Abstracts - Association for Chemoreception Sciences
Abstracts - Association for Chemoreception Sciences
Abstracts - Association for Chemoreception Sciences
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Oral <strong>Abstracts</strong><br />
#1 GIVAUDAN LECTURE:<br />
NON-MODEL MODELS IN OLFACTION<br />
#2 SYMPOSIUM: THE STRUCTURAL<br />
BASIS OF CHEMOSENSORY SIGNALING<br />
Bill S. Hansson<br />
Max Planck Institute <strong>for</strong> Chemical Ecology, Jena, Germany<br />
Our knowledge regarding olfactory structure and function has<br />
taken a quantum leap since the characterization of putative<br />
olfactory receptors both in vertebrates and insects. Still, the<br />
understanding of both ecological and evolutionary processes is<br />
lagging behind. What do different odors really mean to animals,<br />
and how has the system evolved to allow them to respond<br />
behaviorally in a relevant manner. To understand these topics<br />
better we use both a model insect (Drosophila melanogaster),<br />
and a number of non-model arthropods (moths, ants, primitive<br />
insects, land-living crustaceans).<br />
I will spend a short introductory part on recent progress in<br />
our work on drosophilid flies, touching on investigations of<br />
hard-wired smell-driven behavior. The rest of my talk I will<br />
devote to non-model arthropods.<br />
In the desert ant, Cataglyphis <strong>for</strong>tis, we have built on the classic<br />
investigations by the group of Rüdiger Wehner in Zürich. They<br />
demonstrated the amazing ability of these tiny insects to find<br />
their way home in a salt desert using vector-based orientation.<br />
In our investigations we show how the ants use odor cues to<br />
pinpoint their nest entrance, but how this orientation is, in a<br />
life-saving fashion, weighed against vector orientation. We also<br />
show how the ants use olfactory cues to find their main source<br />
of food; dead insects, in a highly efficient way, and how this<br />
smell-based food search is independent of the home vector.<br />
To investigate the evolution of arthropod olfactory systems<br />
we make use of both highly primitive, archeopteran insects<br />
(in comparison to their neopteran relatives), and of land-living<br />
crustaceans that have entered the terrestrial environment<br />
during the last five million years. Using a combination of<br />
transcriptomics, electrophysiology, morphology and bioassays<br />
we show that the neopteran divide coincides with a drastic<br />
development in the insect olfactory system, and that some<br />
land-living crustaceans have developed enormous central<br />
olfactory systems, while others seem to have abandoned<br />
olfaction.<br />
G protein coupling GPCRs: structural and functional<br />
insights into reciprocal G protein and GPCR interactions<br />
Roger K. Sunahara<br />
University of Michigan Medical School Ann Arbor, MI, USA<br />
Recent advances in the structural biology of G protein-coupled<br />
receptors have helped to unravel the intricacies of ligand binding.<br />
Similarly structural and biochemical analyses of heterotrimeric<br />
G proteins have affirmed our understanding of the mechanism<br />
underlying effector interactions and GTPase activity. The recent<br />
crystal structure of a prototypic GPCR, the beta 2<br />
-adrenergic<br />
receptor (beta 2<br />
AR), in a complex with the stimulatory G protein,<br />
Gs, trapped in its nucleotide-free state, has now provided models<br />
<strong>for</strong> activation of G proteins by GPCRs. These data have helped<br />
to delineate how hormone binding to GPCRs leads to GDP<br />
release on G proteins, the principle step that precedes GTP<br />
binding and G protein activation. The crystal structure, together<br />
with data from single particle reconstructions by electron<br />
microscopy and deuterium exchange mass spectrometry, reveal<br />
dramatic changes in the G protein alpha-subunit. The structural<br />
data also suggest that G proteins may allosterically regulate the<br />
receptor by stabilizing a closed con<strong>for</strong>mation on the extracellular<br />
face of the receptor. Radioligand binding analyses suggest<br />
that G protein coupling slows ligand dissociation, consistent<br />
with the observed structural changes in the extracellular face.<br />
Such structural changes account <strong>for</strong> the slower observed ligand<br />
dissociation rates and likely account <strong>for</strong> G protein-dependent<br />
high affinity agonist binding. Together these data support a<br />
plausible model <strong>for</strong> the mechanism <strong>for</strong> receptor-mediated<br />
nucleotide exchange, G protein activation and agonist binding.<br />
Acknowledgements: GM083118<br />
#3 SYMPOSIUM: THE STRUCTURAL<br />
BASIS OF CHEMOSENSORY SIGNALING<br />
Structural Determinants of TRPV Channel Activation<br />
and Desensitization<br />
Rachelle Gaudet<br />
Harvard University Cambridge, MA, USA<br />
ORAL ABSTRACTS<br />
My lab is broadly interested in the mechanisms of signaling<br />
and transport across cellular membranes. Much of our research<br />
centers on TRP channels and their role in sensory perception.<br />
We focus on temperature-sensitive ion channels, particularly<br />
TRPV1 and TRPA1. TRP channels are challenging structural<br />
biology targets because they are large multidomain eukaryotic<br />
membrane proteins and are not naturally abundant. We<br />
take complementary approaches to obtain structural and<br />
functional in<strong>for</strong>mation on TRP channels. One strategy is to<br />
divide and conquer: determine crystal structures of isolated<br />
domains of TRP channels. The results can then combined with<br />
<strong>Abstracts</strong> are printed as submitted by the author(s).<br />
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