[{"doi":"10.1016/j.celrep.2025.116024","author":[{"first_name":"Bin","last_name":"Guan","full_name":"Guan, Bin","id":"56aad729-cca2-11ed-a45a-9b4138991a48"},{"first_name":"Ke Xuan","last_name":"Xie","full_name":"Xie, Ke Xuan"},{"last_name":"Du","full_name":"Du, Xin Qiao","first_name":"Xin Qiao"},{"first_name":"Yu Xuan","full_name":"Bai, Yu Xuan","last_name":"Bai"},{"first_name":"Peng Chao","last_name":"Hao","full_name":"Hao, Peng Chao"},{"last_name":"Lin","full_name":"Lin, Wen Hui","first_name":"Wen Hui"},{"last_name":"Friml","id":"4159519E-F248-11E8-B48F-1D18A9856A87","full_name":"Friml, Jiří","first_name":"Jiří","orcid":"0000-0002-8302-7596"},{"full_name":"Xue, Hong Wei","last_name":"Xue","first_name":"Hong Wei"}],"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","month":"07","external_id":{"isi":["001533244800001"],"pmid":["40668679"]},"citation":{"mla":"Guan, Bin, et al. “Arabidopsis Phospholipase Dζ2 Facilitates Vacuolar Acidification and Autophagy under Phosphorus Starvation by Interacting with VATD.” <i>Cell Reports</i>, vol. 44, no. 7, 116024, Elsevier, 2025, doi:<a href=\"https://doi.org/10.1016/j.celrep.2025.116024\">10.1016/j.celrep.2025.116024</a>.","ieee":"B. Guan <i>et al.</i>, “Arabidopsis phospholipase Dζ2 facilitates vacuolar acidification and autophagy under phosphorus starvation by interacting with VATD,” <i>Cell Reports</i>, vol. 44, no. 7. Elsevier, 2025.","short":"B. Guan, K.X. Xie, X.Q. Du, Y.X. Bai, P.C. Hao, W.H. Lin, J. Friml, H.W. Xue, Cell Reports 44 (2025).","apa":"Guan, B., Xie, K. X., Du, X. Q., Bai, Y. X., Hao, P. C., Lin, W. H., … Xue, H. W. (2025). Arabidopsis phospholipase Dζ2 facilitates vacuolar acidification and autophagy under phosphorus starvation by interacting with VATD. <i>Cell Reports</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.celrep.2025.116024\">https://doi.org/10.1016/j.celrep.2025.116024</a>","ista":"Guan B, Xie KX, Du XQ, Bai YX, Hao PC, Lin WH, Friml J, Xue HW. 2025. Arabidopsis phospholipase Dζ2 facilitates vacuolar acidification and autophagy under phosphorus starvation by interacting with VATD. Cell Reports. 44(7), 116024.","ama":"Guan B, Xie KX, Du XQ, et al. Arabidopsis phospholipase Dζ2 facilitates vacuolar acidification and autophagy under phosphorus starvation by interacting with VATD. <i>Cell Reports</i>. 2025;44(7). doi:<a href=\"https://doi.org/10.1016/j.celrep.2025.116024\">10.1016/j.celrep.2025.116024</a>","chicago":"Guan, Bin, Ke Xuan Xie, Xin Qiao Du, Yu Xuan Bai, Peng Chao Hao, Wen Hui Lin, Jiří Friml, and Hong Wei Xue. “Arabidopsis Phospholipase Dζ2 Facilitates Vacuolar Acidification and Autophagy under Phosphorus Starvation by Interacting with VATD.” <i>Cell Reports</i>. Elsevier, 2025. <a href=\"https://doi.org/10.1016/j.celrep.2025.116024\">https://doi.org/10.1016/j.celrep.2025.116024</a>."},"publication_identifier":{"eissn":["2211-1247"],"issn":["2639-1856"]},"title":"Arabidopsis phospholipase Dζ2 facilitates vacuolar acidification and autophagy under phosphorus starvation by interacting with VATD","publication":"Cell Reports","date_updated":"2025-09-30T14:05:28Z","publisher":"Elsevier","year":"2025","ddc":["580"],"date_created":"2025-07-20T22:02:01Z","oa":1,"OA_type":"hybrid","_id":"20029","day":"22","issue":"7","file":[{"file_id":"20067","file_name":"2025_CellReports_Guan.pdf","success":1,"date_updated":"2025-07-22T08:52:17Z","content_type":"application/pdf","checksum":"ee03deee47a084b0295251dc49470ad4","creator":"dernst","relation":"main_file","file_size":37708120,"access_level":"open_access","date_created":"2025-07-22T08:52:17Z"}],"publication_status":"published","department":[{"_id":"JiFr"}],"isi":1,"scopus_import":"1","has_accepted_license":"1","date_published":"2025-07-22T00:00:00Z","article_number":"116024","acknowledgement":"The