Evolution and functional divergence of the anoctamin family of membrane proteins |
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| Authors: | Vladimir M Milenkovic Marisa Brockmann Heidi Stöhr Bernhard HF Weber Olaf Strauss |
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| Institution: | 1.Experimental Ophthalmology,Regensburg University Medical Center,Regensburg,Germany;2.Institute of Human Genetics,University of Regensburg,Regensburg,Germany |
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| Abstract: | Background The anoctamin family of transmembrane proteins are found in all eukaryotes and consists of 10 members in vertebrates. Ano1
and ano2 were observed to have Ca2+ activated Cl- channel activity. Recent findings however have revealed that ano6, and ano7 can also produce chloride currents, although
with different properties. In contrast, ano9 and ano10 suppress baseline Cl- conductance when co-expressed with ano1 thus suggesting that different anoctamins can interfere with each other. In order
to elucidate intrinsic functional diversity, and underlying evolutionary mechanism among anoctamins, we performed comprehensive
bioinformatics analysis of anoctamin gene family. |
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