An evolutionarily conserved motif is required for Plasmodesmata-located protein 5 to regulate cell-to-cell movement
Numerous cell surface receptors and receptor-like proteins (RLPs) undergo activation or deactivation via a transmembrane domain (TMD). A subset of plant RLPs distinctively localizes to the plasma membrane-lined pores called plasmodesmata. Those RLPs include the Arabidopsis thaliana Plasmodesmata-loc...
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description | Numerous cell surface receptors and receptor-like proteins (RLPs) undergo activation or deactivation via a transmembrane domain (TMD). A subset of plant RLPs distinctively localizes to the plasma membrane-lined pores called plasmodesmata. Those RLPs include the
Arabidopsis thaliana
Plasmodesmata-located protein (PDLP) 5, which is well known for its vital function regulating plasmodesmal gating and molecular movement between cells. In this study, we report that the TMD, although not a determining factor for the plasmodesmal targeting, serves essential roles for the PDLP5 function. In addition to its role for membrane anchoring, the TMD mediates PDLP5 self-interaction and carries an evolutionarily conserved motif that is essential for PDLP5 to regulate cell-to-cell movement. Computational modeling-based analyses suggest that PDLP TMDs have high propensities to dimerize. We discuss how a specific mode(s) of TMD dimerization might serve as a common mechanism for PDLP5 and other PDLP members to regulate cell-to-cell movement.
Wang, Robles-Luna et al demonstrate that in Arabidopsis, the transmembrane domain (TMD) of plasmodesmata-located protein 5 (PDLP5) is required for PDPL5 dimerisation and membrane anchoring. This study suggests the importance of the TMD in the role for PDPL5 in regulating pasmodesmal opening. |
doi_str_mv | 10.1038/s42003-020-1007-0 |
format | Article |
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Arabidopsis thaliana
Plasmodesmata-located protein (PDLP) 5, which is well known for its vital function regulating plasmodesmal gating and molecular movement between cells. In this study, we report that the TMD, although not a determining factor for the plasmodesmal targeting, serves essential roles for the PDLP5 function. In addition to its role for membrane anchoring, the TMD mediates PDLP5 self-interaction and carries an evolutionarily conserved motif that is essential for PDLP5 to regulate cell-to-cell movement. Computational modeling-based analyses suggest that PDLP TMDs have high propensities to dimerize. We discuss how a specific mode(s) of TMD dimerization might serve as a common mechanism for PDLP5 and other PDLP members to regulate cell-to-cell movement.
Wang, Robles-Luna et al demonstrate that in Arabidopsis, the transmembrane domain (TMD) of plasmodesmata-located protein 5 (PDLP5) is required for PDPL5 dimerisation and membrane anchoring. This study suggests the importance of the TMD in the role for PDPL5 in regulating pasmodesmal opening.</description><identifier>ISSN: 2399-3642</identifier><identifier>EISSN: 2399-3642</identifier><identifier>DOI: 10.1038/s42003-020-1007-0</identifier><identifier>PMID: 32504045</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>14/19 ; 14/33 ; 14/35 ; 38/77 ; 631/449/1659 ; 631/449/448/2024 ; 96/109 ; Biology ; Biomedical and Life Sciences ; Cell surface ; Channel gating ; Computer applications ; Conserved sequence ; Deactivation ; Dimerization ; Life Sciences ; Life Sciences & Biomedicine ; Life Sciences & Biomedicine - Other Topics ; Multidisciplinary Sciences ; Plasmodesmata ; Proteins ; Science & Technology ; Science & Technology - Other Topics</subject><ispartof>Communications biology, 2020-06, Vol.3 (1), p.291-291, Article 291</ispartof><rights>The Author(s) 2020</rights><rights>The Author(s) 2020. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>12</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wos000540512500001</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c470t-b42f4518234ec7856823aca818ebb3363dacabdf2d2f4ee69ae9a6f36a8065f3</citedby><cites>FETCH-LOGICAL-c470t-b42f4518234ec7856823aca818ebb3363dacabdf2d2f4ee69ae9a6f36a8065f3</cites><orcidid>0000-0003-3409-5557 ; 0000-0002-0803-4817 ; 0000-0003-4604-7974</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7275062/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7275062/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,729,782,786,866,887,2118,27933,27934,28257,41129,42198,51585,53800,53802</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32504045$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Xu</creatorcontrib><creatorcontrib>Robles Luna, Gabriel</creatorcontrib><creatorcontrib>Arighi, Cecilia Noemi</creatorcontrib><creatorcontrib>Lee, Jung-Youn</creatorcontrib><title>An evolutionarily conserved motif is required for Plasmodesmata-located protein 5 to regulate cell-to-cell movement</title><title>Communications biology</title><addtitle>Commun Biol</addtitle><addtitle>COMMUN BIOL</addtitle><addtitle>Commun Biol</addtitle><description>Numerous cell surface receptors and receptor-like proteins (RLPs) undergo activation or deactivation via a transmembrane domain (TMD). A subset of plant RLPs distinctively localizes to the plasma membrane-lined pores called plasmodesmata. Those RLPs include the
Arabidopsis thaliana
Plasmodesmata-located protein (PDLP) 5, which is well known for its vital function regulating plasmodesmal gating and molecular movement between cells. In this study, we report that the TMD, although not a determining factor for the plasmodesmal targeting, serves essential roles for the PDLP5 function. In addition to its role for membrane anchoring, the TMD mediates PDLP5 self-interaction and carries an evolutionarily conserved motif that is essential for PDLP5 to regulate cell-to-cell movement. Computational modeling-based analyses suggest that PDLP TMDs have high propensities to dimerize. We discuss how a specific mode(s) of TMD dimerization might serve as a common mechanism for PDLP5 and other PDLP members to regulate cell-to-cell movement.
