Authoritarianism in the Living Room: Everyday Disciplines, Senses, and Morality in Taiwan’s Military Villages

With the nationalist government – Kuomintang (KMT) – retreating from mainland China in 1949, some 600,000 military personnel relocated to Taiwan. The military seized former Japanese colonial properties and built its own settlements, establishing temporary military dependents’ villages called juancun (眷村). When the prospect of counter-attacking the mainland vanished, the KMT had to face the reality of settling permanently in Taiwan. How, then, did the KMT’s authoritarian power enter the everyday lives of its own support group? In this article I will focus on the coercive elements of KMT authoritarianism, which permeated these military villages in Taiwan. I will look at the coercive mechanisms through the analytical lens of Foucauldian discipline. I argue that disciplinary techniques such as surveillance, disciplining of the body and the senses, as well as the creation of morality regimes played an important role in the cooptation of village residents into KMT authoritarianism by normalising and naturalising it

Functional Interchangeability of Late Domains, Late Domain Cofactors and Ubiquitin in Viral Budding

The membrane scission event that separates nascent enveloped virions from host cell membranes often requires the ESCRT pathway, which can be engaged through the action of peptide motifs, termed late (L-) domains, in viral proteins. Viral PTAP and YPDL-like L-domains bind directly to the ESCRT-I and ALIX components of the ESCRT pathway, while PPxY motifs bind Nedd4-like, HECT-domain containing, ubiquitin ligases (e.g. WWP1). It has been unclear precisely how ubiquitin ligase recruitment ultimately leads to particle release. Here, using a lysine-free viral Gag protein derived from the prototypic foamy virus (PFV), where attachment of ubiquitin to Gag can be controlled, we show that several different HECT domains can replace the WWP1 HECT domain in chimeric ubiquitin ligases and drive budding. Moreover, artificial recruitment of isolated HECT domains to Gag is sufficient to stimulate budding. Conversely, the HECT domain becomes dispensable if the other domains of WWP1 are directly fused to an ESCRT-1 protein. In each case where budding is driven by a HECT domain, its catalytic activity is essential, but Gag ubiquitination is dispensable, suggesting that ubiquitin ligation to trans-acting proteins drives budding. Paradoxically, however, we also demonstrate that direct fusion of a ubiquitin moiety to the C-terminus of PFV Gag can also promote budding, suggesting that ubiquitination of Gag can substitute for ubiquitination of trans-acting proteins. Depletion of Tsg101 and ALIX inhibits budding that is dependent on ubiquitin that is fused to Gag, or ligated to trans-acting proteins through the action of a PPxY motif. These studies underscore the flexibility in the ways that the ESCRT pathway can be engaged, and suggest a model in which the identity of the protein to which ubiquitin is attached is not critical for subsequent recruitment of ubiquitin-binding components of the ESCRT pathway and viral budding to proceed