@article {1768,
	title = {The taste of carbonation.},
	journal = {Science},
	volume = {326},
	year = {2009},
	month = {2009 Oct 16},
	pages = {443-5},
	abstract = {<p>Carbonated beverages are commonly available and immensely popular, but little is known about the cellular and molecular mechanisms underlying the perception of carbonation in the mouth. In mammals, carbonation elicits both somatosensory and chemosensory responses, including activation of taste neurons. We have identified the cellular and molecular substrates for the taste of carbonation. By targeted genetic ablation and the silencing of synapses in defined populations of taste receptor cells, we demonstrated that the sour-sensing cells act as the taste sensors for carbonation, and showed that carbonic anhydrase 4, a glycosylphosphatidylinositol-anchored enzyme, functions as the principal CO2 taste sensor. Together, these studies reveal the basis of the taste of carbonation as well as the contribution of taste cells in the orosensory response to CO2.</p>
},
	keywords = {Action Potentials, Animals, Benzolamide, Bicarbonates, Calcium Channels, Carbon Dioxide, Carbonated Beverages, Carbonic Anhydrase Inhibitors, Carbonic Anhydrase IV, Carbonic Anhydrases, Cell Surface, Chorda Tympani Nerve, Gene Expression Profiling, Mice, Protons, Receptors, Taste, Taste Buds, Taste Perception, Transgenic},
	issn = {1095-9203},
	doi = {10.1126/science.1174601},
	author = {Chandrashekar, Jayaram and Yarmolinsky, David and von Buchholtz, Lars and Oka, Yuki and Sly, William and Ryba, Nicholas J P and Zuker, Charles S}
}
@article {1772,
	title = {Transforming the architecture of compound eyes.},
	journal = {Nature},
	volume = {443},
	year = {2006},
	month = {2006 Oct 12},
	pages = {696-9},
	abstract = {<p>Eyes differ markedly in the animal kingdom, and are an extreme example of the evolution of multiple anatomical solutions to light detection and image formation. A salient feature of all photoreceptor cells is the presence of a specialized compartment (disc outer segments in vertebrates, and microvillar rhabdomeres in insects), whose primary role is to accommodate the millions of light receptor molecules required for efficient photon collection. In insects, compound eyes can have very different inner architectures. Fruitflies and houseflies have an open rhabdom system, in which the seven rhabdomeres of each ommatidium are separated from each other and function as independent light guides. In contrast, bees and various mosquitoes and beetle species have a closed system, in which rhabdomeres within each ommatidium are fused to each other, thus sharing the same visual axis. To understand the transition between open and closed rhabdom systems, we isolated and characterized the role of Drosophila genes involved in rhabdomere assembly. Here we show that Spacemaker, a secreted protein expressed only in the eyes of insects with open rhabdom systems, acts together with Prominin and the cell adhesion molecule Chaoptin to choreograph the partitioning of rhabdomeres into an open system. Furthermore, the complete loss of spacemaker (spam) converts an open rhabdom system to a closed one, whereas its targeted expression to photoreceptors of a closed system markedly reorganizes the architecture of the compound eyes to resemble an open system. Our results provide a molecular atlas for the construction of microvillar assemblies and illustrate the critical effect of differences in a single structural protein in morphogenesis.</p>
},
	keywords = {Adhesiveness, Animals, Bees, Drosophila melanogaster, Drosophila Proteins, Eye, Eye Proteins, Membrane Glycoproteins, Molecular Sequence Data, Morphogenesis, Mutation},
	issn = {1476-4687},
	doi = {10.1038/nature05128},
	author = {Zelhof, Andrew C and Hardy, Robert W and Becker, Ann and Zuker, Charles S}
}
