The current assembly picture assumes that the core protein attaches to LD through the D2 domain,
dislocating the cellular ADRP in the process [175,184]. This determines a change in both size and
subcellular distribution of LD, which concentrate in the perinuclear region as a consequence of core
accumulation [184]. Intracellular localization of core with LD inversely correlates with the efficacy of
viral assembly. Thus, in the context of mutations that inhibit viral assembly, the core protein accumulates
around LD [185]. On the other hand, for viruses with efficient secretion, the core protein mainly shows
an ER localization [186]. Interestingly, the motility of the core protein on LD was inversely correlated
with the assembly efficacy, suggesting that the high motility of core would increase the odds of core
reaching the LD where it would not take part in the assembly process [187]. These data suggest that core
shuttles between the LD surface and the virion budding site, localized either at the ER or at the LD-ER
interface. Recent life cell imaging studies have shown that core protein rapidly associates with LDs, and
it is lately recruited into LD-independent small mobile structures. These mobile structures, likely
corresponding to viral particles, move along the microtubules, following the secretion pathway along
with apoE, but not apoB lipoprotein [185,188].