S100B-modulated Ca2+-dependent ROS-GC1 transduction machinery in the gustatory epithelium: a new mechanism in gustatory transduction |
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Authors: | Duda Teresa Sharma Rameshwar K |
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Institution: | The Unit of Regulatory and Molecular Biology, Department of Cell Biology, SOM & NJMS, University of Medicine and Dentistry of New Jersey, Stratford, NJ 08084, USA. dudatm@umdnj.edu |
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Abstract: | Gustatory transduction is a biochemical process by which the gustatory signal generates the electric signal. The microvilli of the taste cells in the gustatory epithelium are the sites of gustatory transduction. This study documents the biochemical, molecular, and functional identity of the Ca2+-modulated membrane guanylate cyclase transduction machinery in the bovine gustatory epithelium. The machinery is a two-component system: the Ca2+-sensor protein, S100B; and the transducer, ROS-GC1. S100B senses increments in free Ca2+, undergoes conformational change, binds to the domain amino acids (aa) Gly962-Asn981 and via the transduction domain aa Ile1030-Gln1041 activates ROS-GC1, generating the second messenger, cyclic GMP. In a recent study, operational presence of this machinery has been demonstrated in the photoreceptor bipolar synapse Duda et al., EMBO J. 21 (2002) 2547]. Thus, the machinery has a broader role in sensory perceptions, vision in the retinal neurons and gustation in the tongue. The entry of the ROS-GC transduction machinery defines the beginning of a new paradigm of Ca2+ signaling in the tongue. |
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Keywords: | Tongue S100B ROS-GC membrane guanylate cyclase Calcium signaling Taste |
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