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Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
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Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
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Most plants use the C3 pathway for carbon fixation. However, some plants, such as sugar cane, corn, and cacti that grow in hot conditions, use alternative pathways to fix carbon and conserve energy loss due to photorespiration. Photorespiration is the process that occurs when the oxygen concentration is high. Under such conditions, the rubisco enzyme in the Calvin cycle binds O2 instead of CO2, which halts photosynthesis and consumes energy.
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Ca2+ Release Channels Join the 'Resolution Revolution'.

Ran Zalk1, Andrew R Marks2

  • 1The National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev, Beer Sheva 84105, Israel.

Trends in Biochemical Sciences
|May 14, 2017
PubMed
Summary
This summary is machine-generated.

Ryanodine receptors (RyRs) are crucial calcium channels. Recent cryo-EM structures reveal their architecture, gating, and disease-related mutations, offering therapeutic insights.

Keywords:
calcium channelcryo-EMexcitation–contraction couplingryanodine receptorsstructure

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Structural Biology

Background:

  • Ryanodine receptors (RyRs) are calcium release channels critical for muscle contraction and cellular signaling.
  • Dysfunctional Ca2+ handling via RyRs contributes to various diseases, including heart failure, myopathies, Alzheimer's, and diabetes.
  • Understanding RyR structure and function is vital for developing targeted therapies.

Purpose of the Study:

  • To elucidate the structural basis of RyR1 channel function and gating mechanisms.
  • To provide high-resolution structural insights into disease-associated RyR mutations.
  • To advance the development of therapeutic strategies targeting RyRs.

Main Methods:

  • Mammalian RyR1 cryoelectron microscopy (cryo-EM) was employed to determine structures in multiple functional states.
  • Analysis of high-resolution structures to understand domain organization and ligand interactions.
  • Mapping of disease-causing mutations onto structural models.

Main Results:

  • Detailed architecture of the transmembrane pore and cytoplasmic domains of RyR1 has been resolved.
  • The location and structure of the channel gate and ligand-binding sites are clarified.
  • Structural effects of disease-associated mutations on RyR1 function are elucidated.

Conclusions:

  • Recent cryo-EM structures provide unprecedented insights into RyR1 architecture and gating.
  • This structural information is key to understanding disease mechanisms and identifying therapeutic targets.
  • Further structural studies will enable the development of novel treatments for RyR-related disorders.