English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONS
  This item is discarded!DetailsSummary

Discarded

Journal Article

Serine phosphorylation of ephrinB2 regulates trafficking of synaptic AMPA receptors

MPS-Authors
/persons/resource/persons38825

Essmann,  C. L.
Research Group: Signal Transduction / Acker-Palmer, MPI of Neurobiology, Max Planck Society;

/persons/resource/persons38984

Martinez,  E.
Research Group: Signal Transduction / Acker-Palmer, MPI of Neurobiology, Max Planck Society;

/persons/resource/persons38851

Geiger,  J. C.
Research Group: Signal Transduction / Acker-Palmer, MPI of Neurobiology, Max Planck Society;

/persons/resource/persons39136

Zimmer,  M.
Department: Molecular Neurobiology / Klein, MPI of Neurobiology, Max Planck Society;

/persons/resource/persons39101

Traut,  M. H.
Max Planck Research Group: Synaptic Receptor Trafficking / Stein, MPI of Neurobiology, Max Planck Society;

/persons/resource/persons39087

Stein,  V.
Max Planck Research Group: Synaptic Receptor Trafficking / Stein, MPI of Neurobiology, Max Planck Society;

/persons/resource/persons38927

Klein,  R.
Department: Molecular Neurobiology / Klein, MPI of Neurobiology, Max Planck Society;

/persons/resource/persons38744

Acker-Palmer,  A.
Research Group: Signal Transduction / Acker-Palmer, MPI of Neurobiology, Max Planck Society;

External Resource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Essmann, C. L., Martinez, E., Geiger, J. C., Zimmer, M., Traut, M. H., Stein, V., et al. (2008). Serine phosphorylation of ephrinB2 regulates trafficking of synaptic AMPA receptors. Nature Neuroscience, 11(9), 1035-1043.


Abstract
Plasticity in the brain is essential for maintaining memory and learning and is associated with the dynamic membrane trafficking of AMPA receptors. EphrinB proteins, ligands for EphB receptor tyrosine kinases, are transmembrane molecules with signaling capabilities that are required for spine morphogenesis, synapse formation and synaptic plasticity. Here, we describe a molecular mechanism for ephrinB2 function in controlling synaptic transmission. EphrinB2 signaling is critical for the stabilization of AMPA receptors at the cellular membrane. Mouse hippocampal neurons from conditional ephrinB2 knockouts showed enhanced constitutive internalization of AMPA receptors and reduced synaptic transmission. Mechanistically, glutamate receptor interacting proteins bridge ephrinB ligands and AMPA receptors. Moreover, this function involved a regulatory aspect of ephrinB reverse signaling that involves the phosphorylation of a single serine residue in their cytoplasmic tails. In summary, our findings uncover a model of cooperative AMPA receptor and ephrinB reverse signaling at the synapse.