6gse
Solution structure of the capsid domain from the activity-regulated cytoskeleton-associated protein, Arc
Structural highlights
FunctionARC_RAT Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the stress fiber dynamics and cell migration (By similarity). Required for consolidation of synaptic plasticity as well as formation of long-term memory. Regulates endocytosis of AMPA receptors in response to synaptic activity. Required for homeostatic synaptic scaling of AMPA receptors.[1] [2] Publication Abstract from PubMedThe activity-regulated cytoskeleton-associated protein, Arc, is highly expressed in neuronal dendrites and is involved in synaptic scaling and plasticity. Arc exhibits homology to the capsid-forming Gag proteins from retroviruses and can encapsulate its own mRNA and transport it to neighboring neurons. However, the molecular events that lead to the assembly of Arc capsids and how the capsid formation is regulated are not known. Here we show that the capsid domain of Arc may transiently form homogeneous oligomers of similar size as capsids formed by full-length Arc. We determined a high-resolution structure of the monomeric Arc capsid domain and mapped the initial structural change in the oligomerization process to the N-terminal part of the capsid domain. Peptide ligands from the NMDA receptor subunits inhibit oligomerization, which suggests that Arc's ability to transfer mRNA between cells may be regulated by protein-protein interactions at the synapse. The Capsid Domain of Arc Changes Its Oligomerization Propensity through Direct Interaction with the NMDA Receptor.,Nielsen LD, Pedersen CP, Erlendsson S, Teilum K Structure. 2019 Apr 16. pii: S0969-2126(19)30123-6. doi:, 10.1016/j.str.2019.04.001. PMID:31080121[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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