No / Activity-dependent gene transcription and protein
synthesis underlie many forms of learning-related
synaptic plasticity. At excitatory glutamatergic
synapses, the immediate early gene product Arc/
Arg3.1 couples synaptic activity to postsynaptic
endocytosis of AMPA-type glutamate receptors.
Although the mechanisms for Arc induction have
been described, little is known regarding the molecular
machinery that terminates Arc function. Here, we
demonstrate that the RING domain ubiquitin ligase
Triad3A/RNF216 ubiquitinates Arc, resulting in its
rapid proteasomal degradation. Triad3A associates
with Arc, localizes to clathrin-coated pits, and is
associated with endocytic sites in dendrites and
spines. In the absence of Triad3A, Arc accumulates,
leading to the loss of surface AMPA receptors.
Furthermore, loss of Triad3A mimics and occludes
Arc-dependent forms of synaptic plasticity. Thus,
degradation of Arc by clathrin-localized Triad3A
regulates the availability of synaptic AMPA receptors
and temporally tunes Arc-mediated plasticity at
glutamatergic synapses. / A final draft copy of this article is not yet available.
| Identifer | oai:union.ndltd.org:BRADFORD/oai:bradscholars.brad.ac.uk:10454/8080 |
| Date | 05 February 2014 |
| Creators | Mabb, A.M., Je, H.S., Wall, M.J., Robinson, C.G., Larsen, R.S., Qiang, Y., Corrêa, Sonia A.L., Ehlers, M.D. |
| Source Sets | Bradford Scholars |
| Language | English |
| Detected Language | English |
| Type | Article, No full-text in the repository |
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