First Author | Tien J | Year | 2013 |
Journal | Proc Natl Acad Sci U S A | Volume | 110 |
Issue | 16 | Pages | 6352-7 |
PubMed ID | 23576756 | Mgi Jnum | J:196141 |
Mgi Id | MGI:5486597 | Doi | 10.1073/pnas.1303672110 |
Citation | Tien J, et al. (2013) Identification of a dimerization domain in the TMEM16A calcium-activated chloride channel (CaCC). Proc Natl Acad Sci U S A 110(16):6352-7 |
abstractText | 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. |