AIF1L regulates actomyosin contractility and filopodial extensions in human podocytes
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AIF1L regulates actomyosin contractility and filopodial extensions in human podocytes. / Yasuda-Yamahara, Mako; Rogg, Manuel; Yamahara, Kosuke; Maier, Jasmin I; Huber, Tobias B; Schell, Christoph.
in: PLOS ONE, Jahrgang 13, Nr. 7, 2018, S. e0200487.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - AIF1L regulates actomyosin contractility and filopodial extensions in human podocytes
AU - Yasuda-Yamahara, Mako
AU - Rogg, Manuel
AU - Yamahara, Kosuke
AU - Maier, Jasmin I
AU - Huber, Tobias B
AU - Schell, Christoph
PY - 2018
Y1 - 2018
N2 - 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.
AB - 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.
KW - Actomyosin
KW - Calcium-Binding Proteins
KW - Cells, Cultured
KW - Focal Adhesions
KW - Humans
KW - Intracellular Signaling Peptides and Proteins
KW - Microfilament Proteins
KW - Myosin Light Chains
KW - Podocytes
KW - Pseudopodia
KW - Stress Fibers
KW - Journal Article
KW - Research Support, Non-U.S. Gov't
U2 - 10.1371/journal.pone.0200487
DO - 10.1371/journal.pone.0200487
M3 - SCORING: Journal article
C2 - 30001384
VL - 13
SP - e0200487
JO - PLOS ONE
JF - PLOS ONE
SN - 1932-6203
IS - 7
ER -
