The sound of whiteness: early music vocal performance practice in Britain

American Musicological Society annual meeting, San Francisco, 10 Nov. 2011

Ó Sheán Clárach Mac Domhnaill go dtí Nioclás Tóibín: traidisiún na hamhránaíochta ins na Déise

Féachann an tráchtas seo le solas a chaitheamh ar an amhránaíocht mar a chleachtaítí agus mar a chleactaítear fós i gcontae Phort Láirge í. Ardaítear ann ceisteanna a bhaineann le seachadadh agus le sealbhú na n-amhrán I measc an phobail i gceantar na nDéise sa tréimhse c.1750-1960, ó aimsir Sheáin Chláraigh go dtí an ré sin ina raibh Nioclás Tóibín, ‘rí-amhránaí Éireann’, ar bhuaic a réime. Cuirtear spéis anseo i bhfás agus i dteacht chun cinn an Rómánsachais agus (a leathchúpla) an náisiúnachais ar Mhór-roinn na hEorpa in earr an 18ú haois agus amach san 19ú haois; ar thionchar na ngluaiseachtaí sin i bhfad ó bhaile ar Éirinn i gcoitinne san aimsir úd; orthu sin a raibh díolamaí amhrán á gcur in eagar acu in Éirinn san 19ú agus amach san 20ú haois; agus, ar deireadh, ar an stór amhrán mar atá le clos inniu I measc na ndaoine i nGaeltacht na Déise.

Regulation of tail-anchored ubiquitin conjugating enzymes that are localised to the endoplasmic reticulum

The vast majority of secreted and membrane proteins are translated and folded at the endoplasmic reticulum (ER), where a sophisticated quality control mechanism ensures that only correctly folded proteins exit the ER and traffic to their final destinations. On the other hand, proteins that persistently misfold are eliminated through a process known as ER associated degradation (ERAD). This involves retrotranslocation of the misfolded protein through the ER membrane, and ubiquitination in advance of degradation by cytosolic proteasomes. The process of ERAD is best described in yeast where ubiquitin conjugating enzymes Ubc6p and Ubc7p function with a limited number of E3 ubiquitin ligases to ubiquitinate misfolded proteins. Interestingly, although the mechanistic principles of ERAD have been conserved through evolution, there is increasing evidence that homologues of the yeast enzymes have gained divergent roles and novel regulatory functions in higher eukaryotes, meaning that the process in humans is more complex and involves a larger repertoire of participating proteins. Two homologues of Ubc6p have been described in humans, and have been named as Ubc6 (UBE2J2) and Ubc6e (UBE2J1). However, little work has been done on these enzymes and thus our main objective of this study was to progress the functional characterisation of these ERAD E2 conjugating enzymes. Our studies included a detailed analysis of conditions whereby these proteins are stabilised and degraded. We’ve also explored the different molecular signalling pathways that induced changes on their steady state protein levels. Furthermore, Ubc6e has a phosphorylatable serine residue at position 184. Thus, our studies also involved delineating the signalling kinases that phosphorylate Ubc6e and examining its function in ERAD. Our studies confirm that the E2 Ubc enzymes are regulated posttranslationally and may have important implications in the regulation of ERAD.