The ER-PM interaction is essential for cytokinesis and recruits the actin cytoskeleton through the SCAR/WAVE complex

• 成果类型: Article
• 署名作者: Xu, Zhijing; Zang, Jingze; Zhang, Xintong; Zheng, Qiwei; Li, Yifan; Field, Nadine; Fiserova, Jindriska; Hua, Bing; Qu, Xiaolu; Kriechbaumer, Verena; Deeks, Michael J.; Hussey, Patrick J.; Wang, Pengwei
• 署名单位: Huazhong Agricultural University; Hubei Hongshan Laboratory; Oxford Brookes University; Durham University; Yangzhou University; University of Exeter
• 刊物名称: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
• ISSN/ISSBN: 0027-12960
• DOI: 10.1073/pnas.2416927122
• 发表日期: 2025-02-11
• 关键词: endoplasmic-reticulum; plasma-membrane; arabidopsis; scar; proteins; plasmodesmata; localization; activation; DYNAMICS; mediate

摘要

Plant cytokinesis requires coordination between the actin cytoskeleton, microtubules, and membranes to guide division plane formation and cell plate expansion; how these regulatory factors are coordinated remains unknown. The actin cytoskeleton assembly is controlled by several actin nucleation factors, such as the SCAR/WAVE complex, which regulates actin nucleation and branching through the activation of the ARP2/3 complex. The activity of these actin regulatory proteins is likely influenced by interactions with specific membranes; however, the molecular basis and the biological relevance of SCAR-membrane interactions are also unclear. In this study, we demonstrate that the ER-PM tethering protein VAP27-1 directly interacts with SCAR2 at the ER membrane and that they colocalize to guide cell plate orientation during cell division. In the root meristem, both VAP27-1 and SCAR2 exhibit polarized localization at the cell plates, where the interaction between ER and PM is abundant. VAP27-1 recruits SCAR2 to the cell division plane, where there is a high concentration of actin filaments. In the vap27- 1346 mutant, the densities of cortical ER, SCAR2, and consequently actin filaments are significantly reduced at the cell division plane, affecting cell plate orientation, cell division, and root development. A similar phenomenon is also observed in the scar1234 mutant, suggesting that VAP27 and SCAR proteins regulate cell division through a similar pathway. In conclusion, our data reveal a plant- specific function of VAP27- regulated ER-PM interaction and advance our understanding of plant ER-PM contact site and its role in cell division.