Wang, Robles-Luna et al demonstrate that in Arabidopsis, the transmembrane domain (TMD) of plasmodesmata-located protein 5 (PDLP5) is required for PDPL5 dimerisation and membrane anchoring. This study suggests the importance of the TMD in the role for PDPL5 in regulating pasmodesmal opening.</description><subject>14/19</subject><subject>14/33</subject><subject>14/35</subject><subject>38/77</subject><subject>631/449/1659</subject><subject>631/449/448/2024</subject><subject>96/109</subject><subject>Biology</subject><subject>Biomedical and Life Sciences</subject><subject>Cell surface</subject><subject>Channel gating</subject><subject>Computer applications</subject><subject>Conserved sequence</subject><subject>Deactivation</subject><subject>Dimerization</subject><subject>Life Sciences</subject><subject>Life Sciences & Biomedicine</subject><subject>Life Sciences & Biomedicine - Other Topics</subject><subject>Multidisciplinary Sciences</subject><subject>Plasmodesmata</subject><subject>Proteins</subject><subject>Science & Technology</subject><subject>Science & Technology - Other Topics</subject><issn>2399-3642</issn><issn>2399-3642</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>AOWDO</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkk1r3DAQhk1paUKaH9BLMfRSKG7H-rJ9KYSlTQuB9pC7kOXxVsGWNpK8If--YzbZpoVCTxrNPPNqhldF8bqGDzXw9mMSDIBXwKCqAZoKnhWnjHddxZVgz5_EJ8V5SjcAUHddp7h4WZxwJkGAkKdFuvAl7sO0ZBe8iW66L23wCeMeh3IO2Y2lS2XE28VFyowhlj8mk-YwYJpNNtUUrMlU2cWQ0flSljkQv10mSpcWp6nKoVpPktvjjD6_Kl6MZkp4_nCeFddfPl9vvlZX3y-_bS6uKisayFUv2Chk3TIu0DatVBQZa9q6xb7nXPGBbv0wsoE4RNUZ7IwauTItKDnys-LTQXa39DMOll6OZtK76GYT73UwTv9Z8e6n3oa9blgjQTESePcgEMPtginr2aV1E-MxLEkzQUaotq07Qt_-hd6EJXrajijoWiW7ZhWsD5SNIaWI43GYGvRqqj6YqslUvZqqgXrePN3i2PFoIQHtAbjDPozJOvQWjxjZLgXImuj1B2xcNqvTm7D4TK3v_7-VaHagExF-i_H3jv8e_xfZjM-_</recordid><startdate>20200605</startdate><enddate>20200605</enddate><creator>Wang, Xu</creator><creator>Robles Luna, Gabriel</creator><creator>Arighi, Cecilia Noemi</creator><creator>Lee, Jung-Youn</creator><general>Nature Publishing Group UK</general><general>NATURE PORTFOLIO</general><general>Nature Publishing Group</general><scope>C6C</scope><scope>AOWDO</scope><scope>BLEPL</scope><scope>DTL</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7XB</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-3409-5557</orcidid><orcidid>https://orcid.org/0000-0002-0803-4817</orcidid><orcidid>https://orcid.org/0000-0003-4604-7974</orcidid></search><sort><creationdate>20200605</creationdate><title>An evolutionarily conserved motif is required for Plasmodesmata-located protein 5 to regulate cell-to-cell movement</title><author>Wang, Xu ; 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A subset of plant RLPs distinctively localizes to the plasma membrane-lined pores called plasmodesmata. Those RLPs include the
Arabidopsis thaliana
Plasmodesmata-located protein (PDLP) 5, which is well known for its vital function regulating plasmodesmal gating and molecular movement between cells. In this study, we report that the TMD, although not a determining factor for the plasmodesmal targeting, serves essential roles for the PDLP5 function. In addition to its role for membrane anchoring, the TMD mediates PDLP5 self-interaction and carries an evolutionarily conserved motif that is essential for PDLP5 to regulate cell-to-cell movement. Computational modeling-based analyses suggest that PDLP TMDs have high propensities to dimerize. We discuss how a specific mode(s) of TMD dimerization might serve as a common mechanism for PDLP5 and other PDLP members to regulate cell-to-cell movement.
Wang, Robles-Luna et al demonstrate that in Arabidopsis, the transmembrane domain (TMD) of plasmodesmata-located protein 5 (PDLP5) is required for PDPL5 dimerisation and membrane anchoring. This study suggests the importance of the TMD in the role for PDPL5 in regulating pasmodesmal opening.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>32504045</pmid><doi>10.1038/s42003-020-1007-0</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0003-3409-5557</orcidid><orcidid>https://orcid.org/0000-0002-0803-4817</orcidid><orcidid>https://orcid.org/0000-0003-4604-7974</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | 14/19 14/33 14/35 38/77 631/449/1659 631/449/448/2024 96/109 Biology Biomedical and Life Sciences Cell surface Channel gating Computer applications Conserved sequence Deactivation Dimerization Life Sciences Life Sciences & Biomedicine Life Sciences & Biomedicine - Other Topics Multidisciplinary Sciences Plasmodesmata Proteins Science & Technology Science & Technology - Other Topics |
title | An evolutionarily conserved motif is required for Plasmodesmata-located protein 5 to regulate cell-to-cell movement |
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