Yinwei Zeng was born on September 1994 in Chongqing, China. He earned a Bachelor of Agronomy in July 2018 at Northwest A&F University, China. During his bachelor study, he was fascinated by the plant-microbe interactions and investigated symbiosis's role in plant arsenic tolerance mechanism. After graduating in July 2018, He moved to Ghent University, Belgium to continue research on root development as a PhD candidate in the Horticell group, Department Plants and Crops, Faculty of Bioscience Engineering. Under the supervision of Danny Geelen and Steffen Vanneste, he gained profound insights into regulating adventitious root development using pro-auxin HYSPARIN. He completed his PhD in October 2023 and served as a post-doc to reveal the model of action of HYSPAIN. Yinwei is searching for post-doc opportunities related to plant-microbe interactions and plant development to continue his scientific career.
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HYSPARIN: A chemical approach towards understanding adventitious rooting
YINWEI ZENG, STEFFEN VANNESTE, DANNY GEELEN
Department Plants and Crops, Ghent University, Coupure Links 653, B-9000 Ghent, Belgium
Adventitious root (AR) formation and lateral root branching are agronomic important traits determining crop yield and the efficiency of clonal propagation. While LR initiation has been studied intensively, AR ontogeny and its relationship to the initiation of LRs remain largely unknown. We identified a small molecule named HYSPARIN (HYS) based on a strong AR-inducing capacity without pronounced effects on primary root growth and lateral root branching. We found that HYS activates the pericycle in Arabidopsis hypocotyls, yet is not a typical auxin, as seen in a lack of early induction of transcriptional auxin-responses, DII-Venus degradation or Ca2+ signaling. Yet, HYS-induced AR induction involves nuclear and plasma membrane-localized auxin signaling pathways and the late induction of multiple auxin-inducible genes that are associated with LR development, such as SHY2/IAA3, PUCHI, MAKR4 and GATA23. We further characterized the mode of action of HYS. We found that HYS’s bioactivity is strictly dependent on the cotyledons. This implies that a HYS metabolite, or a HYS-induced compound is formed in cotyledons that need to be transported to the hypocotyl to induce AR. Our data suggest that HYS is hydrolyzed by AMI1 and IAMH1, ILR1-like proteins to slow-release MCPA locally to induce AR formation