Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Weinman, E.J. et al.

Edward J. Weinman, Deborah Steplock, Shirish Shenolikar, Thomas A. Blanpied,

Dynamics of PTH-induced disassembly of Npt2a/NHERF-1 complexes in living OK cells.

Parathyroid hormone (PTH) inhibits the reabsorption of phosphate in the renal proximal tubule by disrupting the binding of the sodium-dependent phosphate transporter 2A (Npt2a) to the adapter protein sodium-hydrogen exchanger regulatory factor-1 (NHERF-1), a process initiated by activation of protein kinase C (PKC). To gain additional insights into the dynamic sequence of events, the time course of these responses was studied in living opossum kidney (OK) cells. Using a FRET-based biosensor, we found that PTH activated intracellular PKC within seconds to minutes. In cells expressing GFP-Npt2a and mCherry-NHERF, PTH did not affect the relative abundance of NHERF-1 but there was a significant and time-dependent decrease in the Npt2a/NHERF-1 ratio. The half-time to maximal dissociation was 15 to 20 min. By contrast, PTH had no effect on the fluorescence ratio for GFP-ezrin compared with mCherry-NHERF-1 at the apical surface. These experiments establish that PTH treatment of proximal tubule OK cells leads to rapid activation of PKC with the subsequent dissociation of Npt2a/NHERF-1 complexes. The association of NHERF-1 with Ezrin and their localization at the apical membrane, however, was unperturbed by PTH, thereby enabling the rapid recruitment and membrane reinsertion of Npt2a and other NHERF-1 targets on termination of the hormone response.[1]

References

Dynamics of PTH-induced disassembly of Npt2a/NHERF-1 complexes in living OK cells. Weinman, E.J., Steplock, D., Shenolikar, S., Blanpied, T.A. Am. J. Physiol. Renal Physiol. (2011) [Pubmed]

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