@article {1770,
	title = {Preserving cell shape under environmental stress.},
	journal = {Nature},
	volume = {452},
	year = {2008},
	month = {2008 Mar 20},
	pages = {361-4},
	abstract = {<p>Maintaining cell shape and tone is crucial for the function and survival of cells and tissues. Mechanotransduction relies on the transformation of minuscule mechanical forces into high-fidelity electrical responses. When mechanoreceptors are stimulated, mechanically sensitive cation channels open and produce an inward transduction current that depolarizes the cell. For this process to operate effectively, the transduction machinery has to retain integrity and remain unfailingly independent of environmental changes. This is particularly challenging for poikilothermic organisms, where changes in temperature in the environment may impact the function of mechanoreceptor neurons. Thus, we wondered how insects whose habitat might quickly vary over several tens of degrees of temperature manage to maintain highly effective mechanical senses. We screened for Drosophila mutants with defective mechanical responses at elevated ambient temperatures, and identified a gene, spam, whose role is to protect the mechanosensory organ from massive cellular deformation caused by heat-induced osmotic imbalance. Here we show that Spam protein forms an extracellular shield that guards mechanosensory neurons from environmental insult. Remarkably, heterologously expressed Spam protein also endowed other cells with superb defence against physically and chemically induced deformation. We studied the mechanical impact of Spam coating and show that spam-coated cells are up to ten times stiffer than uncoated controls. Together, these results help explain how poikilothermic organisms preserve the architecture of critical cells during environmental stress, and illustrate an elegant and simple solution to such challenge.</p>
},
	keywords = {Animals, Biological, Cell Line, Cell Shape, Cellular, Chemical, Drosophila melanogaster, Drosophila Proteins, Electrophysiology, Environment, Eye Proteins, Hot Temperature, Humidity, Mechanical, Mechanoreceptors, Mechanotransduction, Models, Osmotic Pressure, Stimulation, Stress},
	issn = {1476-4687},
	doi = {10.1038/nature06603},
	author = {Cook, Boaz and Hardy, Robert W and McConnaughey, William B and Zuker, Charles S}
}
@article {1777,
	title = {Coding of sweet, bitter, and umami tastes: different receptor cells sharing similar signaling pathways.},
	journal = {Cell},
	volume = {112},
	year = {2003},
	month = {2003 Feb 7},
	pages = {293-301},
	abstract = {<p>Mammals can taste a wide repertoire of chemosensory stimuli. Two unrelated families of receptors (T1Rs and T2Rs) mediate responses to sweet, amino acids, and bitter compounds. Here, we demonstrate that knockouts of TRPM5, a taste TRP ion channel, or PLCbeta2, a phospholipase C selectively expressed in taste tissue, abolish sweet, amino acid, and bitter taste reception, but do not impact sour or salty tastes. Therefore, despite relying on different receptors, sweet, amino acid, and bitter transduction converge on common signaling molecules. Using PLCbeta2 taste-blind animals, we then examined a fundamental question in taste perception: how taste modalities are encoded at the cellular level. Mice engineered to rescue PLCbeta2 function exclusively in bitter-receptor expressing cells respond normally to bitter tastants but do not taste sweet or amino acid stimuli. Thus, bitter is encoded independently of sweet and amino acids, and taste receptor cells are not broadly tuned across these modalities.</p>
},
	keywords = {Action Potentials, Afferent, Animals, Cell Membrane, Cell Surface, Cells, Citric Acid, Cultured, Female, Glutamic Acid, GTP-Binding Proteins, Isoenzymes, Knockout, Male, Membrane Proteins, Mice, Neurons, Phospholipase C beta, Quinine, Receptors, Sensory Receptor Cells, Signal Transduction, Sucrose, Taste, Taste Buds, TRPM Cation Channels, Type C Phospholipases},
	issn = {0092-8674},
	author = {Zhang, Yifeng and Hoon, Mark A and Chandrashekar, Jayaram and Mueller, Ken L and Cook, Boaz and Wu, Dianqing and Zuker, Charles S and Ryba, Nicholas J P}
}
