University of Dundee

About: University of Dundee is a education organization based out in Dundee, United Kingdom. It is known for research contribution in the topics: Population & Protein kinase A. The organization has 19258 authors who have published 39640 publications receiving 1919433 citations. The organization is also known as: Universitas Dundensis & Dundee University.

World class? An investigation of globalisation, difference and international student mobility

Abstract: This paper explores the motivations and meanings of international student mobility. Central to the discussion are the results of a large questionnaire survey and associated in-depth interviews with UK students enrolled in universities in six countries from around the world. The results suggest, first, that several different dimensions of social and cultural capital are accrued through study abroad. It is argued that the search for ‘world class’ education has taken on new significance. Second, the paper argues that analysis of student mobility should not be confined to a framework that separates study abroad from the wider life-course aspirations of students. It is argued that these insights go beyond existing theorisations of international student mobility to incorporate recognition of diverse approaches to difference within cultures of mobility, including class reproduction of distinction, broader notions of distinction within the life-plans of individual students, and how ‘reputations’ associated with educational destinations are structured by individuals, institutions and states in a global higher education system that produces differentially mediated geographies of international student mobility

Emerging role for AS160/TBC1D4 and TBC1D1 in the regulation of GLUT4 traffic

Abstract: Vesicular traffic of the glucose transporter GLUT4 occurs in response to insulin, muscle contraction, and metabolic stimuli that lead to changes in the energy status of the cell. These stimuli are associated with linked kinase cascades that lead to changes in glucose uptake that meet the energy challenges imposed on the highly regulated cell types in insulin-responsive tissues. The need to mechanistically link these kinase-associated stimuli to identifiable intermediates in vesicular traffic has long been known but has been difficult to fulfill. The Rab-GTPase-activating proteins AS160 and TBC1D1 have now emerged as strong candidates to fill this void. Here we review the initial discovery of these proteins as phosphorylated substrates for Akt and the more recent emerging data that indicate that these proteins are substrates for additional kinases that are downstream of contraction and energy status signaling. The mechanism of coupling these phosphorylated proteins to vesicle traffic appears to be dependent on linking to small GTPase of the Rab family. We examine the current state of a hypothesis that suggests that phosphorylation of the Rab-GTPase-activating proteins leads to increased GTP loading of Rab proteins on GLUT4 vesicles and subsequently to increased interaction with Rab effectors that control GLUT4 vesicle translocation.

Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis

Abstract: Ubiquitin modification is mediated by a large family of specificity determining ubiquitin E3 ligases. To facilitate ubiquitin transfer, RING E3 ligases bind both substrate and a ubiquitin E2 conjugating enzyme linked to ubiquitin via a thioester bond, but the mechanism of transfer has remained elusive. Here we report the crystal structure of the dimeric RING domain of rat RNF4 in complex with E2 (UbcH5A) linked by an isopeptide bond to ubiquitin. While the E2 contacts a single protomer of the RING, ubiquitin is folded back onto the E2 by contacts from both RING protomers. The carboxy-terminal tail of ubiquitin is locked into an active site groove on the E2 by an intricate network of interactions, resulting in changes at the E2 active site. This arrangement is primed for catalysis as it can deprotonate the incoming substrate lysine residue and stabilize the consequent tetrahedral transition-state intermediate.