study was supported by National Natural Science Foundation of China (NSFC, 92354301, 32230011, 32200274, and 91954206). The computations were run on the Siyuan-1 cluster supported by the Center for High-Performance Computing at Shanghai Jiao Tong University.","pmid":1,"OA_place":"publisher","language":[{"iso":"eng"}],"license":"https://creativecommons.org/licenses/by-nc/4.0/","oa_version":"Published Version","file_date_updated":"2025-07-22T08:52:17Z","abstract":[{"lang":"eng","text":"Vacuolar acidification is crucial for the homeostasis of intracellular pH and the recycling of proteins and nutrients in cells, thereby playing important roles in various physiological processes related to vacuolar function. The key factors regulating vacuolar acidification and underlying mechanisms remain unclear. Here, we report that Arabidopsis phospholipase Dζ2 (PLDζ2) promotes the acidification of the vacuolar lumen to stimulate autophagic degradation under phosphorus deficiency. The pldζ2 mutant massively accumulates autophagic structures while exhibiting premature leaf senescence under nutrient starvation. Impaired autophagic flux, lytic vacuole morphology, and lytic degradation in pldζ2 indicate that PLDζ2 regulates autophagy by affecting the vacuolar function. PLDζ2 locates in both tonoplast and cytoplasm. Genetic, structural, and biochemical studies demonstrate that PLDζ2 directly interacts with vacuolar-type ATPase (V-ATPase) subunit D (VATD) to promote vacuolar acidification and autophagy under phosphorus starvation. These findings reveal the importance of V-ATPase and vacuolar pH in autophagic activity and provide clues in elucidating the regulatory mechanism of vacuolar acidification."}],"quality_controlled":"1","article_type":"original","article_processing_charge":"Yes (in subscription journal)","intvolume":"        44","tmp":{"image":"/images/cc_by_nc.png","short":"CC BY-NC (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)"},"volume":44,"status":"public","type":"journal_article"},{"publication_status":"published","issue":"8","file":[{"content_type":"application/pdf","checksum":"3c43e040a4a7a65ec67ae1d2bb81261a","creator":"dernst","date_created":"2025-08-05T06:15:09Z","access_level":"open_access","relation":"main_file","file_size":24178018,"date_updated":"2025-08-05T06:15:09Z","file_id":"20120","file_name":"2025_CellReports_Xu.pdf","success":1}],"oa":1,"ddc":["580"],"date_created":"2025-08-04T13:39:11Z","_id":"20116","day":"24","OA_type":"gold","publication_identifier":{"eissn":["2211-1247"]},"title":"Germin-like protein 1 interacts with proteasome regulator 1 to regulate auxin signaling by controlling Aux/IAA homeostasis","publisher":"Elsevier","date_updated":"2025-09-30T14:13:45Z","year":"2025","publication":"Cell Reports","author":[{"first_name":"Faqing","last_name":"Xu","full_name":"Xu, Faqing"},{"last_name":"Yu","full_name":"Yu, Yongqiang","first_name":"Yongqiang"},{"last_name":"Guan","full_name":"Guan, Bin","id":"56aad729-cca2-11ed-a45a-9b4138991a48","first_name":"Bin"},{"first_name":"Tongda","full_name":"Xu, Tongda","last_name":"Xu"},{"last_name":"Xu","full_name":"Xu, Zhihong","first_name":"Zhihong"},{"first_name":"Hongwei","full_name":"Xue, Hongwei","last_name":"Xue"}],"doi":"10.1016/j.celrep.2025.116056","month":"07","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","external_id":{"isi":["001542038500001"],"pmid":["40714631"]},"citation":{"ama":"Xu F, Yu Y, Guan B, Xu T, Xu Z, Xue H. Germin-like protein 1 interacts with proteasome regulator 1 to regulate auxin signaling by controlling Aux/IAA homeostasis. <i>Cell Reports</i>. 