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

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Date
2011-01
Authors
Weinman, Edward J
Steplock, Deborah
Shenolikar, Shirish
Blanpied, Thomas A
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Abstract
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.
Type
Journal article
Subject
Kidney
Cell Line
Animals
Opossums
Multiprotein Complexes
Parathyroid Hormone
Sodium-Hydrogen Antiporter
Cytoskeletal Proteins
Phosphoproteins
Female
Sodium-Phosphate Cotransporter Proteins, Type IIa
Permalink
https://hdl.handle.net/10161/17232
Published Version (Please cite this version)
10.1152/ajprenal.00532.2010
Publication Info
Weinman, Edward J; Steplock, Deborah; Shenolikar, Shirish; & Blanpied, Thomas A (2011). Dynamics of PTH-induced disassembly of Npt2a/NHERF-1 complexes in living OK cells. American journal of physiology. Renal physiology, 300(1). pp. F231-F235. 10.1152/ajprenal.00532.2010. Retrieved from https://hdl.handle.net/10161/17232.
This is constructed from limited available data and may be imprecise. To cite this article, please review & use the official citation provided by the journal.
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Scholars@Duke

Shenolikar

Shirish Shenolikar

Professor Emeritus of Psychiatry and Behavioral Sciences
Protein phosphorylation controls a wide range of physiological processes in mammalian tissues. Phosphorylation state of cellular proteins is controlled by the opposing actions of protein kinases and phosphatases that are regulated by hormones, neurotransmitters, growth factors and other environmental cues. Our research attempts to understand the communication between protein kinases and phosphatases that dictates cellular protein phosphorylation and the cell's response to hormones. Over the
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