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April 19, 2017Journal of Biological ChemistryOpen Access

Modulation of TMEM16A channel activity by the von Willebrand factor type A (VWA) domain of the calcium-activated chloride channel regulator 1 (CLCA1)

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Key result

The von Willebrand factor type A (VWA) domain of CLCA1 is necessary and sufficient to increase TMEM16A protein levels at the cell surface and activate TMEM16A-like currents in HEK293T cells.

Population

HEK293T cells

Design

Preclinical

Authors

MSMonica Sala‐RabanalWashington University in St. LouisZYZeynep YurtseverWashington University in St. LouisKBKayla N. BerryWashington University in St. Louis

Discussion

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Implication

May inform TMEM16A-targeted cystic fibrosis therapies; leaves open translation from cell models to in vivo or clinical use.

Structured PICO

P
Population
HEK293T cells
I
Intervention
Transfection with CLCA1 constructs containing the von Willebrand factor type A (VWA) domain or exposure to secreted VWA domain alone
O
Outcome
TMEM16A protein levels on the cell surface and TMEM16A-like currentssurrogate

The VWA domain of CLCA1 selectively activates TMEM16A chloride channels by stabilizing them at the cell surface, highlighting a potential therapeutic mechanism for cystic fibrosis.

Cite This Study

Sala‐Rabanal et al. (2017) studied this question. CLCA1 VWA domain was evaluated on TMEM16A channel activity and cell surface protein levels. The von Willebrand factor type A (VWA) domain of CLCA1 is necessary and sufficient to increase TMEM16A protein levels at the cell surface and activate TMEM16A-like currents in HEK293T cells.

synapsesocial.com/papers/6a9e9e3bfbeca46cb71cd394https://doi.org/10.1074/jbc.m117.788232
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Also Consider

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