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Structural insight into TRPV5 channel function and modulation.

Shangyu Dang1, Mark K van Goor1,2, Daniel Asarnow1

  • 1Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143.

Proceedings of the National Academy of Sciences of the United States of America
|April 13, 2019
PubMed
Summary
This summary is machine-generated.

Transient receptor potential vanilloid 5 (TRPV5) channels regulate calcium. New structures reveal how calcium and calmodulin (CaM) control TRPV5 activity, showing flexible CaM binding.

Keywords:
TRP channelcalciumcalmodulincryo-EM

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Area of Science:

  • Biophysics
  • Structural Biology
  • Molecular Physiology

Background:

  • Transient receptor potential vanilloid 5 (TRPV5) is a calcium-selective ion channel crucial for calcium homeostasis.
  • Unlike other TRPV channels, TRPV5 is constitutively open and regulated by calcium-dependent calmodulin (CaM) binding, not temperature or ligands.

Purpose of the Study:

  • To elucidate the structural mechanisms underlying calcium-dependent regulation of TRPV5.
  • To investigate the interaction between TRPV5 and calmodulin (CaM) at high resolution.

Main Methods:

  • High-resolution electron cryomicroscopy (cryo-EM) was used to determine structures.
  • Structures were obtained for truncated and full-length TRPV5, a W583A mutant, and TRPV5 complexed with CaM, all within lipid nanodiscs.

Main Results:

  • The study presents high-resolution cryo-EM structures of TRPV5 in various states, including with CaM.
  • These structures reveal the molecular details of how calcium binding modulates TRPV5 channel activity via CaM.
  • A flexible stoichiometry of CaM binding to TRPV5 was observed.

Conclusions:

  • The determined structures provide unprecedented insight into the calcium-sensing mechanism of TRPV5.
  • Understanding TRPV5 regulation is key for calcium homeostasis and related physiological processes.