XB-ART-8834Dev Biol 2001 Jun 29;9051-2:134-41.
Show Gene links Show Anatomy links
MAP2 phosphorylation and visual plasticity in Xenopus.
Microtubule-associated protein 2 (MAP2) has been implicated in activity-dependent structural changes in dendrites. MAP2 regulates the assembly of cytoskeletal proteins such as microtubules and actin, and its function is phosphorylation-dependent. In hippocampus, MAP2 has been reported to be dephosphorylated by activation of the NMDA-type glutamate receptor, a key player in synaptic plasticity. In this work, we used a phospho-specific MAP2 antibody (Ab 305) that recognizes epitopes close to the microtubule-binding domain to investigate the possible role of MAP2 in the Xenopus visual system. The binocular system in Xenopus exhibits activity-dependent synapse rearrangement during a critical period of development. We have found that, in critical period animals, NMDA receptor activation leads to the dephosphorylation of MAP2 at sites recognized by Ab 305 in a dose-dependent manner. We compared the responses of MAP2 to NMDA treatment in animals with high binocular plasticity (critical period juveniles and dark-reared adults) and low plasticity (normal adults). Our results show that, in all groups, NMDA treatment induces the dephosphorylation of MAP2. Tecta from frogs with different degrees of plasticity show no differences in the baseline level of MAP2 phosphorylation or in the NMDA-induced MAP2 dephosphorylation response. These results suggest that activity may modify dendrite structure via the NMDA receptor--MAP2-cytoskeletal protein pathway, but this pathway does not seem to be a determinant of the degree of plasticity.
PubMed ID: 11423088
Article link: Dev Biol
Species referenced: Xenopus laevis
Genes referenced: actl6a map2 tecta.1 tecta.2