Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Protein tyrosine phosphorylation: implications for synaptic function

J W Gurd1

  • 1Division of Life Sciences, University of Toronto at Scarborough, Ontario, Canada. gurd@scar.utoronto.ca

Neurochemistry International
|November 19, 1997
PubMed
Summary

Tyrosine phosphorylation, crucial for mature cell function, significantly impacts brain synaptic activity. Dysregulation of tyrosine kinases and phosphatases alters synaptic protein phosphorylation, affecting neuronal function.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Changes in phosphorylation of the NMDA receptor in the rat hippocampus induced by status epilepticus.

Journal of neurochemistry·2005
Same author

Seizure activity results in increased tyrosine phosphorylation of the N-methyl-D-aspartate receptor in the hippocampus.

Brain research. Molecular brain research·2001
Same author

Increased phosphorylation of the NR1 subunit of the NMDA receptor following cerebral ischemia.

Journal of neurochemistry·2001
Same author

Transient cerebral ischemia increases tyrosine phosphorylation of the synaptic RAS-GTPase activating protein, SynGAP.

Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism·2001
Same author

Tyrosine phosphorylation of the N-methyl-D-aspartate receptor by exogenous and postsynaptic density-associated Src-family kinases.

Journal of neurochemistry·2001
Same author

Altered association of protein tyrosine kinases with postsynaptic densities after transient cerebral ischemia in the rat brain.

Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism·2000

Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Tyrosine phosphorylation was initially linked to cell growth but is now known to regulate mature cell functions.
  • The brain, especially synaptic regions, shows high tyrosine kinase activity and abundant tyrosine-phosphorylated proteins.
  • Emerging research highlights tyrosine phosphorylation's role in synaptic function regulation.

Purpose of the Study:

  • To review the established and emerging roles of tyrosine phosphorylation in regulating mature cell function.
  • To explore the specific involvement of tyrosine phosphorylation in synaptic function and plasticity.
  • To discuss the consequences of altered tyrosine kinase and phosphatase activity on synaptic and neuronal function.

Main Methods:

  • Literature review of studies on tyrosine phosphorylation in neuronal systems.

Related Experiment Videos

  • Analysis of research on synaptic proteins and their regulation by tyrosine phosphorylation.
  • Examination of the impact of physiological and pathological conditions on tyrosine phosphorylation.
  • Main Results:

    • Tyrosine phosphorylation is critical for regulating mature cell functions, particularly in the brain's synaptic regions.
    • It influences synaptic activity during processes like depolarization, long-term potentiation/depression, and ischemia.
    • Altered tyrosine kinase/phosphatase activity leads to changes in synaptic protein phosphorylation.

    Conclusions:

    • Tyrosine phosphorylation plays a vital role in modulating synaptic function and neuronal activity.
    • Imbalances in tyrosine kinase and phosphatase activity can lead to both short-term and long-term functional changes at the synapse.
    • Further research into tyrosine phosphorylation is essential for understanding brain function and neurological disorders.