--- _id: '10719' abstract: - lang: eng text: Auxin, one of the first identified and most widely studied phytohormones, has been and will remain a hot topic in plant biology. After more than a century of passionate exploration, the mysteries of its synthesis, transport, signaling, and metabolism have largely been unlocked. Due to the rapid development of new technologies, new methods, and new genetic materials, the study of auxin has entered the fast lane over the past 30 years. Here, we highlight advances in understanding auxin signaling, including auxin perception, rapid auxin responses, TRANSPORT INHIBITOR RESPONSE 1 and AUXIN SIGNALING F-boxes (TIR1/AFBs)-mediated transcriptional and non-transcriptional branches, and the epigenetic regulation of auxin signaling. We also focus on feedback inhibition mechanisms that prevent the over-amplification of auxin signals. In addition, we cover the TRANSMEMBRANE KINASEs (TMKs)-mediated non-canonical signaling, which converges with TIR1/AFBs-mediated transcriptional regulation to coordinate plant growth and development. The identification of additional auxin signaling components and their regulation will continue to open new avenues of research in this field, leading to an increasingly deeper, more comprehensive understanding of how auxin signals are interpreted at the cellular level to regulate plant growth and development. acknowledgement: "This research was financially supported by the National Natural Science Foundation of China and the Israel Science Foundation (NSFC-ISF; 32061143005), National Natural Science Foundation of China (32000225), Natural Science Foundation of Shandong Province (ZR2020QC036), and China Postdoctoral Science Foundation (2020M682165).\r\n" article_processing_charge: No article_type: review author: - first_name: Z full_name: Yu, Z last_name: Yu - first_name: F full_name: Zhang, F last_name: Zhang - first_name: Jiří full_name: Friml, Jiří id: 4159519E-F248-11E8-B48F-1D18A9856A87 last_name: Friml orcid: 0000-0002-8302-7596 - first_name: Z full_name: Ding, Z last_name: Ding citation: ama: 'Yu Z, Zhang F, Friml J, Ding Z. Auxin signaling: Research advances over the past 30 years. Journal of Integrative Plant Biology. 2022;64(2):371-392. doi:10.1111/jipb.13225' apa: 'Yu, Z., Zhang, F., Friml, J., & Ding, Z. (2022). Auxin signaling: Research advances over the past 30 years. Journal of Integrative Plant Biology. Wiley. https://doi.org/10.1111/jipb.13225' chicago: 'Yu, Z, F Zhang, Jiří Friml, and Z Ding. “Auxin Signaling: Research Advances over the Past 30 Years.” Journal of Integrative Plant Biology. Wiley, 2022. https://doi.org/10.1111/jipb.13225.' ieee: 'Z. Yu, F. Zhang, J. Friml, and Z. Ding, “Auxin signaling: Research advances over the past 30 years,” Journal of Integrative Plant Biology, vol. 64, no. 2. Wiley, pp. 371–392, 2022.' ista: 'Yu Z, Zhang F, Friml J, Ding Z. 2022. Auxin signaling: Research advances over the past 30 years. Journal of Integrative Plant Biology. 64(2), 371–392.' mla: 'Yu, Z., et al. “Auxin Signaling: Research Advances over the Past 30 Years.” Journal of Integrative Plant Biology, vol. 64, no. 2, Wiley, 2022, pp. 371–92, doi:10.1111/jipb.13225.' short: Z. Yu, F. Zhang, J. Friml, Z. Ding, Journal of Integrative Plant Biology 64 (2022) 371–392. date_created: 2022-02-03T09:52:59Z date_published: 2022-02-01T00:00:00Z date_updated: 2023-08-02T14:08:30Z day: '01' department: - _id: JiFr doi: 10.1111/jipb.13225 external_id: isi: - '000761281200011' pmid: - '35018726' intvolume: ' 64' isi: 1 issue: '2' language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1111/jipb.13225 month: '02' oa: 1 oa_version: Published Version page: 371-392 pmid: 1 publication: Journal of Integrative Plant Biology publication_identifier: eissn: - 1744-7909 issn: - 1672-9072 publication_status: published publisher: Wiley quality_controlled: '1' scopus_import: '1' status: public title: 'Auxin signaling: Research advances over the past 30 years' type: journal_article