcium-mediated Association of a Putative Vacuolar Sorting Receptor PV72 with a Propeptide of 2S Albumin</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2002-03-08</date><risdate>2002</risdate><volume>277</volume><issue>10</issue><spage>8708</spage><epage>8715</epage><pages>8708-8715</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>PV72, a type I membrane protein with three epidermal-growth factor (EGF)-like motifs, was found to be localized on the membranes of the precursor-accumulating (PAC) vesicles that accumulated precursors of various seed storage proteins. To clarify the function of PV72 as a sorting receptor, we expressed four modified PV72s and analyzed their ability to bind the internal propeptide (the 2S-I peptide) of pro2S albumin by affinity chromatography and surface plasmon resonance. The recombinant PV72 specifically bound to the 2S-I peptide with a KD value of 0.2 μm, which was low enough for it to function as a receptor. The EGF-like motifs modulated the Ca2+-dependent conformational change of PV72 to form a functional pocket for the ligand binding. The binding of Ca2+ stabilizes the receptor-ligand complex even at pH 4.0. The association and dissociation of PV72 with the ligand is modulated by the Ca2+ concentration (EC50 value = 40 μm) rather than the environmental pH. 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| subjects | 2S Albumins, Plant Amino Acid Motifs Antigens, Plant Calcium - metabolism Cucurbita - metabolism Electrophoresis, Polyacrylamide Gel Epidermal Growth Factor - metabolism Glycoproteins - metabolism Hydrogen-Ion Concentration Immunohistochemistry Kinetics Ligands Peptides - chemistry Plant Proteins - chemistry Protein Binding Protein Conformation Protein Precursors - chemistry Protein Structure, Tertiary Receptors, Cytoplasmic and Nuclear - chemistry Receptors, Cytoplasmic and Nuclear - metabolism Recombinant Proteins - metabolism Spectrometry, Fluorescence Surface Plasmon Resonance |
| title | Calcium-mediated Association of a Putative Vacuolar Sorting Receptor PV72 with a Propeptide of 2S Albumin |
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