Forschungs- & Entwicklungsinformationsdienst der Gemeinschaft - CORDIS

FP6

ACTIN CYTOSKELETON Berichtzusammenfassung

Project ID: 510554
Gefördert unter: FP6-MOBILITY
Land: Hungary

Final Activity Report Summary - ACTIN CYTOSKELETON (Actin cytoskeleton and cell signalling)

The major aims of this project were to provide financial support for young researchers reintegrating to their home country. In accordance with this aim, a substantial part of the support was spent establishing the appropriate environment for my group to carry out the research activities outlined in my proposal. These investments involved the purchase of chemicals, pipettes, plastic and glass wear, fluorescence and phophorescence cuvettes and numerous other consumables which are essential for the investigations. These investments greatly enhanced the available lab facilities, increased the efficiency of my group, and provided the essential conditions for the initiation of research activity after my return to Pécs from England.

Scientific results due to the effective reintegration of the actin cytoskeleton group could start the research activities with relatively short delay. The studies involved in this period were of two kinds, studies in collaboration with international research groups (from Germany, England, Finland) and investigations by the group with no collaborations. In collaboration with Professor Alfred Wittinghofer's research group we determined the three dimensional structure of an fh2 formin fragment from a mammalian (mouse) source. The structure of the mdia1-fh2 was resolved and interpreted in the light of the biochemical results obtained in this project. This work appeared in Molecular Cell (2004, 565(1-3); 163) and was the first formin structure published. In the investigation of motor proteins we described the function and kinetic behaviour of single and double headed kinesins. The results were published in 2004. As a result of the initiation of the work in Hungary, a new project investigated the interactions between cyclic toxic hexapeptides phalloidin and jasplakinolide- with actin filaments. The observation clearly showed that both drugs have a substantial effect on the conformation of actin filaments, and the effect of jasplakinolide proved to be stronger than that of phalloidin. Our data also demonstrated that there are long range allosteric interactions along he actin filaments, suggesting that these interactions can play important role in vivo as information channels. The results were published in two articles.

Kontakt

Gabor HILD
Tel.: +36-7253-6267
Fax: +36-7225-36261
E-Mail-Adresse
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