user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8 volume: 64 year: '2022' ... --- _id: '10768' abstract: - lang: eng text: Among the most fascinated properties of the plant hormone auxin is its ability to promote formation of its own directional transport routes. These gradually narrowing auxin channels form from the auxin source toward the sink and involve coordinated, collective polarization of individual cells. Once established, the channels provide positional information, along which new vascular strands form, for example, during organogenesis, regeneration, or leave venation. The main prerequisite of this still mysterious auxin canalization mechanism is a feedback between auxin signaling and its directional transport. This is manifested by auxin-induced re-arrangements of polar, subcellular localization of PIN-FORMED (PIN) auxin exporters. Immanent open questions relate to how position of auxin source and sink as well as tissue context are sensed and translated into tissue polarization and how cells communicate to polarize coordinately. Recently, identification of the first molecular players opens new avenues into molecular studies of this intriguing example of self-organizing plant development. acknowledgement: The authors apologize to those researchers whose work was not cited. In addition, exciting topics such as PIN polarization in context of phyllotaxis, shoot branching and termination of gravitropic bending, or role of additional auxin transporters could not have been included owing to lack of space. This work was supported by the Czech Science Foundation GAČR (GA18-26981S). The authors also acknowledge the EMBO for supporting J.H. with a long-term fellowship (ALTF217-2021). article_number: '102174' article_processing_charge: Yes (via OA deal) article_type: original author: - first_name: Jakub full_name: Hajny, Jakub id: 4800CC20-F248-11E8-B48F-1D18A9856A87 last_name: Hajny orcid: 0000-0003-2140-7195 - first_name: Shutang full_name: Tan, Shutang id: 2DE75584-F248-11E8-B48F-1D18A9856A87 last_name: Tan orcid: 0000-0002-0471-8285 - first_name: Jiří full_name: Friml, Jiří id: 4159519E-F248-11E8-B48F-1D18A9856A87 last_name: Friml orcid: 0000-0002-8302-7596 citation: ama: 'Hajny J, Tan S, Friml J. Auxin canalization: From speculative models toward molecular players. Current Opinion in Plant Biology. 2022;65(2). doi:10.1016/j.pbi.2022.102174' apa: 'Hajny, J., Tan, S., & Friml, J. (2022). Auxin canalization: From speculative models toward molecular players. Current Opinion in Plant Biology. Elsevier. https://doi.org/10.1016/j.pbi.2022.102174' chicago: 'Hajny, Jakub, Shutang Tan, and Jiří Friml. “Auxin Canalization: From Speculative Models toward Molecular Players.” Current Opinion in Plant Biology. Elsevier, 2022. https://doi.org/10.1016/j.pbi.2022.102174.' ieee: 'J. Hajny, S. Tan, and J. Friml, “Auxin canalization: From speculative models toward molecular players,” Current Opinion in Plant Biology, vol. 65, no. 2. Elsevier, 2022.' ista: 'Hajny J, Tan S, Friml J. 2022. Auxin canalization: From speculative models toward molecular players. Current Opinion in Plant Biology. 65(2), 102174.' mla: 'Hajny, Jakub, et al. “Auxin Canalization: From Speculative Models toward Molecular Players.” Current Opinion in Plant Biology, vol. 65, no. 2, 102174, Elsevier, 2022, doi:10.1016/j.pbi.2022.102174.' short: J. Hajny, S. Tan, J. Friml, Current Opinion in Plant Biology 65 (2022). date_created: 2022-02-20T23:01:32Z date_published: 2022-02-01T00:00:00Z date_updated: 2023-08-02T14:29:12Z day: '01' ddc: - '580' department: - _id: JiFr doi: 10.1016/j.pbi.2022.102174 external_id: isi: - '000758724700004' pmid: - '35123880' file: - access_level: open_access checksum: f1ee02b6fb4200934eeb31fa69120885 content_type: application/pdf creator: dernst date_created: 2022-03-10T13:34:09Z date_updated: 2022-03-10T13:34:09Z file_id: '10844' file_name: 2022_CurrentOpPlantBiology_Hajny.pdf file_size: 820322 relation: main_file success: 1 file_date_updated: 