1. AIF1L regulates actomyosin contractility and filopodial extensions in human podocytes.
- Author
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Yasuda-Yamahara M, Rogg M, Yamahara K, Maier JI, Huber TB, and Schell C
- Subjects
- Cells, Cultured, Focal Adhesions metabolism, Humans, Intracellular Signaling Peptides and Proteins metabolism, Myosin Light Chains metabolism, Podocytes cytology, Stress Fibers metabolism, Actomyosin metabolism, Calcium-Binding Proteins metabolism, Microfilament Proteins metabolism, Podocytes metabolism, Pseudopodia metabolism
- Abstract
Podocytes are highly-specialized epithelial cells essentially required for the generation and the maintenance of the kidney filtration barrier. This elementary function is directly based on an elaborated cytoskeletal apparatus establishing a complex network of primary and secondary processes. Here, we identify the actin-bundling protein allograft-inflammatory-inhibitor 1 like (AIF1L) as a selectively expressed podocyte protein in vivo. We describe the distinct subcellular localization of AIF1L to actin stress fibers, focal adhesion complexes and the nuclear compartment of podocytes in vitro. Genetic deletion of AIF1L in immortalized human podocytes resulted in an increased formation of filopodial extensions and decreased actomyosin contractility. By the use of SILAC based quantitative proteomics analysis we describe the podocyte specific AIF1L interactome and identify several components of the actomyosin machinery such as MYL9 and UNC45A as potential AIF1L interaction partners. Together, these findings indicate an involvement of AIF1L in the stabilization of podocyte morphology by titrating actomyosin contractility and membrane dynamics., Competing Interests: The authors have declared that no competing interests exist.
- Published
- 2018
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