The regulated trafficking of neurotransmitter receptors at synapses is critical for synaptic function and plasticity. However, the molecular machinery that controls active transport of receptors into synapses is largely unknown. We found that, in rat hippocampus, the insertion of AMPA receptors (AMPARs) into spines during synaptic plasticity requires a specific motor protein, which we identified as myosin Va. We found that myosin Va associates with AMPARs through its cargo binding domain. This interaction was enhanced by active, GTP-bound Rab11, which is also transported by the motor protein. Myosin Va mediated the CaMKII-triggered translocation of GluR1 receptors from the dendritic shaft into spines, but it was not required for constitutive GluR2 trafficking. Accordingly, myosin Va was specifically required for long-term potentiation, but not for basal synaptic transmission. In summary, we identified the specific motor protein and organelle acceptor that catalyze the directional transport of AMPARs into spines during activity-dependent synaptic plasticity.

Motor protein-dependent transport of AMPA receptors into spines during long-term potentiation / S.S. Correia, S. Bassani, T.C. Brown, M.F. Lisé, D.S. Backos, A. El-Husseini, M. Passafaro, J.A. Esteban. - In: NATURE NEUROSCIENCE. - ISSN 1097-6256. - 11:4(2008), pp. 457-466.

Motor protein-dependent transport of AMPA receptors into spines during long-term potentiation

S. Bassani
Secondo
;
2008

Abstract

The regulated trafficking of neurotransmitter receptors at synapses is critical for synaptic function and plasticity. However, the molecular machinery that controls active transport of receptors into synapses is largely unknown. We found that, in rat hippocampus, the insertion of AMPA receptors (AMPARs) into spines during synaptic plasticity requires a specific motor protein, which we identified as myosin Va. We found that myosin Va associates with AMPARs through its cargo binding domain. This interaction was enhanced by active, GTP-bound Rab11, which is also transported by the motor protein. Myosin Va mediated the CaMKII-triggered translocation of GluR1 receptors from the dendritic shaft into spines, but it was not required for constitutive GluR2 trafficking. Accordingly, myosin Va was specifically required for long-term potentiation, but not for basal synaptic transmission. In summary, we identified the specific motor protein and organelle acceptor that catalyze the directional transport of AMPARs into spines during activity-dependent synaptic plasticity.
MYOSIN-VA ; SYNAPTIC-TRANSMISSION ; DENDRITIC SPINES ; RECYCLING ENDOSOMES ; GRISCELLI-DISEASE ; ACTIN-FILAMENTS ; TRAFFICKING ; PLASTICITY ; SYNAPSES ; NEURONS
2008
Article (author)
File in questo prodotto:
Non ci sono file associati a questo prodotto.
Pubblicazioni consigliate

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/57512
Citazioni
  • ???jsp.display-item.citation.pmc??? 119
  • Scopus 206
  • ???jsp.display-item.citation.isi??? 202
social impact