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

CaMKII-dependent phosphorylation regulates SAP97/NR2A interaction.

Fabrizio Gardoni1, Daniela Mauceri, Chiara Fiorentini

  • 1Center of Excellence on Neurodegenerative Diseases and Department of Pharmacological Sciences, University of Milano, via Balzaretti 9, 20133 Milano, Italy. Fabrizio.Gardoni@unimi.it

The Journal of Biological Chemistry
|August 23, 2003
PubMed
Summary

Synapse-associated protein 97 (SAP97) phosphorylation by CaMKII regulates its interaction with NMDA receptors. This phosphorylation controls the synaptic targeting of NMDA receptor subunits, impacting 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

LRRK2 Mutation Alters Dopamine D2 Receptor Localization in Induced Pluripotent Stem Cells-Derived Astrocytes From Parkinson's Disease Patients: Implications for Neuronal Damage.

Journal of neurochemistry·2026
Same author

Conditioned accumbal dopamine transients forecast individual preference for drug versus natural rewards and compulsive behavior.

Nature neuroscience·2026
Same author

Pharmacological Inhibition of FKBP51 Mitigates Early Life Adversity-Induced Social Deficits in Male Mice.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same author

From eye to AI: Studying rodent social behavior in the era of machine learning.

Neuroscience and biobehavioral reviews·2026
Same author

Discovery of Small-Molecule Inhibitors of the KCNQ1/Kv7.1 Potassium Channel with Virtual Screening and Functional Validation in Electrophysiological Assays and KCNQ1-Knockout Neural Stem Cells.

ACS chemical neuroscience·2026
Same author

Olfactory tubercle mediates adaptive social behavior by controlling threat assessment and the expression of social threat memories during recall in male mice.

Nature communications·2026

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Synapse-associated protein 97 (SAP97) is a key protein in the postsynaptic density.
  • SAP97 is involved in targeting ionotropic glutamate receptors to synapses.
  • The regulation of SAP97 function at the synapse is not fully understood.

Purpose of the Study:

  • To investigate the regulation of SAP97 interaction with NMDA receptors.
  • To elucidate the role of Ca2+/calmodulin-dependent protein kinase II (CaMKII) in SAP97 function.
  • To understand the mechanism controlling NMDA receptor synaptic targeting.

Main Methods:

  • Co-localization studies in hippocampal neurons and COS-7 cells.
  • Metabolic labeling and Western blotting to assess protein phosphorylation.

Related Experiment Videos

  • In vitro pull-out assays and co-immunoprecipitation experiments.
  • Site-directed mutagenesis to study phosphorylation effects.

    • Main Results:

    • SAP97 co-localizes with NMDA receptors and CaMKII at the postsynaptic density.
    • NMDA receptor activation induces CaMKII-dependent phosphorylation of SAP97 at Ser-232.
    • CaMKII-dependent phosphorylation disrupts the interaction between SAP97 and the NR2A subunit of NMDA receptors.
    • Expression of a SAP97 phosphorylation-mimicking mutant affects NMDA receptor targeting.

    Conclusions:

    • SAP97 directly interacts with the NR2A subunit of NMDA receptors via its PDZ1 domain.
    • CaMKII-dependent phosphorylation of SAP97 at Ser-232 regulates the SAP97-NR2A interaction.
    • This phosphorylation-dependent mechanism provides novel insights into the regulation of NMDA receptor synaptic targeting.