ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology

Anne-Laure Perraud, Andrea Fleig, Christopher A. Dunn, Leigh Ann Bagley, Pierre Launay, Carsten Schmitz, Alexander J. Stokes, Qiqin Zhu, Maurice J. Bessman, Reinhold Penner, Jean-Pierre Kinet and Andrew M. Scharenberg ()
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Anne-Laure Perraud: Beth Israel Deaconess Medical Center and Harvard Medical School
Andrea Fleig: Center for Biomedical Research at The Queen's Medical Center and John A. Burns School of Medicine at the University of Hawaii
Christopher A. Dunn: Johns Hopkins University
Leigh Ann Bagley: Center for Biomedical Research at The Queen's Medical Center and John A. Burns School of Medicine at the University of Hawaii
Pierre Launay: Beth Israel Deaconess Medical Center and Harvard Medical School
Carsten Schmitz: Beth Israel Deaconess Medical Center and Harvard Medical School
Alexander J. Stokes: Beth Israel Deaconess Medical Center and Harvard Medical School
Qiqin Zhu: Beth Israel Deaconess Medical Center and Harvard Medical School
Maurice J. Bessman: Johns Hopkins University
Reinhold Penner: Center for Biomedical Research at The Queen's Medical Center and John A. Burns School of Medicine at the University of Hawaii
Jean-Pierre Kinet: Beth Israel Deaconess Medical Center and Harvard Medical School
Andrew M. Scharenberg: Beth Israel Deaconess Medical Center and Harvard Medical School

Nature, 2001, vol. 411, issue 6837, 595-599

Abstract: Abstract Free ADP-ribose (ADPR), a product of NAD hydrolysis and a breakdown product of the calcium-release second messenger cyclic ADPR (cADPR), has no defined role as an intracellular signalling molecule in vertebrate systems. Here we show that a 350-amino-acid protein (designated NUDT9) and a homologous domain (NUDT9 homology domain) near the carboxy terminus of the LTRPC2/TrpC7 putative cation channel1 both function as specific ADPR pyrophosphatases. Whole-cell and single-channel analysis of HEK-293 cells expressing LTRPC2 show that LTRPC2 functions as a calcium-permeable cation channel that is specifically gated by free ADPR. The expression of native LTRPC2 transcripts is detectable in many tissues including the U937 monocyte cell line, in which ADPR induces large cation currents (designated IADPR) that closely match those mediated by recombinant LTRPC2. These results indicate that intracellular ADPR regulates calcium entry into cells that express LTRPC2.

Date: 2001
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DOI: 10.1038/35079100

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