Ligand-induced activation of human TRPM2 requires the terminal ribose of ADPR and involves Arg1433 and Tyr1349

• Published in: Biochemical journal Vol. 474; no. 13; p. 2159
• Main Authors: Fliegert, Ralf, Watt, Joanna M, Schöbel, Anja, Rozewitz, Monika D, Moreau, Christelle, Kirchberger, Tanja, Thomas, Mark P, Sick, Wiebke, Araujo, Andrea C, Harneit, Angelika, Potter, Barry V L, Guse, Andreas H
• Format: Journal Article
• Language: English
• Published: England 16.06.2017
• Subjects: Adenosine Diphosphate Ribose - chemistry; Adenosine Diphosphate Ribose - genetics; Adenosine Diphosphate Ribose - metabolism; Amino Acid Sequence; Arginine - chemistry; Arginine - genetics; Arginine - metabolism; Calcium - metabolism; Calcium Signaling; HEK293 Cells; Humans; Ion Channel Gating; Mutagenesis, Site-Directed; Mutation - genetics; Patch-Clamp Techniques; Protein Binding; Protein Conformation; Pyrophosphatases - metabolism; Sequence Homology, Amino Acid; TRPM Cation Channels - chemistry; TRPM Cation Channels - genetics; TRPM Cation Channels - metabolism; Tyrosine - chemistry; Tyrosine - genetics; Tyrosine - metabolism; protein structure; adenosine diphosphate ribose; transient receptor potential channels

TRPM2 (transient receptor potential channel, subfamily melastatin, member 2) is a Ca -permeable non-selective cation channel activated by the binding of adenosine 5'-diphosphoribose (ADPR) to its cytoplasmic NUDT9H domain (NUDT9 homology domain). Activation of TRPM2 by ADPR downstream of oxidat...