Heritage and nation narration in contested societies

The targeted destruction of heritage sites in recent conflicts in Syria, Iraq and Mali has tragically illustrated how the treatment of heritage, as the tangible manifestation of the identity of the ‘other’, can be a symptom of the nadir to which group relations can descend. In a world in which the nation-state remains the primary means of identification, the following overarching research question was investigated: How do nation-states narrate their pasts in the built form? Drawing upon the conceptualisation of heritage as a present-orientated and political construct that is utilised to represent the values of the “dominant political, social, religious or ethnic groups” (Graham, Ashworth & Tunbridge 2000: p.183), this paper discusses the role that heritage interventions can play in both emphasising gulfs and building bridges in divided post-conflict societies (Fojut 2009).

Actin dynamics provides membrane tension to merge fusing vesicles into the plasma membrane

Vesicle fusion is executed via formation of an Ω-shaped structure (Ω-profile), followed by closure (kiss-and-run) or merging of the Ω-profile into the plasma membrane (full fusion). Although Ω-profile closure limits release but recycles vesicles economically, Ω-profile merging facilitates release but couples to classical endocytosis for recycling. Despite its crucial role in determining exocytosis/endocytosis modes, how Ω-profile merging is mediated is poorly understood in endocrine cells and neurons containing small ∼30-300 nm vesicles. Here, using confocal and super-resolution STED imaging, force measurements, pharmacology and gene knockout, we show that dynamic assembly of filamentous actin, involving ATP hydrolysis, N-WASP and formin, mediates Ω-profile merging by providing sufficient plasma membrane tension to shrink the Ω-profile in neuroendocrine chromaffin cells containing ∼300 nm vesicles. Actin-directed compounds also induce Ω-profile accumulation at lamprey synaptic active zones, suggesting that actin may mediate Ω-profile merging at synapses. These results uncover molecular and biophysical mechanisms underlying Ω-profile merging.