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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...
Intracellular Signaling Cascades01:24

Intracellular Signaling Cascades

Once a ligand binds to a receptor, the signal is transmitted through the membrane and into the cytoplasm. The continuation of a signal in this manner is called signal transduction. Signal transduction only occurs with cell-surface receptors, which cannot interact with most components of the cell, such as DNA. Only internal receptors can interact directly with DNA in the nucleus to initiate protein synthesis. When a ligand binds to its receptor, conformational changes occur that affect the...
Intracellular Signaling Cascades01:24

Intracellular Signaling Cascades

Once a ligand binds to a receptor, the signal is transmitted through the membrane and into the cytoplasm. The continuation of a signal in this manner is called signal transduction. Signal transduction only occurs with cell-surface receptors, which cannot interact with most components of the cell, such as DNA. Only internal receptors can interact directly with DNA in the nucleus to initiate protein synthesis. When a ligand binds to its receptor, conformational changes occur that affect the...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Amplifying Signals via Second Messengers01:15

Amplifying Signals via Second Messengers

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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Dissection of Local Ca2+ Signals in Cultured Cells by Membrane-targeted Ca2+ Indicators
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Dissection of Local Ca2+ Signals in Cultured Cells by Membrane-targeted Ca2+ Indicators

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The CBL-CIPK Ca(2+)-decoding signaling network: function and perspectives.

Stefan Weinl1, Jörg Kudla1

  • 1Universität Münster, Institut für Botanik und Botanischer Garten, Schlossplatz 4, 48149 Münster, Germany.

The New Phytologist
|October 28, 2009
PubMed
Summary
This summary is machine-generated.

Plant calcium sensors, calcineurin B-like (CBL) proteins, and their interacting kinases (CIPKs) form crucial networks for adaptation. This review explores their evolution and function in signal processing.

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Area of Science:

  • Plant molecular biology and signaling
  • Calcium-mediated signal transduction pathways

Background:

  • Calcium ions act as essential messengers in plant development and adaptation.
  • Calcineurin B-like (CBL) proteins are key calcium sensors that interact with CBL-interacting protein kinases (CIPKs).

Purpose of the Study:

  • To review novel findings on the evolution of the CBL-CIPK signaling network.
  • To provide insights into the physiological functions of CBL-CIPK complexes in plants.
  • To discuss emerging principles of information processing within this signaling system.

Main Methods:

  • Literature review of recent research on CBL and CIPK proteins.
  • Analysis of evolutionary trends in CBL-CIPK network formation.
  • Synthesis of current understanding of CBL-CIPK complex functions.

Main Results:

  • The CBL-CIPK network enables flexible and specific signal-response coupling in plants.
  • Evolutionary studies reveal the intricate development of this signaling system.
  • Key physiological roles of CBL-CIPK complexes in environmental adaptation are highlighted.

Conclusions:

  • The CBL-CIPK signaling network is fundamental for plant adaptation and development.
  • Understanding the evolution and function of CBL-CIPK complexes offers insights into plant resilience.
  • Emerging principles governing information processing in this network are crucial for future research.