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001     557601
005     20240927190515.0
024 7 _ |a G:(GEPRIS)156346553
|d 156346553
035 _ _ |a G:(GEPRIS)156346553
040 _ _ |a GEPRIS
|c http://gepris.its.kfa-juelich.de
150 _ _ |a Identification and characterisation of Rab binding motifs in Golgi coiled-coil proteins
|y 2009 - 2012
371 _ _ |a Dr. Tobias H. Kloepper
450 _ _ |a DFG project G:(GEPRIS)156346553
|w d
|y 2009 - 2012
510 1 _ |a Deutsche Forschungsgemeinschaft
|0 I:(DE-588b)2007744-0
|b DFG
680 _ _ |a In eukaryotic cells the exchange of material between intracellular compartments is mediated by transport vesicles. While the formation and subsequent fusion of vesicles to an acceptor compartment is well understood comparatively little is known regarding how the target compartment is recognised. In recent years work in the Munro lab has focused on long coiled-coil proteins of the Golgi, and now uncovered several putative binding sites for multiple Rab G proteins within them, suggesting that the general function of Golgi coiled-coil proteins is to surround the Golgi in a meshwork which tethers Rab-coated structures to Golgi membranes. This research project aims to develop a prediction scheme that is capable of predicting which Rab proteins bind to specific coiled-coil motifs. The plan is to first unlock the evolutionary history ofthe Rab- and Golgi coiled-coil protein families within the eukaryotic kingdom and to establish a precise and sensitive classification scheme for these. This will serve as a basis for the prediction of conserved motifs within the Golgi coiled-coil protein families. The end goal is to predict possible Rab binding partners for the identified conserved motifs through advanced bioinformatical methods. Finally, basic biochemical methods will be used to verify these predictions.
909 C O |o oai:juser.fz-juelich.de:983444
|p authority:GRANT
|p authority
909 C O |o oai:juser.fz-juelich.de:983444
980 _ _ |a G
980 _ _ |a AUTHORITY

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