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Absolute proteomic quantification reveals design principles of sperm flagellar chemosensation.

MPS-Authors

Hamzeh,  Hussein
Department of Molecular Sensory Systems, Center of Advanced European Studies and Research (caesar), Max Planck Society;
External Organizations;

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Alvarez,  Luis
Department of Molecular Sensory Systems, Center of Advanced European Studies and Research (caesar), Max Planck Society;

Pascal,  René
Department of Molecular Sensory Systems, Center of Advanced European Studies and Research (caesar), Max Planck Society;

Lavryk,  Fedir
Department of Molecular Sensory Systems, Center of Advanced European Studies and Research (caesar), Max Planck Society;

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Bönigk,  Wolfgang
Department of Molecular Sensory Systems, Center of Advanced European Studies and Research (caesar), Max Planck Society;

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Körschen,  Heinz Gerd
Department of Molecular Sensory Systems, Center of Advanced European Studies and Research (caesar), Max Planck Society;

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Müller,  Astrid
Department of Molecular Sensory Systems, Center of Advanced European Studies and Research (caesar), Max Planck Society;

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Rennhack,  Andreas
Department of Molecular Sensory Systems, Center of Advanced European Studies and Research (caesar), Max Planck Society;

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Strünker,  Timo
Department of Molecular Sensory Systems, Center of Advanced European Studies and Research (caesar), Max Planck Society;
External Organizations;

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Seifert,  Reinhard
Department of Molecular Sensory Systems, Center of Advanced European Studies and Research (caesar), Max Planck Society;
External Organizations;

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Kaupp,  Ulrich Benjamin
Department of Molecular Sensory Systems, Center of Advanced European Studies and Research (caesar), Max Planck Society;
External Organizations;

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Citation

Trötschel, C., Hamzeh, H., Alvarez, L., Pascal, R., Lavryk, F., Bönigk, W., et al. (2020). Absolute proteomic quantification reveals design principles of sperm flagellar chemosensation. EMBO Journal, 39: e102723. doi:10.15252/embj.2019102723.


Cite as: http://hdl.handle.net/21.11116/0000-0005-6FBB-D
Abstract
Cilia serve as cellular antennae that translate sensory information into physiological responses. In the sperm flagellum, a single chemoattractant molecule can trigger a Ca2+ rise that controls motility. The mechanisms underlying such ultra-sensitivity are ill-defined. Here, we determine by mass spectrometry the copy number of nineteen chemosensory signaling proteins in sperm flagella from the sea urchin Arbacia punctulata. Proteins are up to 1,000-fold more abundant than the free cellular messengers cAMP, cGMP, H+ , and Ca2+ . Opto-chemical techniques show that high protein concentrations kinetically compartmentalize the flagellum: Within milliseconds, cGMP is relayed from the receptor guanylate cyclase to a cGMP-gated channel that serves as a perfect chemo-electrical transducer. cGMP is rapidly hydrolyzed, possibly via "substrate channeling" from the channel to the phosphodiesterase PDE5. The channel/PDE5 tandem encodes cGMP turnover rates rather than concentrations. The rate-detection mechanism allows continuous stimulus sampling over a wide dynamic range. The textbook notion of signal amplification-few enzyme molecules process many messenger molecules-does not hold for sperm flagella. Instead, high protein concentrations ascertain messenger detection. Similar mechanisms may occur in other small compartments like primary cilia or dendritic spines.