Independent activation of distinct pores in dimeric TMEM16A channels.

doi:10.1085/jgp.201611651

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Article

Independent activation of distinct pores in dimeric TMEM16A channels.

The Journal of general physiology - 1 Nov 2016

Jeng Grace, Aggarwal Muskaan, Yu Wei-Ping, Chen Tsung-Yu

Abstract excerpt

The TMEM16 family encompasses Ca2+-activated Cl- channels (CaCCs) and lipid scramblases. These proteins are formed by two identical subunits, as confirmed by the recently solved crystal structure of a TMEM16 lipid scramblase. However, the high-resolution structure did not provide definitive information regarding the pore architecture of the TMEM16 channels. In this study, we express TMEM16A channels constituting...

Topics

Animals
Anoctamin-1
Binding Sites
Calcium
Chloride Channels
HEK293 Cells
Humans
Ion Channel Gating
Mice
Mutation
Protein Binding
Protein Subunits

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PMID: 27799319
DOI: 10.1085/jgp.201611651
PMCID: PMC5089935

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