Review article about the rapid progress in the elucidation of the structure-function relationship of TRPM2

The transient receptor potential melastatin 2 (TRPM2) cation channel consists of a N-terminal channel domain and a C-terminal enzyme domain. It is activated by the cytosolic enriched second messenger ADP-ribose and is directly linked to oxidative stress-mediated apoptosis. The functional characterization of species variants as well as extensive structure function analysis lead to the recent discovery of a novel type of ADP-ribose binding pocket. Currently there is abundant data available, but in some cases the experimental results are contradictory. In a new review article of our group (, published in the International Journal of Molecular Sciences, the currently available experimental data on TRPM2 are summarized and evaluated. This should facilitate the development of future strategies in order to finally clarify structure-function relationships of this important ion channel.

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