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Minerva Stiftung: Home
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Minerva Centers
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* Wilhelm Kühne Minerva Center for Studies of Visual Transduction

Hebrew University of Jerusalem
(Established 1989)

Director

Prof. Baruch Minke
Dept. of Physiology
Hadassah Medical School
The Hebrew University of Jerusalem
P.O.Box 12272
Jerusalem 91120
Tel.: 00972-2-6758331
Fax: 00972-2-6439736
E-mail: minke@md.huji.ac.il
Internet: http://ard.huji.ac.il

Chairman of the Advisory Council

Prof. Dr. U. Benjamin Kaupp
IBI-1
Forschungszentrum Jülich
52428 Jülich
Tel.: 0049-2461-61-4041
Fax: 0049-2461-61-4216
E-mail: a.eckert@fz-juelich.de

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* Fields of research/Forschungsgebiete

Visual transduction, whereby light is translated into a neuronal signal that can be communicated to other neurons is the main topic of research. Particular emphasis is placed on genetic dissection of this process, using Drosophila visual mutants.
Hauptgebiet der Forschung ist die visuelle Transduktion, durch die in den Sehzellen der Lichtreiz in ein Nerven-Signal übersetzt wird, das anderen Neuronen mitgeteilt werden kann. Ein besonderer Schwerpunkt wird auf die genetische Zergliederung dieses Prozes-ses durch Verwendung von Drosophila-Mutanten mit visuellen Defekten gelegt.
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* Key Words

Transmembrane signaling, visual transduction, genetic dissection, phosphoinositide signaling, Ca2+ mobilization, retinal degeneration, electrophysiology of photoreceptors, biochemical analysis of visual mutants
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* Research activities and aims

Drosophila phototransduction is a prototype of Ca2+ mediated signaling, operating via the phosphoinositide cascade. Inositide signaling relies on an Insp3-induced Ca2+ release from internal stores and on Ca2+ entry which takes place when the stores become depleted of Ca2+ . This interplay between Ca2+ release and Ca2+ entry has been termed "capacitative Ca2+ entry" and the inward current "release activated current" (CRAC) to indicate gating of Ca2+ entry by Ca2+ store depletion. Our genetic molecular and functional studies indicate that the transient receptor potential mutant (trp) is the first putative "store-operated Ca2+ entry" - mutant and the TRP protein is an archetypal member of multigene family whose products share a structure that is highly conserved throughout evolution, from worms to humans.
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