Reference : Angiotensin II regulates phosphorylation of actin-associated proteins in human podocytes
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Angiotensin II regulates phosphorylation of actin-associated proteins in human podocytes
Schenk, Laura K []
Möller-Kerutt, Annika []
Klosowski, Rafael []
Wolters, Dirk []
Schaffner, Elisabeth mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >]
Weide, Thomas []
Pavenstädt, Hermann []
Vollenbröker, Beate mailto [Medizinische Klinik und Poliklinik D, Albert Schweitzer Campus 1, A14, D-48149 Münster, Germany.]
FASEB Journal
Federation of American Society for Experimental Biology
Yes (verified by ORBilu)
[en] kidney ; L-plastin ; actin turnover
[en] Within the kidney, angiotensin II (AngII) targets different cell types in the vasculature, tubuli, and glomeruli. An important part of the renal filtration barrier is composed of podocytes with their actin-rich foot processes. In this study, we used stable isotope labeling with amino acids in cell culture coupled to mass spectrometry to characterize relative changes in the phosphoproteome of human podocytes in response to short-term treatment with AngII. In 4 replicates, we identified a total of 17,956 peptides that were traceable to 2081 distinct proteins. Bioinformatic analyses revealed that among the increasingly phosphorylated peptides are predominantly peptides that are related to actin filaments, cytoskeleton, lamellipodia, mammalian target of rapamycin, and MAPK signaling. Among others, this screening approach highlighted the increased phosphorylation of actin-bundling protein, L-plastin (LCP1). AngII-dependent phosphorylation of LCP1 in cultured podocytes was mediated by the kinases ERK, p90 ribosomal S6 kinase, PKA, or PKC. LCP1 phosphorylation increased filopodia formation. In
addition, treatmentwith AngII led to LCP1 redistribution to the cell margins,membrane ruffling, and formation of lamellipodia. Our data highlight the importance of AngII-triggered actin cytoskeleton-associated signal transduction in podocytes.
Researchers ; Professionals ; Students

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