However, upon stimulation with VEGF we observed that only the larger isoform is translocated to the nucleus.
The larger isoform is also more abundant in brain and spinal cord (Claudiani et al., 2005), specifically in neurons (Charvin et al., 2003).
Large isoforms are concentrated postsynaptically at the NMJ [44].
Interestingly, in WT brain the Scn9a transcript had two isoforms, but in NOVA DKO brain the larger isoform was lost.
Interestingly, following SeV H4 but not SeV WT infection, the larger isoform was degraded, whereas the shorter isoform was not affected.
Importantly, treatment with the proteasome inhibitor MG132 prevented degradation of the larger MAVS isoform, signifying that following RLR activation, the larger MAVS isoform is ubiquitinated then selectively degraded by the proteasome.
The finding that the larger MAVS isoform is selectively degraded following RLR activation prompted us to investigate the mechanism of this degradation.
Because only the larger MAVS isoform is degraded following RLR activation, we hypothesized that the lysine residues that are targeted by TRIM25 to promote MAVS ubiquitination are only present in the larger isoform.
From the 59 178 transcript isoforms obtained by Oases assembly, a set of 53 409 non-redundant transcripts (including only the largest transcript isoform) was obtained with N50 length of 900 bp, largest contig length of 8173 bp and average contig length of 523 bp (Fig. 2A).
Specifically, the human MHC IIx isoform is larger than its MHC IIa (as seen in Fig. 1), whereas in the antelopes, it is slightly smaller than their respective MHC IIa.
