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TitleStructural basis of calmodulin modulation of the rod cyclic nucleotide-gated channel.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 120, Issue 15, Page e2300309120, Year 2023
Publish dateApr 11, 2023
AuthorsDiane C A Barret / Dina Schuster / Matthew J Rodrigues / Alexander Leitner / Paola Picotti / Gebhard F X Schertler / U Benjamin Kaupp / Volodymyr M Korkhov / Jacopo Marino /
PubMed AbstractCalmodulin (CaM) regulates many ion channels to control calcium entry into cells, and mutations that alter this interaction are linked to fatal diseases. The structural basis of CaM regulation ...Calmodulin (CaM) regulates many ion channels to control calcium entry into cells, and mutations that alter this interaction are linked to fatal diseases. The structural basis of CaM regulation remains largely unexplored. In retinal photoreceptors, CaM binds to the CNGB subunit of cyclic nucleotide-gated (CNG) channels and, thereby, adjusts the channel's Cyclic guanosine monophosphate (cGMP) sensitivity in response to changes in ambient light conditions. Here, we provide the structural characterization for CaM regulation of a CNG channel by using a combination of single-particle cryo-electron microscopy and structural proteomics. CaM connects the CNGA and CNGB subunits, resulting in structural changes both in the cytosolic and transmembrane regions of the channel. Cross-linking and limited proteolysis-coupled mass spectrometry mapped the conformational changes induced by CaM in vitro and in the native membrane. We propose that CaM is a constitutive subunit of the rod channel to ensure high sensitivity in dim light. Our mass spectrometry-based approach is generally relevant for studying the effect of CaM on ion channels in tissues of medical interest, where only minute quantities are available.
External linksProc Natl Acad Sci U S A / PubMed:37011209 / PubMed Central
MethodsEM (single particle)
Resolution2.76 - 4.66 Å
Structure data

16311

8bx7

EMDB-16311, PDB-8bx7:
Structure of the rod CNG channel bound to calmodulin
Method: EM (single particle) / Resolution: 2.76 Å

EMDB-16313: The structure of the rod CNG channel bound to calmodulin
Method: EM (single particle) / Resolution: 4.66 Å

Source
  • bos taurus (cattle)
KeywordsMEMBRANE PROTEIN / CNG channel / calmodulin / rod photoreceptor / vision

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