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. 2004 Nov;124(5):527–540. doi: 10.1085/jgp.200409153

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Copyright © 2004, The Rockefeller University Press

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Figure 3. — Extracellular ATP induces phosphorylation and dephosphorylation of ciliary polypeptides in intact epithelial tissue. (A) Typical pattern of phosphorylated polypeptides in cilia isolated from epithelial tissue exposure to extracellular ATP (100 μM) for 3 min (lane 2) or 5 min (lane 3), as compared with untreated control (lane 1). Western blot analysis using anti-phosphoserine antibody indicates an increase in phosphorylation of 27, 37, and 44 kD polypeptides, and a decrease in phosphorylation of 35, 69, 100, and 130 kD polypeptides. (B) Reprobing of the nitrocellulose membrane presented in A with anti–α-tubulin antibody demonstrates equal protein loading. Representative blot of at least 10 similar experiments is shown. (C) Time course of extracellular ATP-dependent ciliary polypeptide phosphorylation. (D) Time course of extracellular ATP-dependent ciliary polypeptide dephosphorylation. Data represents a quantitative analysis of the magnitude of protein phosphorylation (C) and dephosphorylation (D) induced by extracellular ATP (100 μM). The optical density of protein bands on Western blots was measured, as described under materials and methods. The data indicate similar time dependences for the phosphorylation (C) of three major polypeptides (44, 37, and 27 kD) and dephosphorylation (D) of three additional polypeptides (130, 100, and 69 kD), which can be seen in A. The maximal phosphorylation and dephosphorylation effects were obtained at 1–5 min. Each point is the mean ± SEM of 4–10 experiments.