RT Journal Article SR Electronic T1 Synthetic dysmobility screening reveals a phosphorylation-independent facet of the SLK-Ezrin-F-actin signaling cascade JF bioRxiv FD Cold Spring Harbor Laboratory SP 2024.07.23.604488 DO 10.1101/2024.07.23.604488 A1 Lin, Hsuan-Chao A1 Lin, Yun-Yu A1 Wei, Ling-Ying A1 Zhang, Jia-Ming A1 Tsai, Pei-Ju A1 Lin, Yu-Chiao A1 Chia, Jean-San A1 Tsai, Feng-Chiao YR 2024 UL http://biorxiv.org/content/early/2024/07/24/2024.07.23.604488.abstract AB This study investigates the role of Ste20-like kinase (SLK) in cytoskeletal dynamics, focusing on its interaction with Ezrin and actin remodeling, independent of phosphorylation processes. We utilized HaCaT to explore the effects of SLK and Ezrin knockdown, as well as the application of specific inhibitors on the organization of actin structures. Our findings reveal that both SLK and Ezrin significantly influence the architecture of actin cytoskeletons with differential impacts observed between protein knockdown and dephosphorylation events. Additionally, our results suggest novel, phosphorylation-independent pathways through which Ezrin modulates actin dynamics, potentially indicating alternative, non-enzymatic roles for Ezrin in cytoskeletal integrity.Competing Interest StatementThe authors have declared no competing interest.