Annexin II Light Chain p11 Interacts With ENaC to Increase Functional Activity at the Membrane

Frontiers in Physiology
Tanya T CheungSteven B Condliffe

Abstract

The epithelial Na+ channel (ENaC) provides for Na+ absorption in various types of epithelia including the kidney, lung, and colon where ENaC is localized to the apical membrane to enable Na+ entry into the cell. The degree of Na+ entry via ENaC largely depends on the number of active channels localized to the cell membrane, and is tightly controlled by interactions with ubiquitin ligases, kinases, and G-proteins. While regulation of ENaC endocytosis has been well-studied, relatively little is understood of the proteins that govern ENaC exocytosis. We hypothesized that the annexin II light chain, p11, could participate in the transport of ENaC along the exocytic pathway. Our results demonstrate that all three ENaC channel subunits interacted with p11 in an in vitro binding assay. Furthermore, p11 was able to immunoprecipitate ENaC in epithelial cells. Quantitative mass spectrometry of affinity-purified ENaC-p11 complexes recovered several other trafficking proteins including HSP-90 and annexin A6. We also report that p11 exhibits a robust protein expression in cortical collecting duct epithelial cells. However, the expression of p11 in these cells was not influenced by either short-term or long-term exposure to aldosterone. To d...Continue Reading

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Citations

May 31, 2020·Pflügers Archiv : European journal of physiology·Masumi InoueMasaki Kameyama
Oct 28, 2019·American Journal of Physiology. Renal Physiology·Adam W WareFiona J McDonald
Nov 17, 2020·Frontiers in Cell and Developmental Biology·Yayun Xu, Feihu Chen
May 19, 2020·Trends in Pharmacological Sciences·Ji-Seon Seo, Per Svenningsson

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Methods Mentioned

BETA
co-immunoprecipitation
transfection
pull-down
immunoprecipitation
PCR
ubiquitination

Software Mentioned

Prism
Proteome Discoverer
Acquire and Analyze
GraphPad
CFX Manager
Mascot

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