Please use this identifier to cite or link to this item: https://doi.org/10.1152/ajprenal.00532.2010
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dc.titleDynamics of PTH-induced disassembly of Npt2a/NHERF-1 complexes in living OK cells
dc.contributor.authorWeinman, E.J.
dc.contributor.authorSteplock, D.
dc.contributor.authorShenolikar, S.
dc.contributor.authorBlanpied, T.A.
dc.date.accessioned2016-06-01T10:25:05Z
dc.date.available2016-06-01T10:25:05Z
dc.date.issued2011-01
dc.identifier.citationWeinman, E.J., Steplock, D., Shenolikar, S., Blanpied, T.A. (2011-01). Dynamics of PTH-induced disassembly of Npt2a/NHERF-1 complexes in living OK cells. American Journal of Physiology - Renal Physiology 300 (1) : F231-F235. ScholarBank@NUS Repository. https://doi.org/10.1152/ajprenal.00532.2010
dc.identifier.issn03636127
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/124659
dc.description.abstractParathyroid 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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1152/ajprenal.00532.2010
dc.sourceScopus
dc.subjectEzrin
dc.subjectProtein kinase C
dc.subjectRenal phosphate transport
dc.typeArticle
dc.contributor.departmentDUKE-NUS GRADUATE MEDICAL SCHOOL S'PORE
dc.description.doi10.1152/ajprenal.00532.2010
dc.description.sourcetitleAmerican Journal of Physiology - Renal Physiology
dc.description.volume300
dc.description.issue1
dc.description.pageF231-F235
dc.description.codenAJPPF
dc.identifier.isiut000285964000026
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