{"ddc":["580"],"file_date_updated":"2022-09-08T08:02:54Z","acknowledgement":"We thank the Cryo-EM Center of the University of Science and Technology of China (USTC) and the Center for Biological Imaging (CBI), Institute of Biophysics, Chinese Academy of Science, for the EM facility support; we thank B. Zhu, X. Huang and all the other staff members for their technical support on cryo-EM data collection. We thank J. Ren for his technical support with the transport assays and M. Seeger for providing the sybody libraries. This work was supported by the Strategic Priority Research Program of Chinese Academy of Sciences (XDB 37020204 to D.L. and XDB37020103 to Linfeng Sun), National Natural Science Foundation of China (82151215 and 31870726 to D.L., 31900885 to X.L., and 31870732 to Linfeng Sun), Natural Science Foundation of Anhui Province (2008085MC90 to X.L. and 2008085J15 to Linfeng Sun), the Fundamental Research Funds for the Central Universities (WK9100000031 to Linfeng Sun), and the USTC Research Funds of the Double First-Class Initiative (YD9100002004 to Linfeng Sun). Linfeng Sun is supported by an Outstanding Young Scholar Award from the Qiu Shi Science and Technologies Foundation, and a Young Scholar Award from the Cyrus Tang Foundation.","isi":1,"year":"2022","volume":609,"intvolume":" 609","_id":"12054","language":[{"iso":"eng"}],"article_type":"original","citation":{"mla":"Yang, Z., et al. “Structural Insights into Auxin Recognition and Efflux by Arabidopsis PIN1.” Nature, vol. 609, no. 7927, Springer Nature, 2022, pp. 611–15, doi:10.1038/s41586-022-05143-9.","ieee":"Z. Yang et al., “Structural insights into auxin recognition and efflux by Arabidopsis PIN1,” Nature, vol. 609, no. 7927. Springer Nature, pp. 611–615, 2022.","apa":"Yang, Z., Xia, J., Hong, J., Zhang, C., Wei, H., Ying, W., … Sun, L. (2022). Structural insights into auxin recognition and efflux by Arabidopsis PIN1. Nature. Springer Nature. https://doi.org/10.1038/s41586-022-05143-9","ista":"Yang Z, Xia J, Hong J, Zhang C, Wei H, Ying W, Sun C, Sun L, Mao Y, Gao Y, Tan S, Friml J, Li D, Liu X, Sun L. 2022. Structural insights into auxin recognition and efflux by Arabidopsis PIN1. Nature. 609(7927), 611–615.","chicago":"Yang, Z, J Xia, J Hong, C Zhang, H Wei, W Ying, C Sun, et al. “Structural Insights into Auxin Recognition and Efflux by Arabidopsis PIN1.” Nature. Springer Nature, 2022. https://doi.org/10.1038/s41586-022-05143-9.","ama":"Yang Z, Xia J, Hong J, et al. Structural insights into auxin recognition and efflux by Arabidopsis PIN1. Nature. 2022;609(7927):611-615. doi:10.1038/s41586-022-05143-9","short":"Z. Yang, J. Xia, J. Hong, C. Zhang, H. Wei, W. Ying, C. Sun, L. Sun, Y. Mao, Y. Gao, S. Tan, J. Friml, D. Li, X. Liu, L. Sun, Nature 609 (2022) 611–615."},"publication_identifier":{"issn":["0028-0836"],"eissn":["1476-4687"]},"external_id":{"isi":["000848082900002"],"pmid":["35917925"]},"publication":"Nature","has_accepted_license":"1","author":[{"full_name":"Yang, Z","last_name":"Yang","first_name":"Z"},{"full_name":"Xia, J","last_name":"Xia","first_name":"J"},{"full_name":"Hong, J","last_name":"Hong","first_name":"J"},{"last_name":"Zhang","first_name":"C","full_name":"Zhang, C"},{"first_name":"H","last_name":"Wei","full_name":"Wei, H"},{"last_name":"Ying","first_name":"W","full_name":"Ying, W"},{"full_name":"Sun, C","first_name":"C","last_name":"Sun"},{"full_name":"Sun, L","last_name":"Sun","first_name":"L"},{"last_name":"Mao","first_name":"Y","full_name":"Mao, Y"},{"last_name":"Gao","first_name":"Y","full_name":"Gao, Y"},{"full_name":"Tan, S","last_name":"Tan","first_name":"S"},{"orcid":"0000-0002-8302-7596","full_name":"Friml, Jiří","id":"4159519E-F248-11E8-B48F-1D18A9856A87","last_name":"Friml","first_name":"Jiří"},{"last_name":"Li","first_name":"D","full_name":"Li, D"},{"first_name":"X","last_name":"Liu","full_name":"Liu, X"},{"last_name":"Sun","first_name":"L","full_name":"Sun, L"}],"page":"611-615","doi":"10.1038/s41586-022-05143-9","status":"public","quality_controlled":"1","title":"Structural insights into auxin recognition and efflux by Arabidopsis PIN1","scopus_import":"1","publisher":"Springer Nature","date_created":"2022-09-07T14:19:52Z","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","oa_version":"Published Version","oa":1,"abstract":[{"text":"Polar auxin transport is unique to plants and coordinates their growth and development1,2. The PIN-FORMED (PIN) auxin transporters exhibit highly asymmetrical localizations at the plasma membrane and drive polar auxin transport3,4; however, their structures and transport mechanisms remain largely unknown. Here, we report three inward-facing conformation structures of Arabidopsis thaliana PIN1: the apo state, bound to the natural auxin indole-3-acetic acid (IAA), and in complex with the polar auxin transport inhibitor N-1-naphthylphthalamic acid (NPA). The transmembrane domain of PIN1 shares a conserved NhaA fold5. In the substrate-bound structure, IAA is coordinated by both hydrophobic stacking and hydrogen bonding. NPA competes with IAA for the same site at the intracellular pocket, but with a much higher affinity. These findings inform our understanding of the substrate recognition and transport mechanisms of PINs and set up a framework for future research on directional auxin transport, one of the most crucial processes underlying plant development.","lang":"eng"}],"department":[{"_id":"JiFr"}],"issue":"7927","publication_status":"published","date_published":"2022-08-02T00:00:00Z","date_updated":"2023-08-03T13:41:44Z","pmid":1,"tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"article_processing_charge":"No","month":"08","day":"02","type":"journal_article","file":[{"date_updated":"2022-09-08T08:02:54Z","file_id":"12064","success":1,"date_created":"2022-09-08T08:02:54Z","file_size":32344580,"relation":"main_file","checksum":"3136a585f8e1c7e73b5e1418b3d01898","content_type":"application/pdf","file_name":"2022_Nature_Yang.pdf","access_level":"open_access","creator":"dernst"}]}