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Mannowetz, N.

Publications and source records attributed to Mannowetz, N..

2 recordsLinked to original sources

EFCAB9 is a pH-Dependent Ca2+ Sensor that Regulates CatSper Channel Activity and Sperm Motility

SummaryVarying pH of luminal fluid along the female reproductive tract is a physiological cue that modulates sperm motility. CatSper is a sperm-specific, pH-sensitive calcium channel essential for hyperactivated motility and male fertility. Multi-subunit CatSper channel complexes organize linear Ca2+ signaling nanodomains along the sperm tail. Here, we identify EF-hand calciumbinding domain-containing protein 9 (EFCAB9) as a dual function, cytoplasmic machine modulating the channel activity and the domain organization of CatSper. Knockout mice studies demonstrate that EFCAB9, in complex with the CatSper subunit, CAT SPER{zeta}, is essential for pH-dependent and Ca2+ sensitive activation of the CatSper channel. In the absence of EFCAB9, sperm motility and fertility is compromised and the linear arrangement of the Ca2+ signaling domains is disrupted. EFCAB9 interacts directly with CATSPER{zeta} in a Ca2+ dependent manner and dissociates at elevated pH.These observations suggest that EFCAB9 is a long-sought, intracellular, pH-dependent Ca2+ sensor that triggers changes in sperm motility.\n\nHighlightsO_LIEfcab9 encodes an evolutionarily conserved, sperm-specific EF-hand domain protein\nC_LIO_LIEfcab9-deficient mice have sperm motility defects and reduced male fertility\nC_LIO_LIEFCAB9 is a pH-tuned Ca2+ sensor for flagellar CatSper Ca2+ channel\nC_LIO_LIEFCAB9 is a dual function machine in gatekeeping and domain organization of CatSper\nC_LI

cell biology↗

Asymmetrically Positioned Flagellar Control Units Regulate Human Sperm Rotation

The ability of sperm to fertilize an egg is controlled by ion channels, one of which is the pH-dependent calcium channel of sperm CatSper. For CatSper to be fully activated, the cytoplasmic pH must be alkaline, which is accomplished by either proton transporters, or a faster mechanism, such as the voltage-gated proton channel Hv1. To ensure effective regulation, these channels and regulatory proteins must be tightly compartmentalized. Here, we characterize human sperm nanodomains that are comprised of Hv1, CatSper and regulatory protein ABHD2. Super-resolution microscopy revealed that Hv1 forms asymmetrically positioned bilaterally distributed longitudinal lines that span the entire length of the sperm tail. Such a distribution provides a direct structural basis for the selective activation of CatSper, and subsequent flagellar rotation along the long axis that, together with hyperactivated motility, enhances sperm fertility. Indeed, Hv1 inhibition leads to a decrease in sperm rotation. Thus, sperm ion channels are organized in distinct regulatory nanodomains that control hyperactivated motility and rotation.

cell biology↗