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Pichlo, M.* ; Bungert-Plümke, S.* ; Weyand, I.* ; Seifert, R.* ; Bönigk, W.* ; Strünker, T.* ; Kashikar, N.D.* ; Goodwin, N.* ; Müller, A.* ; Pelzer, P.* ; Van, Q.* ; Enderlein, J.* ; Klemm, C.* ; Krause, E.* ; Trötschel, C.* ; Poetsch, A.* ; Kremmer, E. ; Kaupp, U.B.*

High density and ligand affinity confer ultrasensitive signal detection by a guanylyl cyclase chemoreceptor.

J. Cell Biol. 206, 541-557 (2014)
Verlagsversion DOI PMC
Free by publisher
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
Guanylyl cyclases (GCs), which synthesize the messenger cyclic guanosine 3',5'-monophosphate, control several sensory functions, such as phototransduction, chemosensation, and thermosensation, in many species from worms to mammals. The GC chemoreceptor in sea urchin sperm can decode chemoattractant concentrations with single-molecule sensitivity. The molecular and cellular underpinnings of such ultrasensitivity are not known for any eukaryotic chemoreceptor. In this paper, we show that an exquisitely high density of 3 × 10(5) GC chemoreceptors and subnanomolar ligand affinity provide a high ligand-capture efficacy and render sperm perfect absorbers. The GC activity is terminated within 150 ms by dephosphorylation steps of the receptor, which provides a means for precise control of the GC lifetime and which reduces "molecule noise." Compared with other ultrasensitive sensory systems, the 10-fold signal amplification by the GC receptor is surprisingly low. The hallmarks of this signaling mechanism provide a blueprint for chemical sensing in small compartments, such as olfactory cilia, insect antennae, or even synaptic boutons.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Natriuretic-peptide Receptor; Nucleotide-gated Channels; Sea-urchin Sperm; Single-photon Responses; Kinase Homology Domain; De-novo Peptide; Phosphorylation Sites; Structure Prediction; Corynebacterium-glutamicum; Caenorhabditis-elegans
ISSN (print) / ISBN 0021-9525
e-ISSN 1540-8140
Zeitschrift Journal of Cell Biology, The
Quellenangaben Band: 206, Heft: 4, Seiten: 541-557 Artikelnummer: , Supplement: ,
Verlag Rockefeller University Press
Verlagsort New York
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Molecular Immunology (IMI)