2022-03-10T13:34:09Z has_accepted_license: '1' intvolume: ' 65' isi: 1 issue: '2' language: - iso: eng month: '02' oa: 1 oa_version: Published Version pmid: 1 publication: Current Opinion in Plant Biology publication_identifier: issn: - 1369-5266 publication_status: published publisher: Elsevier quality_controlled: '1' scopus_import: '1' status: public title: 'Auxin canalization: From speculative models toward molecular players' tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8 volume: 65 year: '2022' ... --- _id: '10841' abstract: - lang: eng text: In eukaryotes, clathrin-coated vesicles (CCVs) facilitate the internalization of material from the cell surface as well as the movement of cargo in post-Golgi trafficking pathways. This diversity of functions is partially provided by multiple monomeric and multimeric clathrin adaptor complexes that provide compartment and cargo selectivity. The adaptor-protein assembly polypeptide-1 (AP-1) complex operates as part of the secretory pathway at the trans-Golgi network (TGN), while the AP-2 complex and the TPLATE complex jointly operate at the plasma membrane to execute clathrin-mediated endocytosis. Key to our further understanding of clathrin-mediated trafficking in plants will be the comprehensive identification and characterization of the network of evolutionarily conserved and plant-specific core and accessory machinery involved in the formation and targeting of CCVs. To facilitate these studies, we have analyzed the proteome of enriched TGN/early endosome-derived and endocytic CCVs isolated from dividing and expanding suspension-cultured Arabidopsis (Arabidopsis thaliana) cells. Tandem mass spectrometry analysis results were validated by differential chemical labeling experiments to identify proteins co-enriching with CCVs. Proteins enriched in CCVs included previously characterized CCV components and cargos such as the vacuolar sorting receptors in addition to conserved and plant-specific components whose function in clathrin-mediated trafficking has not been previously defined. Notably, in addition to AP-1 and AP-2, all subunits of the AP-4 complex, but not AP-3 or AP-5, were found to be in high abundance in the CCV proteome. The association of AP-4 with suspension-cultured Arabidopsis CCVs is further supported via additional biochemical data. acknowledged_ssus: - _id: EM-Fac acknowledgement: 'The authors would like to acknowledge the VIB Proteomics Core Facility (VIB-UGent Center for Medical Biotechnology in Ghent, Belgium) and the Research Technology Support Facility Proteomics Core (Michigan State University in East Lansing, Michigan) for sample analysis, as well as the University of Wisconsin Biotechnology Center Mass Spectrometry Core Facility (Madison, WI) for help with data processing. Additionally, we are grateful to Sue Weintraub (UT Health San Antonio) and Sydney Thomas (UW- Madison) for assistance with data analysis. This research was supported by grants to S.Y.B. from the National Science Foundation (Nos. 1121998 and 1614915) and a Vilas Associate Award (University of Wisconsin, Madison, Graduate School); to J.P. from the National Natural Science Foundation of China (Nos. 91754104, 31820103008, and 31670283); to I.H. from the National Research Foundation of Korea (No. 2019R1A2B5B03099982). This research was also supported by the Scientific Service Units (SSU) of IST Austria through resources provided by the Electron microscopy Facility (EMF). A.J. is supported by funding from the Austrian Science Fund (FWF): I3630B25 to J.F. A.H. is supported by funding from the National Science Foundation (NSF IOS Nos. 1025837 and 1147032).' article_processing_charge: No article_type: original author: - first_name: DA full_name: Dahhan, DA last_name: Dahhan - first_name: GD full_name: Reynolds, GD last_name: Reynolds - first_name: JJ full_name: Cárdenas, JJ last_name: Cárdenas - first_name: D full_name: Eeckhout, D last_name: Eeckhout - first_name: Alexander J full_name: Johnson, Alexander J id: 46A62C3A-F248-11E8-B48F-1D18A9856A87 last_name: Johnson orcid: 0000-0002-2739-8843 - first_name: K full_name: Yperman, K last_name: Yperman - first_name: Walter full_name: Kaufmann, Walter id: 3F99E422-F248-11E8-B48F-1D18A9856A87 last_name: Kaufmann orcid: 0000-0001-9735-5315 - first_name: N full_name: Vang, N last_name: Vang - first_name: X full_name: Yan, X last_name: Yan - first_name: I full_name: Hwang, I last_name: Hwang - first_name: A full_name: Heese, A last_name: Heese - first_name: G full_name: De Jaeger, G last_name: De Jaeger - first_name: Jiří full_name: Friml, Jiří id: 4159519E-F248-11E8-B48F-1D18A9856A87 last_name: Friml orcid: 0000-0002-8302-7596 - first_name: D full_name: Van Damme, D last_name: Van Damme - first_name: J full_name: Pan, J last_name: Pan - first_name: SY full_name: Bednarek, SY last_name: Bednarek citation: ama: Dahhan D, Reynolds G, Cárdenas J, et al. Proteomic characterization of isolated Arabidopsis clathrin-coated vesicles reveals evolutionarily conserved and plant-specific components. Plant Cell. 2022;34(6):2150-2173. doi:10.1093/plcell/koac071 apa: Dahhan, D., Reynolds, G., Cárdenas, J., Eeckhout, D., Johnson, A. J., Yperman, K., … Bednarek, S. (2022). Proteomic characterization of isolated Arabidopsis clathrin-coated vesicles reveals evolutionarily conserved and plant-specific components. Plant Cell. Oxford Academic. https://doi.org/10.1093/plcell/koac071 chicago: Dahhan, DA, GD Reynolds, JJ Cárdenas, D Eeckhout, Alexander J Johnson, K Yperman, Walter Kaufmann, et al. “Proteomic Characterization of Isolated Arabidopsis Clathrin-Coated Vesicles Reveals Evolutionarily Conserved and Plant-Specific Components.” Plant Cell. Oxford Academic, 2022. https://doi.org/10.1093/plcell/koac071. ieee: D. Dahhan et al., “Proteomic characterization of isolated Arabidopsis clathrin-coated vesicles reveals evolutionarily conserved and plant-specific components,” Plant Cell, vol. 34, no. 6. Oxford Academic, pp. 2150–2173, 2022. ista: Dahhan D, Reynolds G, Cárdenas J, Eeckhout D, Johnson AJ, Yperman K, Kaufmann W, Vang N, Yan X, Hwang I, Heese A, De Jaeger G, Friml J, Van Damme D, Pan J, Bednarek S. 2022. Proteomic characterization of isolated Arabidopsis clathrin-coated vesicles reveals evolutionarily conserved and plant-specific components. Plant Cell. 34(6), 2150–2173. mla: Dahhan, DA, et al. “Proteomic Characterization of Isolated Arabidopsis Clathrin-Coated Vesicles Reveals Evolutionarily Conserved and Plant-Specific Components.” Plant Cell, vol. 34, no. 6, Oxford Academic, 2022, pp. 2150–73, doi:10.1093/plcell/koac071. short: D. Dahhan, G. Reynolds, J. Cárdenas, D. Eeckhout, A.J. Johnson, K. Yperman, W. Kaufmann, N. Vang, X. Yan, I. Hwang, A. Heese, G. De Jaeger, J. Friml, D. Van Damme, J. Pan, S. Bednarek, Plant Cell 34 (2022) 2150–2173. date_created: 2022-03-08T13:47:51Z date_published: 2022-06-01T00:00:00Z date_updated: 2023-08-02T14:46:48Z day: '01' department: - _id: JiFr - _id: EM-Fac doi: 10.1093/plcell/koac071 external_id: isi: - '000767438800001' pmid: - '35218346' intvolume: ' 34' isi: 1 issue: '6' language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1101/2021.09.16.460678 month: '06' oa: 1 oa_version: Preprint page: 2150-2173 pmid: 1 project: - _id: 26538374-B435-11E9-9278-68D0E5697425 call_identifier: FWF grant_number: I03630 name: Molecular mechanisms of endocytic cargo recognition in plants publication: Plant Cell publication_identifier: eissn: - 1532-298x issn: - 1040-4651 publication_status: published publisher: Oxford Academic quality_controlled: '1' scopus_import: '1' status: public title: Proteomic characterization of isolated Arabidopsis clathrin-coated vesicles reveals evolutionarily conserved and plant-specific components type: journal_article user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8 volume: 34 year: '2022' ... --- _id: '10888' abstract: - lang: eng text: Despite the growing interest in using chemical genetics in plant research, small molecule