2025;44(8). doi:<a href=\"https://doi.org/10.1016/j.celrep.2025.116056\">10.1016/j.celrep.2025.116056</a>","chicago":"Xu, Faqing, Yongqiang Yu, Bin Guan, Tongda Xu, Zhihong Xu, and Hongwei Xue. “Germin-like Protein 1 Interacts with Proteasome Regulator 1 to Regulate Auxin Signaling by Controlling Aux/IAA Homeostasis.” <i>Cell Reports</i>. Elsevier, 2025. <a href=\"https://doi.org/10.1016/j.celrep.2025.116056\">https://doi.org/10.1016/j.celrep.2025.116056</a>.","ista":"Xu F, Yu Y, Guan B, Xu T, Xu Z, Xue H. 2025. Germin-like protein 1 interacts with proteasome regulator 1 to regulate auxin signaling by controlling Aux/IAA homeostasis. Cell Reports. 44(8), 116056.","apa":"Xu, F., Yu, Y., Guan, B., Xu, T., Xu, Z., &#38; Xue, H. (2025). Germin-like protein 1 interacts with proteasome regulator 1 to regulate auxin signaling by controlling Aux/IAA homeostasis. <i>Cell Reports</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.celrep.2025.116056\">https://doi.org/10.1016/j.celrep.2025.116056</a>","short":"F. Xu, Y. Yu, B. Guan, T. Xu, Z. Xu, H. Xue, Cell Reports 44 (2025).","mla":"Xu, Faqing, et al. “Germin-like Protein 1 Interacts with Proteasome Regulator 1 to Regulate Auxin Signaling by Controlling Aux/IAA Homeostasis.” <i>Cell Reports</i>, vol. 44, no. 8, 116056, Elsevier, 2025, doi:<a href=\"https://doi.org/10.1016/j.celrep.2025.116056\">10.1016/j.celrep.2025.116056</a>.","ieee":"F. Xu, Y. Yu, B. Guan, T. Xu, Z. Xu, and H. Xue, “Germin-like protein 1 interacts with proteasome regulator 1 to regulate auxin signaling by controlling Aux/IAA homeostasis,” <i>Cell Reports</i>, vol. 44, no. 8. Elsevier, 2025."},"tmp":{"image":"/images/cc_by_nc.png","short":"CC BY-NC (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)"},"intvolume":"        44","volume":44,"status":"public","type":"journal_article","abstract":[{"lang":"eng","text":"Auxin regulates various aspects of plant growth and development by modulating the transcription of target genes through the degradation of auxin/indole-3-acetic acid (Aux/IAA) repressors via the 26S proteasome. Proteasome regulator 1 (PTRE1), a positive regulator of proteasome activity, has been implicated in auxin-mediated proteasome suppression; however, the mechanism by which auxin modulates PTRE1 function remains unclear. Here, we demonstrate that auxin promotes the interaction between germin-like protein 1 (GLP1) and PTRE1, facilitating PTRE1 retention at the plasma membrane. The relocation of PTRE1 results in reduced nuclear 26S proteasome activity, and thus the attenuated Aux/IAA degradation and altered Aux/IAA homeostasis, ultimately resulting in suppressed auxin-mediated transcriptional regulation. Our findings uncover a previously uncharacterized regulatory axis in auxin signaling that controls Aux/IAA protein stability, functioning alongside the TIR1- and TRANSMEMBRANE KINASE 1 (TMK1)-mediated pathways, and highlight the coordination of auxin signaling from the cell surface to the nucleus via auxin-induced PTRE1 relocation, which fine-tunes Aux/IAA protein homeostasis and auxin responses."}],"file_date_updated":"2025-08-05T06:15:09Z","language":[{"iso":"eng"}],"oa_version":"Published Version","article_processing_charge":"Yes","quality_controlled":"1","article_type":"original","OA_place":"publisher","pmid":1,"scopus_import":"1","department":[{"_id":"JiFr"}],"isi":1,"article_number":"116056","date_published":"2025-07-24T00:00:00Z","DOAJ_listed":"1","acknowledgement":"The study was supported by the National Natural Science Foundation of China (NSFC; 32230011, 91954206, and 31721001). We thank Dr. Deli Lin (Shanghai Jiao Tong University) for kind help with the laser confocal microscope observation and the Arabidopsis Biological Resource Center (ABRC) for providing T-DNA insertional mutants.","has_accepted_license":"1"}]