MAPK MODULES · 3D organization of yeast MAP-kinase modules
FP7 — People (Marie Curie Actions)
- Duration
- 2008-04-01 → 2012-03-31
- EU contribution
- €100,000
- Participants
- 1
- Scheme
- MC-IRG
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Results in brief
3D organization of yeast MAP-kinase modules
Four years after my relocation to Hungary, I managed to set up an independent lab mostly financed from international grants. The work in this lab is focusing on the molecular logic of natural signalling networks and I introduced a completely new line of research at the Department of Biochemistry in the most prestigious university of Hungary. I have also greatly developed the infrastructure required for structural biology projects at the hosting department. I have supervised four Master, six Bachelor students and there are currently four Doctor of Philosophy (PhD) students and a postdoctoral fellow working under my supervision. My habilitation defence is scheduled to take place this summer and I am hoping to obtain a tenured associate professor position at my host department starting in 2013.
Data: CORDIS, © European Union
Project objective
Eukaryotic cells contain myriad signaling pathways used to transmit information from the plasma membrane to the nucleus. Given the large number of pathways in a cell, how is it that a given stimulus leads to a precise response? This problem is particularly acute in kinase pathways, such as mitogen-activated protein kinase (MAPK) cascades, which often share common protein components. Over the last decade, however, a paradigm that has emerged is that signaling pathway specificity can be mediated, in part, by scaffolding proteins that bind pathway members and restrict them to act only on one another. In yeast, as well as in mammals, several scaffold proteins for MAP-kinase cascades have been identified. These scaffolds allow one or more common kinases to function in distinct signaling pathways without improper cross-talk. However, very little is known about the mechanism by which these scaffold molecules physically control transmission of signaling information. We therefore plan to determine the three-dimensional structures of MAP-kinase modules of the yeast mating and high osmolarity response pathways, which are organized by two non-related scaffold proteins: Ste5 and Pbs2. The components (four kinases and two scaffold proteins) will be expressed as recombinant proteins and the complex reconstituted in vitro. We will use a multifaceted approach with the following specific aims: (1) to determine the structure of the reconstituted Ste5 and Pbs2 scaffolded complex by X-ray crystallography or electron cryomicroscopy and (2) to identify well-ordered fragments of the scaffolds that interact with individual member kinases to determine the structure of informative sub-complexes by X-ray crystallography.
Original text from CORDIS.
Participants
- EOTVOS LORAND TUDOMANYEGYETEM · BudapestCoordinatorHungary
Links
Data: CORDIS, © European Union