14-3-3 proteins stabilize actin and vimentin filaments to maintain processes in glomerular podocyte

Link to bioRxiv paper: http://biorxiv.org/cgi/content/short/2023.04.25.538276v1?rss=1 Authors: Yasuda, H., Fukusumi, Y., Zhang, Y., Kawachi, H. Abstract: Adaptor protein 14-3-3s have isoform-specific binding partners and roles. We reported 14-3-3{beta} interacts with FKBP12 and synaptopodin to maintain the structure of actin fibers in podocytes. However, differential roles of 14-3-3 isoforms in kidneys are unclear. Herein, we showed that 14-3-3{beta} was dominantly co-localized with FKBP12 in foot processes and was partially co-localized with Par3 at slit diaphragm in podocytes. 14-3-3{beta} interacted with Par3, and FKBP12 bound to 14-3-3{beta} competitively with Par3. Although deletion of 14-3-3{beta} enhanced the interaction of Par3-Par6, it altered actin fiber structure and processes. 14-3-3{beta} and synaptopodin were downregulated in podocyte injury models. 14-3-3{sigma} in podocytes interacted with vimentin in primary processes but not with the actin-associated proteins in foot processes. Deletion of 14-3-3{sigma} altered vimentin fiber structure and processes. 14-3-3{sigma} and vimentin were upregulated in the early phase of podocyte injury models but were decreased in the end stage. Together, the precise localization of 14-3-3{beta} at actin cytoskeleton plays a role in maintaining foot processes and Par complex in podocytes. 14-3-3{sigma} at vimentin cytoskeleton is essential for maintaining primary processes. Copy rights belong to original authors. Visit the link for more info Podcast created by Paper Player, LLC