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Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6352-7. doi: 10.1073/pnas.1303672110. Epub 2013 Apr 1.

Identification of a dimerization domain in the TMEM16A calcium-activated chloride channel (CaCC).

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Department of Physiology, and Howard Hughes Medical Institute, University of California, San Francisco, CA 94158, USA.


Transmembrane proteins with unknown function 16 (TMEM16A) is a calcium-activated chloride channel (CaCC) important for neuronal, exocrine, and smooth muscle functions. TMEM16A belongs to a family of integral membrane proteins that includes another CaCC, TMEM16B, responsible for controlling action potential waveform and synaptic efficacy, and a small-conductance calcium-activated nonselective cation channel, TMEM16F, linked to Scott syndrome. We find that these channels in the TMEM16 family share a homodimeric architecture facilitated by their cytoplasmic N termini. This dimerization domain is important for channel assembly in eukaryotic cells, and the in vitro association of peptides containing the dimerization domain is consistent with a homotypic protein-protein interaction. Amino acid substitutions in the dimerization domain affect functional TMEM16A-CaCC channel expression, as expected from its critical role in channel subunit assembly.

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