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Correction of Fig 7

Posted by SeungilRo on 25 Apr 2018 at 22:38 GMT

CORRECTION
Correction: Transcriptome of interstitial cells of Cajal reveals unique and selective gene signatures

Moon Young Lee☯, Se Eun Ha☯, Chanjae Park☯, Paul J. Park1, Robert Fuchs, Lai Wei,
Brian G. Jorgensen, Doug Redelman, Sean M. Ward, Kenton M. Sanders, Seungil Ro
☯ These authors contributed equally to this work.

There was an error in Fig 7B: A topological map of ANO1 variants. A topological map of ANO1 variants shows the pore region located at an extracellular loop between transmembrane domains TM5-6 in Fig 7B. The transmembrane domains and pore region of ANO1 were predicted and constructed based on information obtained from the UniProt [1], a transmembrane prediction database (PMpred) [2] and the model topology of ANO family proteins (ANO1-10) that consist of eight transmembrane domains and a pore located at an extracellular loop between TM5-6 [3]. However, a recent paper by Paulino C. et. al. [4] who characterized the transmembrane and pore regions of ANO1 revealed that the channel structure of ANO1 is different from the predicted topology of ANO family proteins: the pore region is largely shielded from the membrane in the cytoplasmic side between TM6-7 instead of an extracellular loop between TM5-6. This new structure of the channel was supported by the revised model of ANO1 topology that is proposed by Yu K. et. al. with evidence of the epitope accessibility and Ca2+-dependent gating properties of the channel in inside-out excised patches [5]. They also found that most programs (12 out of 14) using different algorithms predicting transmembranes in ANO1 couldn’t correctly predict all transmembrane domains. Therefore, we revised the topological map of ANO1 variants identified in this study based on the new structure of the channel [4].



Fig 7. Identification of ANO1 protein. (B) A topological map of ANO1 variants. Each circle denotes the corresponding amino acid. Colors on amino acid sequence show distinct regions and domains: red, missing or inserted peptides from differentially spliced exons; green, start codons found in differentially spliced variants. Alternatively starting methionines, insertion, or deletion in each ANO1 variant are indicated with variant IDs. Eight transmembrane domains TM1-8 and a pore region are shown. Voltage sensor (EEEEE) [6] and Ca2+ binding site (E-E) [5, 7] are also indicated.


Reference

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7. Tien J, Peters CJ, Wong XM, Cheng T, Jan YN, Jan LY, et al. A comprehensive search for calcium binding sites critical for TMEM16A calcium-activated chloride channel activity. eLife. 2014;3. doi: 10.7554/eLife.02772. PubMed PMID: 24980701; PubMed Central PMCID: PMC4112547.


No competing interests declared.