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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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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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GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory...
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Feedback Regulation of Calcium Concentration01:27

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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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cAMP-dependent Protein Kinase Pathways01:25

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Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Many receptor binding ligands are hydrophilic; they do not cross the cell membrane but bind to cell-surface receptors. Thus, their message must be relayed by second messengers present in the cell cytoplasm. There are several second messenger pathways, each with its own way of relaying information. For example, the G protein-coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol pathway is active when the receptor induces...
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Updated: Apr 13, 2026

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

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SK channels and calmodulin.

John P Adelman1

  • 1a Vollum Institute ; Oregon Health & Science University ; Portland , OR USA.

Channels (Austin, Tex.)
|May 6, 2015
PubMed
Summary
This summary is machine-generated.

Calmodulin (CaM) acts as the calcium (Ca2+) gating cue for SK channels. This review details experiments showing CaM is an intrinsic SK channel subunit and a regulatory target.

Keywords:
Ca2+-gatingE-F handsParameciumSK channelcalmodulincuringintrinsic subunit

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • Calcium ions (Ca2+) are crucial intracellular signals regulating diverse physiological processes.
  • Intracellular Ca2+ levels are tightly controlled, with calmodulin (CaM) as a key Ca2+-binding protein.
  • CaM's structure includes E-F hand motifs enabling Ca2+ chelation and conformational flexibility.

Purpose of the Study:

  • To review the historical discovery of calmodulin's role in SK channel function.
  • To present experimental evidence establishing calmodulin as an intrinsic subunit of SK channels.
  • To highlight calmodulin as a regulatory target within the SK channel complex.

Main Methods:

  • Literature review of historical and contemporary research on Ca2+ signaling and ion channels.
  • Analysis of experimental data demonstrating the physical association between CaM and SK channels.
  • Examination of studies investigating the regulatory mechanisms involving CaM in SK channel activity.

Main Results:

  • Calmodulin (CaM) has been identified as the primary Ca2+-gating cue for Small-conductance (SK) channels.
  • Experimental evidence confirms that CaM is an integral subunit of the SK channel complex, not merely a peripheral modulator.
  • CaM itself is subject to regulatory modifications that influence SK channel gating and function.

Conclusions:

  • Calmodulin is essential for Ca2+-dependent regulation of SK channel activity.
  • The intrinsic nature of CaM within SK channels underscores its fundamental role in channel physiology.
  • Understanding CaM-SK channel interactions provides insights into cellular Ca2+ signaling pathways.