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Related Concept Videos

Insulin: The Receptor and Signaling Pathways01:28

Insulin: The Receptor and Signaling Pathways

Insulin action is mediated through a receptor tyrosine kinase, akin to the IGF-1 receptor. The number of receptors per cell varies significantly, from 40 on erythrocytes to 300,000 on adipocytes and hepatocytes. The insulin receptor consists of linked α/β subunit dimers, forming a heterotetramer glycoprotein with two extracellular α subunits and two β subunits spanning the membrane. The α subunits inhibit the inherent tyrosine kinase activity of the β subunits, but this inhibition is released...
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
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...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
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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Related Experiment Video

Updated: Jul 6, 2026

Studying the Hypothalamic Insulin Signal to Peripheral Glucose Intolerance with a Continuous Drug Infusion System into the Mouse Brain
08:32

Studying the Hypothalamic Insulin Signal to Peripheral Glucose Intolerance with a Continuous Drug Infusion System into the Mouse Brain

Published on: January 4, 2018

Insulin signal transduction pathways.

M J Quon1, A J Butte, S I Taylor

  • 1Diabetes Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

Trends in Endocrinology and Metabolism: TEM
|November 1, 1994
PubMed
Summary
This summary is machine-generated.

Insulin signaling activates the insulin receptor tyrosine kinase, initiating pathways that regulate cellular functions. Understanding these insulin receptor pathways and src homology 2 (SH2) domain interactions is key to cellular regulation.

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Glucose Uptake Measurement and Response to Insulin Stimulation in In Vitro Cultured Human Primary Myotubes
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Signaling

Background:

  • Insulin elicits diverse cellular effects by activating its receptor.
  • Insulin receptor activation involves tyrosine kinase activity and protein phosphorylation.
  • Src homology 2 (SH2) domains are critical for mediating intracellular signaling pathways.

Purpose of the Study:

  • To review recent advancements in understanding insulin signaling pathways.
  • To elucidate the molecular mechanisms linking insulin receptor activation to biological outcomes.
  • To highlight the role of SH2 domain-mediated interactions in insulin's pleiotropic effects.

Main Methods:

  • Review of recent scientific literature.
  • Analysis of molecular interactions in insulin signaling.
  • Elucidation of signal transduction pathways.

Main Results:

  • Insulin receptor tyrosine kinase phosphorylates key intracellular proteins.
  • Phosphotyrosine residues serve as binding sites for SH2 domain-containing proteins.
  • These interactions regulate multiple downstream intracellular signaling cascades.

Conclusions:

  • Insulin's complex biological actions are initiated by receptor tyrosine kinase activation.
  • SH2 domain-mediated protein-protein interactions are central to insulin signal transduction.
  • Further research into these pathways can illuminate insulin's role in cellular regulation.