Thomas K Berger, David M. Fußhöller, Normann Goodwin, W. Bönigk, A. Müller, Nasim Dokani Khesroshahi, C. Brenker, D. Wachten, E. Krause, U. Kaupp, T. Strünker
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Post‐translational cleavage of Hv1 in human sperm tunes pH‐ and voltage‐dependent gating
In human sperm, proton flux across the membrane is controlled by the voltage‐gated proton channel Hv1. We show that sperm harbour both Hv1 and an N‐terminally cleaved isoform termed Hv1Sper. The pH‐control of Hv1Sper and Hv1 is distinctively different. Hv1Sper and Hv1 can form heterodimers that combine features of both constituents. Cleavage and heterodimerization of Hv1 might represent an adaptation to the specific requirements of pH control in sperm.
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