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Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time
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Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time

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NAADP on target.

Robert Hooper1, Sandip Patel

  • 1Department of Cell and Developmental Biology, University College London, UK. r.hooper@ucl.ac.uk

Advances in Experimental Medicine and Biology
|March 29, 2012
PubMed
Summary
This summary is machine-generated.

Nicotinic acid adenine dinucleotide phosphate (NAADP) mobilizes intracellular calcium. Recent research identifies two-pore channels (TPCs) as the molecular targets of NAADP, likely located on acidic organelles.

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Area of Science:

  • Cell Biology
  • Ion Channel Physiology
  • Molecular Pharmacology

Background:

  • Nicotinic acid adenine dinucleotide phosphate (NAADP) is a key intracellular messenger regulating calcium (Ca2+) levels.
  • The precise molecular identity of NAADP-sensitive Ca2+ channels, particularly on acidic organelles, has been a long-standing question in cell signaling.

Purpose of the Study:

  • To identify the molecular targets of NAADP.
  • To characterize the function and localization of these novel ion channels.

Main Methods:

  • Biophysical analysis and site-directed mutagenesis were used to investigate TPCs.
  • Knockdown studies were performed to assess the physiological roles of TPCs.
  • Localization studies focused on the endo-lysosomal system.

Main Results:

  • Two-pore channels (TPCs) were identified as likely molecular targets for NAADP.
  • TPCs are located on the endo-lysosomal system and are sensitive to NAADP.
  • TPCs function as pore-forming subunits of NAADP-gated Ca2+ channels, coupled to ER Ca2+ channels.
  • TPCs regulate smooth muscle contraction, differentiation, and endothelial cell activation.

Conclusions:

  • TPCs are strongly indicated as the long-sought molecular targets of NAADP.
  • TPCs represent a novel class of ion channels crucial for cellular calcium signaling and various physiological processes.