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Related Concept Videos

Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
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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.
Interaction domains in cell signaling
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Rab Cascades01:25

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Directing Proteins to the Rough Endoplasmic Reticulum01:34

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Related Experiment Video

Updated: May 24, 2026

Development and Application of Rapamycin-regulated Tyrosine Phosphatases
06:56

Development and Application of Rapamycin-regulated Tyrosine Phosphatases

Published on: September 6, 2024

Semaphorin signaling meets rap.

Johannes L Bos1, Willem-Jan Pannekoek

  • 1Molecular Cancer Research, Centre of Biomedical Genetics and Cancer Genomics Centre, University Medical Center Utrecht, Universiteitsweg 100, 3584 CG Utrecht, Netherlands. j.l.bos@umcutrecht.nl

Science Signaling
|February 23, 2012
PubMed
Summary

Plexins, which guide neurite outgrowth, directly inhibit Rap proteins. This semaphorin signaling discovery reveals how small GTPases control cell behavior during axon guidance.

Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Plexins are transmembrane receptors crucial for semaphorin-mediated axon guidance.
  • Plexins possess an intracellular guanosine triphosphatase (GTPase)-activating protein (GAP) domain.
  • Small GTPases, like Rap proteins, regulate cell adhesion and migration, processes vital for axon guidance.

Purpose of the Study:

  • To investigate the specific GTPase targets of plexin's intracellular GAP domain.
  • To elucidate the mechanism by which semaphorin signaling influences Rap GTPase activity.
  • To connect semaphorin and Rap-mediated signaling pathways in the context of neurite outgrowth.

Main Methods:

  • Biochemical assays to determine plexin GAP activity specificity.
  • Analysis of semaphorin-induced plexin dimerization.

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Lentivirus-mediated Genetic Manipulation and Visualization of Olfactory Sensory Neurons in vivo
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  • Investigation of Rap1 inhibition downstream of semaphorin signaling.

    • Main Results:

    • Plexin's GAP activity is specific for Rap proteins, not Ras.
    • Semaphorin-induced plexin dimerization activates its GAP function.
    • Activated plexin GAP activity leads to local inhibition of Rap1.
    • Inhibition of Rap1 by plexin promotes neurite retraction.

    Conclusions:

    • Semaphorin signaling directly interfaces with Rap-mediated signaling through plexin's GAP activity.
    • Plexins act as key regulators, inhibiting Rap1 to control neurite retraction.
    • This study highlights the role of small GTPases in spatially and temporally controlling cell behavior, particularly in neural development.