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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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