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Papers In Press, published online ahead of print March 1, 2002
J. Biol. Chem, 10.1074/jbc.C200050200
Submitted on January 25, 2002
Revised on February 27, 2002
Accepted on March 1, 2002

Solution structure of the GABAA receptor associated protein GABARAP: Implications for biological function and its regulation

Thomas Stangler, Lorenz M. Mayr, and Dieter Willbold

IBI-2, Forschungszentrum Juelich, Juelich 52425

Corresponding Author: dieter.willbold{at}uni-duesseldorf.de

Control of neurotransmitter receptor expression and delivery to the postsynaptic membrane is of critical importance for neural signal transduction at synapses. The GABAA receptor associated protein GABARAP was reported to have an important role for movement and sorting of GABAA receptor molecules to the postsynaptic membrane. GABARAP not only binds to GABAA receptor gamma2-subunit, but also to tubulin, gephyrin and ULK1. We present for the first time the high resolution structure of human GABARAP determined by nuclear magnetic resonance in aqueous solution. One part of the molecule, despite being well ordered and rigid on a MHz time scale, exists in at least two different conformations that interchange to each other on a time scale slower than 25 Hz. An important feature of the solution structure is the observation that amino and carboxyl terminal ends of the protein directly interact with each other, which is not seen in recently reported crystal structures. The possible biological relevance of these observations for the regulation of GABARAP interactions and functions is discussed.


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