Soluble and membrane-bound protein carrier mediate direct copper transport to the ethylene receptor family
The plant hormone ethylene is a key regulator of plant growth, development and stress adaption. Ethylene perception and response are mediated by a family of integral membrane receptors (ETRs) localized at the ER-Golgi network. The biological function of these receptors relies on a protein-bound copp...
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| Veröffentlicht in: | Scientific reports 2019-07, Vol.9 (1), p.10715-11, Article 10715 |
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| creator | Hoppen, Claudia Müller, Lena Hänsch, Sebastian Uzun, Buket Milić, Dalibor Meyer, Andreas J. Weidtkamp-Peters, Stefanie Groth, Georg |
| description | The plant hormone ethylene is a key regulator of plant growth, development and stress adaption. Ethylene perception and response are mediated by a family of integral membrane receptors (ETRs) localized at the ER-Golgi network. The biological function of these receptors relies on a protein-bound copper cofactor. Nonetheless, molecular processes and structures controlling assembly and integration of the metal into the functional plant hormone receptor are still unknown. Here, we have explored the molecular pathways of copper transfer from the plant cytosol to the ethylene receptor family by analyzing protein–protein interactions of receptors with soluble and membrane-bound plant copper carriers. Our results suggest that receptors primarily acquire their metal cofactor from copper transporter RESPONSIVE-TO-ANTAGONIST-1 (RAN1) which has been loaded with the transition metal beforehand by soluble copper carriers of the ATX1-family. In addition, we found evidence for a direct interaction of ETRs with soluble chaperones ANTIOXIDANT-1 (ATX1) and COPPER TRANSPORT PROTEIN (CCH) raising the possibility of a direct copper exchange between soluble chaperones and receptors. |
| doi_str_mv | 10.1038/s41598-019-47185-6 |
| format | Article |
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Ethylene perception and response are mediated by a family of integral membrane receptors (ETRs) localized at the ER-Golgi network. The biological function of these receptors relies on a protein-bound copper cofactor. Nonetheless, molecular processes and structures controlling assembly and integration of the metal into the functional plant hormone receptor are still unknown. Here, we have explored the molecular pathways of copper transfer from the plant cytosol to the ethylene receptor family by analyzing protein–protein interactions of receptors with soluble and membrane-bound plant copper carriers. Our results suggest that receptors primarily acquire their metal cofactor from copper transporter RESPONSIVE-TO-ANTAGONIST-1 (RAN1) which has been loaded with the transition metal beforehand by soluble copper carriers of the ATX1-family. 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metabolism</topic><topic>Chaperones</topic><topic>Copper</topic><topic>Copper - metabolism</topic><topic>Copper Transport Proteins - metabolism</topic><topic>Cytosol</topic><topic>Cytosol - metabolism</topic><topic>Ethylene</topic><topic>Golgi apparatus</topic><topic>Humanities and Social Sciences</topic><topic>Membrane proteins</topic><topic>Molecular Chaperones - metabolism</topic><topic>multidisciplinary</topic><topic>Nicotiana - metabolism</topic><topic>Plant growth</topic><topic>Plant hormones</topic><topic>Plant Proteins - metabolism</topic><topic>Protein Binding</topic><topic>Protein interaction</topic><topic>Protein transport</topic><topic>Proteins</topic><topic>Receptor mechanisms</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hoppen, Claudia</creatorcontrib><creatorcontrib>Müller, Lena</creatorcontrib><creatorcontrib>Hänsch, Sebastian</creatorcontrib><creatorcontrib>Uzun, Buket</creatorcontrib><creatorcontrib>Milić, Dalibor</creatorcontrib><creatorcontrib>Meyer, Andreas J.</creatorcontrib><creatorcontrib>Weidtkamp-Peters, Stefanie</creatorcontrib><creatorcontrib>Groth, Georg</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hoppen, Claudia</au><au>Müller, Lena</au><au>Hänsch, Sebastian</au><au>Uzun, Buket</au><au>Milić, Dalibor</au><au>Meyer, Andreas J.</au><au>Weidtkamp-Peters, Stefanie</au><au>Groth, Georg</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Soluble and membrane-bound protein carrier mediate direct copper transport to the ethylene receptor family</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2019-07-24</date><risdate>2019</risdate><volume>9</volume><issue>1</issue><spage>10715</spage><epage>11</epage><pages>10715-11</pages><artnum>10715</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>The plant hormone ethylene is a key regulator of plant growth, development and stress adaption. Ethylene perception and response are mediated by a family of integral membrane receptors (ETRs) localized at the ER-Golgi network. The biological function of these receptors relies on a protein-bound copper cofactor. Nonetheless, molecular processes and structures controlling assembly and integration of the metal into the functional plant hormone receptor are still unknown. Here, we have explored the molecular pathways of copper transfer from the plant cytosol to the ethylene receptor family by analyzing protein–protein interactions of receptors with soluble and membrane-bound plant copper carriers. Our results suggest that receptors primarily acquire their metal cofactor from copper transporter RESPONSIVE-TO-ANTAGONIST-1 (RAN1) which has been loaded with the transition metal beforehand by soluble copper carriers of the ATX1-family. In addition, we found evidence for a direct interaction of ETRs with soluble chaperones ANTIOXIDANT-1 (ATX1) and COPPER TRANSPORT PROTEIN (CCH) raising the possibility of a direct copper exchange between soluble chaperones and receptors.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>31341214</pmid><doi>10.1038/s41598-019-47185-6</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0001-5760-6677</orcidid><orcidid>https://orcid.org/0000-0001-8144-4364</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 14/19 14/35 631/449/1741 631/45/56 631/45/612 639/638/45 82/16 82/80 82/83 96/95 Antioxidants Cell Membrane - metabolism Chaperones Copper Copper - metabolism Copper Transport Proteins - metabolism Cytosol Cytosol - metabolism Ethylene Golgi apparatus Humanities and Social Sciences Membrane proteins Molecular Chaperones - metabolism multidisciplinary Nicotiana - metabolism Plant growth Plant hormones Plant Proteins - metabolism Protein Binding Protein interaction Protein transport Proteins Receptor mechanisms Receptors, Cell Surface - metabolism Science Science (multidisciplinary) |
| title | Soluble and membrane-bound protein carrier mediate direct copper transport to the ethylene receptor family |
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