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Related Concept Videos

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...
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...
Signal Transduction: Overview01:26

Signal Transduction: Overview

Cells respond to many types of information, often through receptor proteins positioned on the membrane. They respond to chemical signals, such as hormones, neurotransmitters, and other signaling molecules, initiating a series of molecular reactions to produce an appropriate response. This is called signal transduction. Cells also coordinate different responses elicited by the same signaling molecule via mediators, allowing molecular cross-talk.
Typically, signal transduction involves three...
Signal Sequences and Sorting Receptors01:41

Signal Sequences and Sorting Receptors

Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
Basic Operations on Signals01:22

Basic Operations on Signals

Basic signal operations include time reversal, time scaling, time shifting, and amplitude transformations. These operations are fundamental in signal processing and analysis.
Time Reversal mirrors a continuous-time signal about the vertical axis at t=0. This is achieved by substituting t with −t. For example, if a signal x(t) is considered, the time-reversed signal is x(−t). This operation can be graphically represented, showing the mirrored signal.
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...

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Related Experiment Video

Updated: Jun 8, 2026

Optogenetic Signaling Activation in Zebrafish Embryos
07:18

Optogenetic Signaling Activation in Zebrafish Embryos

Published on: October 27, 2023

Signals: tinkering with domains.

Erich Bornberg-Bauer1

  • 1Institute for Evolution and Biodiversity, University of Münster, Hüfferstrasse 1, D48149, Münster, Germany. ebb@uni-muenster.de

Science Signaling
|September 16, 2010
PubMed
Summary

Evolution repurposes protein domains for new functions by altering sequences while maintaining structural stability. This modularity allows for novel adaptations, with lab techniques helping to map these evolutionary pathways.

Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Biochemistry

Background:

  • Cell signaling relies on protein domains as reusable modules for diverse message transfer.
  • Protein domains often employ structural scaffolds that permit sequence variation without compromising stability.

Discussion:

  • The exploration of sequence space reveals that random mutations can readily confer novel functions.
  • A limited portion of potential sequence space is actually utilized during evolution.
  • Understanding these constraints is key to deciphering complex structure-function relationships.

Key Insights:

  • Evolutionary processes reuse existing molecular modules, such as protein domains, across various signaling contexts.
  • Structural stability is maintained despite sequence variation due to conserved scaffolds within protein domains.

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A Microfluidics Approach for the Functional Investigation of Signaling Oscillations Governing Somitogenesis
08:06

A Microfluidics Approach for the Functional Investigation of Signaling Oscillations Governing Somitogenesis

Published on: March 19, 2021

Related Experiment Videos

Last Updated: Jun 8, 2026

Optogenetic Signaling Activation in Zebrafish Embryos
07:18

Optogenetic Signaling Activation in Zebrafish Embryos

Published on: October 27, 2023

A Microfluidics Approach for the Functional Investigation of Signaling Oscillations Governing Somitogenesis
08:06

A Microfluidics Approach for the Functional Investigation of Signaling Oscillations Governing Somitogenesis

Published on: March 19, 2021

  • The potential for novel function arises frequently from mutations, highlighting the vast, underexplored sequence space.

    • Outlook:

    • Advanced laboratory techniques enable the inference of evolutionary trajectories.
    • Future research can explore the attainable complex structure-function relationships by understanding evolutionary constraints.