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Cell-surface Signaling

Cell-surface Signaling

Hormones—or any molecule that binds to a receptor, known as a ligand—that are lipid-insoluble (water-soluble) are not able to diffuse across the cell membrane. In order to be able to affect a cell without entering it, these hormones bind to receptors on the cell membrane. When a first messenger, a hormone, binds to a receptor, a signal cascade is set off, causing second messengers, proteins inside the cell, to become activated, resulting in downstream effects.

Amplifying Signals via Second Messengers

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...

What are Second Messengers?

What are Second Messengers?

Because many receptor binding ligands are hydrophilic, they do not cross the cell membrane and thus their message must be relayed to a second messenger on the inside. There are several second messenger pathways, each with their own way of relaying information. G-protein coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol path is active when the receptor induces phospholipase C to hydrolyze the phospholipid,...

What are Second Messengers?

What are Second Messengers?

Because many receptor binding ligands are hydrophilic, they do not cross the cell membrane and thus their message must be relayed to a second messenger on the inside. There are several second messenger pathways, each with their own way of relaying information. G-protein coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol path is active when the receptor induces phospholipase C to hydrolyze the phospholipid,...

Calmodulin-dependent Signaling

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,...

Contact-dependent Signaling

Contact-dependent Signaling

Contact-dependent signaling, as the name suggests, requires that communicating cells be in direct contact with each other. This is achieved either through receptor-ligand interactions or by specialized cytoplasmic channels that allow the flow of small molecules between cells. In animal cells, channels called gap junctions facilitate contact-dependent signaling in certain tissues, whereas, plasmodesmata perform a similar function in plants.
Gap Junctions
In animal cells, gap junctions are formed...

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Related Experiment Video

Updated: Jun 12, 2026

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)

Published on: November 29, 2014

Bound to the messenger.

|June 5, 2010

Summary

This summary is machine-generated.

A novel method precisely maps RNA-binding proteins across the entire transcriptome. This technique identifies the exact locations where proteins attach to their target RNA molecules.

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Last Updated: Jun 12, 2026

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)

Published on: November 29, 2014

Spatiotemporally Controlled Nuclear Translocation of Guests in Living Cells Using Caged Molecular Glues as Photoactivatable Tags

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Published on: January 17, 2019

mRNA Interactome Capture from Plant Protoplasts

mRNA Interactome Capture from Plant Protoplasts

Published on: July 28, 2017

Area of Science:

Molecular Biology
Genomics
Biochemistry

Background:

Understanding RNA-protein interactions is crucial for gene regulation.
Current methods lack the resolution to pinpoint binding sites genome-wide.
Specific RNA-binding proteins (RBPs) play vital roles in cellular processes.

Discussion:

The developed technique enables high-resolution mapping of RBP binding sites.
It provides unprecedented detail on the distribution of RBPs on target RNAs.
This advancement facilitates the study of RBP-RNA interactions in various biological contexts.

Key Insights:

Transcriptome-wide isolation of protein-bound RNAs is now possible with high precision.
The precise location of RNA-binding proteins on target RNAs can be determined.
This method offers a powerful tool for functional genomics and molecular biology research.

Outlook:

Future applications include studying disease mechanisms involving aberrant RBP binding.
This technique can accelerate the discovery of novel regulatory networks.
Further refinement may enable dynamic studies of RBP-RNA interactions in real-time.