Roger Goody

Roger Goody

Emeritus Group, Physical Biochemistry

Research Interests

We have continued our studies of Rab proteins and their role in intracellular vesicular transport and have also dealt with some more general aspects of GTPases, in particular with respect to development of methods to modulate their function and to identify important partner molecules. Several of the studies of the last few years have been directed at understanding the mechanism of targeting of Rab proteins to specific membranes.

Selected Publications

PubMed Liste>

Rai A, Singh AK, Bleimling N, Posern G, Vetter IR, Goody RS (2022). Rep15 interacts with several Rab GTPases and has a distinct fold for a Rab effector. Nat Commun.

Rai A, Bleimling N, Vetter IR, Goody RS (2020). The mechanism of activation of the actin binding protein EHBP1 by Rab8 family members. Nat Commun

Rai A, Oprisko A, Campos J, Fu Y, Friese T, Itzen A, Goody RS, Gazdag EM, Müller MP (2016). bMERB domains are bivalent Rab8 effectors evolved by gene duplication.eLife 2016;5:e18675

Wiegandt D, Vieweg S, Hofmann F, Koch D, Li F, Wu YW, Itzen A, Muller MP, and Goody RS (2015). Locking GTPases covalently in their functional states.Nature communications 6, 7773.
doi: 10.1038/ncomms8773 .

Gazdag EM, Streller A, Haneburger I, Hilbi H, Vetter IR, Goody RS, and Itzen A (2013). Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB. Embo Rep 14, 199-205.
doi: 10.1038/embor.2012.211

Blumer J, Rey J, Dehmelt L, Mazel T, Wu YW, Bastiaens P, Goody RS, and Itzen A (2013). RabGEFs are a major determinant for specific Rab membrane targeting. J Cell Biol 200, 287-300.

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