施一公团队发表最新PNAS论文

Core Viewpoint - The recent research published in PNAS by a team from Westlake University reveals the structural basis of auxin binding and transport by the AUX1 protein in Arabidopsis thaliana, which is crucial for understanding plant growth and development [2][5]. Group 1: Research Findings - The study elucidates the cryo-electron microscopy structures of AUX1 in both IAA-unbound and IAA-bound states, highlighting the significant conformational changes that occur upon IAA binding [3][5]. - AUX1 exists as a monomer and comprises 11 transmembrane helices, with TM1 to TM5 and TM6 to TM10 forming two halves of the classic LeuT fold, while TM11 interacts at the junction of these halves [5]. - The central pocket formed by TM1, TM3, TM6, and TM8 specifically recognizes IAA, and the conformational changes in TM1 and TM6 are critical for the transport of IAA [5]. Group 2: Implications and Future Research - The findings provide a molecular basis for AUX1-mediated IAA binding and transport, laying the groundwork for future structural-based functional studies of the AUX1/LAX family and the application of auxin analogs in agriculture [5]. - Following the PNAS publication, a related study from institutions in France, Denmark, and Germany was published in Nature Plants, which also analyzed the structures and mechanisms of AUX/LAX transporters involved in auxin import [6].