target identification remains a major challenge. The cellular thermal shift assay coupled with high-resolution mass spectrometry (CETSA MS) that monitors changes in the thermal stability of proteins caused by their interactions with small molecules, other proteins, or posttranslational modifications, allows the discovery of drug targets or the study of protein–metabolite and protein–protein interactions mainly in mammalian cells. To showcase the applicability of this method in plants, we applied CETSA MS to intact Arabidopsis thaliana cells and identified the thermal proteome of the plant-specific glycogen synthase kinase 3 (GSK3) inhibitor, bikinin. A comparison between the thermal and the phosphoproteomes of bikinin revealed the auxin efflux carrier PIN-FORMED1 (PIN1) as a substrate of the Arabidopsis GSK3s that negatively regulate the brassinosteroid signaling. We established that PIN1 phosphorylation by the GSK3s is essential for maintaining its intracellular polarity that is required for auxin-mediated regulation of vascular patterning in the leaf, thus revealing cross-talk between brassinosteroid and auxin signaling. acknowledgement: "We thank Yanhai Yin for providing the anti-BES1 antibody, Johan Winne and Brenda Callebaut for synthesizing bikinin, Yuki Kondo and Hiroo Fukuda for published materials, Tomasz Nodzy\x03nski for useful advice, and Martine De Cock for help in preparing the manuscript. This\r\nwork was supported by the China Scholarship Council for predoctoral (Q.L. and X.X.) and postdoctoral (Y.Z.) fellowships; the Agency for Innovation by Science and Technology for a predoctoral fellowship (W.D.); the Research Foundation-Flanders, Projects G009018N and G002121N (E.R.); and the VIB TechWatch Fund (E.R.)." article_number: e2118220119 article_processing_charge: No article_type: original author: - first_name: Qing full_name: Lu, Qing last_name: Lu - first_name: Yonghong full_name: Zhang, Yonghong last_name: Zhang - first_name: Joakim full_name: Hellner, Joakim last_name: Hellner - first_name: Caterina full_name: Giannini, Caterina id: e3fdddd5-f6e0-11ea-865d-ca99ee6367f4 last_name: Giannini - first_name: Xiangyu full_name: Xu, Xiangyu last_name: Xu - first_name: Jarne full_name: Pauwels, Jarne last_name: Pauwels - first_name: Qian full_name: Ma, Qian last_name: Ma - first_name: Wim full_name: Dejonghe, Wim last_name: Dejonghe - first_name: Huibin full_name: Han, Huibin id: 31435098-F248-11E8-B48F-1D18A9856A87 last_name: Han - first_name: Brigitte full_name: Van De Cotte, Brigitte last_name: Van De Cotte - first_name: Francis full_name: Impens, Francis last_name: Impens - first_name: Kris full_name: Gevaert, Kris last_name: Gevaert - first_name: Ive full_name: De Smet, Ive last_name: De Smet - first_name: Jiří full_name: Friml, Jiří id: 4159519E-F248-11E8-B48F-1D18A9856A87 last_name: Friml orcid: 0000-0002-8302-7596 - first_name: Daniel Martinez full_name: Molina, Daniel Martinez last_name: Molina - first_name: Eugenia full_name: Russinova, Eugenia last_name: Russinova citation: ama: Lu Q, Zhang Y, Hellner J, et al. Proteome-wide cellular thermal shift assay reveals unexpected cross-talk between brassinosteroid and auxin signaling. Proceedings of the National Academy of Sciences of the United States of America. 2022;119(11). doi:10.1073/pnas.2118220119 apa: Lu, Q., Zhang, Y., Hellner, J., Giannini, C., Xu, X., Pauwels, J., … Russinova, E. (2022). Proteome-wide cellular thermal shift assay reveals unexpected cross-talk between brassinosteroid and auxin signaling. Proceedings of the National Academy of Sciences of the United States of America. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.2118220119 chicago: Lu, Qing, Yonghong Zhang, Joakim Hellner, Caterina Giannini, Xiangyu Xu, Jarne Pauwels, Qian Ma, et al. “Proteome-Wide Cellular Thermal Shift Assay Reveals Unexpected Cross-Talk between Brassinosteroid and Auxin Signaling.” Proceedings of the National Academy of Sciences of the United States of America. Proceedings of the National Academy of Sciences, 2022. https://doi.org/10.1073/pnas.2118220119. ieee: Q. Lu et al., “Proteome-wide cellular thermal shift assay reveals unexpected cross-talk between brassinosteroid and auxin signaling,” Proceedings of the National Academy of Sciences of the United States of America, vol. 119, no. 11. Proceedings of the National Academy of Sciences, 2022. ista: Lu Q, Zhang Y, Hellner J, Giannini C, Xu X, Pauwels J, Ma Q, Dejonghe W, Han H, Van De Cotte B, Impens F, Gevaert K, De Smet I, Friml J, Molina DM, Russinova E. 2022. Proteome-wide cellular thermal shift assay reveals unexpected cross-talk between brassinosteroid and auxin signaling. Proceedings of the National Academy of Sciences of the United States of America. 119(11), e2118220119. mla: Lu, Qing, et al. “Proteome-Wide Cellular Thermal Shift Assay Reveals Unexpected Cross-Talk between Brassinosteroid and Auxin Signaling.” Proceedings of the National Academy of Sciences of the United States of America, vol. 119, no. 11, e2118220119, Proceedings of the National Academy of Sciences, 2022, doi:10.1073/pnas.2118220119. short: Q. Lu, Y. Zhang, J. Hellner, C. Giannini, X. Xu, J. Pauwels, Q. Ma, W. Dejonghe, H. Han, B. Van De Cotte, F. Impens, K. Gevaert, I. De Smet, J. Friml, D.M. Molina, E. Russinova, Proceedings of the National Academy of Sciences of the United States of America 119 (2022). date_created: 2022-03-20T23:01:39Z date_published: 2022-03-07T00:00:00Z date_updated: 2023-08-03T06:06:27Z day: '07' ddc: - '580' department: - _id: JiFr doi: 10.1073/pnas.2118220119 external_id: isi: - '000771756300008' pmid: - '35254915' file: - access_level: open_access checksum: 83e0fea7919570d0b519b41193342571 content_type: application/pdf creator: dernst date_created: 2022-03-21T09:19:47Z date_updated: 2022-03-21T09:19:47Z file_id: '10910' file_name: 2022_PNAS_Lu.pdf file_size: 2169534 relation: main_file success: 1 file_date_updated: 2022-03-21T09:19:47Z has_accepted_license: '1' intvolume: ' 119' isi: 1 issue: '11' language: - iso: eng license: https://creativecommons.org/licenses/by-nc-nd/4.0/ month: '03' oa: 1 oa_version: Published Version pmid: 1 publication: Proceedings of the National Academy of Sciences of the United States of America publication_identifier: eissn: - 1091-6490 publication_status: published publisher: Proceedings of the National Academy of Sciences quality_controlled: '1' scopus_import: '1' status: public title: Proteome-wide cellular thermal shift assay reveals unexpected cross-talk between brassinosteroid and auxin signaling tmp: image: /images/cc_by_nc_nd.png legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) short: CC BY-NC-ND (4.0) type: journal_article user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8 volume: 119 year: '2022' ... --- _id: '11589' abstract: - lang: eng text: Calcium-dependent protein kinases (CPK) are key components of a wide array of signaling pathways, translating stress and nutrient signaling into the modulation of cellular processes such as ion transport and transcription. However, not much is known about CPKs in endomembrane trafficking. Here, we screened for CPKs that impact on root growth and gravitropism, by overexpressing constitutively active forms of CPKs under the control of an inducible promoter in Arabidopsis thaliana. We found that inducible overexpression of an constitutive active CPK30 (CA-CPK30) resulted in a loss of root gravitropism and ectopic auxin accumulation in the root tip. Immunolocalization revealed that CA-CPK30 roots have reduced PIN protein levels, PIN1 polarity defects and impaired Brefeldin A (BFA)-sensitive trafficking. Moreover, FM4-64 uptake was reduced, indicative of a defect in endocytosis. The effects on BFA-sensitive trafficking were not specific to PINs, as BFA could not induce aggregation of ARF1- and CHC-labeled endosomes in CA-CPK30. Interestingly, the interference with BFA-body formation, could be reverted by increasing the extracellular pH, indicating a pH-dependence of this CA-CPK30 effect. Altogether, our data reveal an important role for CPK30 in root growth regulation and endomembrane trafficking in Arabidopsis thaliana. acknowledgement: "RW and JC predoctoral fellows that were supported by the Chinese Science Counsil. The IPS2 benefits from the support of the LabEx Saclay Plant Sciences-SPS (ANR-10-LABX-0040-SPS).\r\nWe thank Jen Sheen for establishing and generously sharing the CKP family clone sets, and for providing useful feedback on the manuscript." article_number: '862398' article_processing_charge: No article_type: original author: - first_name: Ren full_name: Wang, Ren last_name: Wang - first_name: Ellie full_name: Himschoot, Ellie last_name: Himschoot - first_name: Jian full_name: Chen, Jian last_name: Chen - first_name: Marie full_name: Boudsocq, Marie last_name: Boudsocq - first_name: Danny full_name: Geelen, Danny last_name: Geelen - first_name: Jiří full_name: Friml, Jiří id: 4159519E-F248-11E8-B48F-1D18A9856A87 last_name: Friml orcid: 0000-0002-8302-7596 - first_name: Tom full_name: Beeckman, Tom last_name: Beeckman - first_name: Steffen full_name: Vanneste, Steffen last_name: Vanneste citation: ama: Wang R, Himschoot E, Chen J, et al. Constitutive active CPK30 interferes with root growth and endomembrane trafficking in Arabidopsis thaliana. Frontiers in Plant Science. 2022;13. doi:10.3389/fpls.2022.862398 apa: Wang, R., Himschoot, E., Chen, J., Boudsocq, M., Geelen, D., Friml, J., … Vanneste, S. (2022). Constitutive active CPK30 interferes with root growth and endomembrane trafficking in Arabidopsis thaliana. Frontiers in Plant Science. Frontiers. https://doi.org/10.3389/fpls.2022.862398 chicago: Wang, Ren, Ellie Himschoot, Jian Chen, Marie Boudsocq, Danny Geelen, Jiří Friml, Tom Beeckman, and Steffen Vanneste. “Constitutive Active CPK30 Interferes with Root Growth and Endomembrane Trafficking in Arabidopsis Thaliana.” Frontiers in Plant Science. Frontiers, 2022. https://doi.org/10.3389/fpls.2022.862398. ieee: R. Wang et al., “Constitutive active CPK30 interferes with root growth and endomembrane trafficking in Arabidopsis thaliana,” Frontiers in Plant Science, vol. 13. Frontiers, 2022. ista: Wang R, Himschoot E, Chen J, Boudsocq M, Geelen D, Friml J, Beeckman T, Vanneste S. 2022. Constitutive active CPK30 interferes with root growth and endomembrane trafficking in Arabidopsis thaliana. Frontiers in Plant Science. 13, 862398. mla: Wang, Ren, et al. “Constitutive Active CPK30 Interferes with Root Growth and Endomembrane Trafficking in Arabidopsis Thaliana.” Frontiers in Plant Science, vol. 13, 862398, Frontiers, 2022, doi:10.3389/fpls.2022.862398. short: R. Wang, E. Himschoot, J. Chen, M. Boudsocq, D. Geelen, J. Friml, T. Beeckman, S. Vanneste, Frontiers in Plant Science 13 (2022). date_created: 2022-07-17T22:01:54Z date_published: 2022-06-16T00:00:00Z date_updated: 2023-08-03T12:01:47Z day: '16' ddc: - '580' department: - _id: JiFr doi: 10.3389/fpls.2022.862398 external_id: isi: - '000819250500001' pmid: - '35783951' file: - access_level: open_access checksum: 95313515637c0f84de591d204375d764 content_type: application/pdf creator: dernst date_created: 2022-07-18T08:05:15Z date_updated: 2022-07-18T08:05:15Z file_id: '11596' file_name: 2022_FrontiersPlantScience_Wang.pdf file_size: 5040638 relation: main_file success: 1 file_date_updated: 2022-07-18T08:05:15Z has_accepted_license: '1' intvolume: ' 13' isi: 1 language: - iso: eng month: '06' oa: 1 oa_version: Published Version pmid: 1 publication: Frontiers in Plant Science publication_identifier: eissn: - 1664-462X publication_status: published publisher: Frontiers quality_controlled: '1' related_material: link: - relation: erratum url: https://doi.org/10.3389/fpls.2022.1100792 scopus_import: '1' status: public title: Constitutive active CPK30 interferes with root growth and endomembrane trafficking in Arabidopsis thaliana tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8 volume: 13 year: '2022' ...