Recent Australian media scandals suggest that university students are increasingly outsourcing their assessments to third parties-a behaviour known as 'contract cheating'. This paper reports on findings from a large survey of students from eight Australian universities (n=14,086) which sought to explore students' experiences with and attitudes towards contract cheating, and the contextual factors that may influence this behavior. A spectrum of seven outsourcing behaviours were investigated, and three significant variables were found to be associated with contract cheating: dissatisfaction with the teaching and learning environment, a perception that there are 'lots of opportunities to cheat', and speaking a Language Other than English (LOTE) at home. To minimise contract cheating, our evidence suggests that universities need to support the development of teaching and learning environments which nurture strong student-teacher relationships, reduce opportunities to cheat through curriculum and assessment design, and address the well-recognised language and learning needs of LOTE students.

Ethanol enhances ␥-aminobutyrate (GABA) signaling in the brain, but its actions are inconsistent at GABA A receptors, especially at low concentrations achieved during social drinking. We postulated that the ⑀ isoform of protein kinase C (PKC⑀) regulates the ethanol sensitivity of GABA A receptors, as mice lacking PKC⑀ show an increased behavioral response to ethanol. Here we developed an ATP analog-sensitive PKC⑀ mutant to selectively inhibit the catalytic activity of PKC⑀. We used this mutant and PKC⑀ ؊/؊ mice to determine that PKC⑀ phosphorylates ␥2 subunits at serine 327 and that reduced phosphorylation of this site enhances the actions of ethanol and benzodiazepines at ␣1␤2␥2 receptors, which is the most abundant GABA A receptor subtype in the brain. Our findings indicate that PKC⑀ phosphorylation of ␥2 regulates the response of GABA A receptors to specific allosteric modulators, and, in particular, PKC⑀ inhibition renders these receptors sensitive to low intoxicating concentrations of ethanol. ␥-Aminobutyrate type A (GABA A )3 receptors mediate the majority of rapid inhibitory neurotransmission in the brain and are an important target for ethanol, the most widely abused drug (1). Ethanol modulation of GABA A receptors was first identified in synaptosomal preparations where intoxicating concentrations (10 -30 mM) enhanced receptor function as measured by 36 Cl uptake assays (2, 3). However, after 30 years of investigation, it is apparent that ethanol enhancement of synaptic GABA A receptors is variable and in some preparations cannot be detected even at anesthetic concentrations (1, 4).GABA A receptors are pentameric protein complexes of subunits from eight classes (␣1-6, ␤1-3, ␥1-3, ␦, ⑀, , , and 1-3) (5). Most receptors are composed of two ␣ subunits and two ␤ subunits that co-assemble with one ␥2 subunit, which anchors these receptors at synapses where they mediate phasic inhibition (6). A minority contain a ␦ subunit instead of ␥2; these receptors are extrasynaptic and mediate tonic inhibition in neurons (7). Because earlier ethanol studies that focused on GABA currents carried by ␥2-containing receptors produced variable results, recent attention has turned to ethanol effects at receptors containing ␦ subunits. Reports from three laboratories found these receptors enhanced by low (Յ30 mM) intoxicating concentrations of ethanol (8 -10). However, two recent studies were unable to demonstrate low dose ethanol sensitivity of ␦-containing GABA A receptors (11, 12), indicating that, like synaptic GABA A receptors, ethanol modulation of extrasynaptic receptors is also variable.The reasons for this high degree of variability are unknown. One possibility is that intracellular signaling pathways may regulate ethanol sensitivity of GABA A receptors, and the activity of such pathways was not controlled for in these studies. This hypothesis is consistent with our findings in mice lacking protein kinase C⑀ (PKC⑀), which show an increased behavioral response to ethanol (13). Ethanol modulation of GABA A receptors is a...

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Alcoholism is a progressive disorder that involves the amygdala. Mice lacking protein kinase C epsilon (PKCe) show reduced ethanol consumption, sensitivity and reward. We therefore investigated whether PKCe signaling in the amygdala is involved in ethanol consumption. Local knockdown of PKCe in the amygdala reduced ethanol consumption and preference in a limited-access paradigm. Further, mice that are heterozygous for the PKCe allele consume less ethanol compared with wildtype mice in this paradigm. These mice have a >50% reduction in the abundance of PKCe in the amygdala compared with wild-type mice. We conclude that amygdala PKCe is important for ethanol consumption in mice.

A low level of response to ethanol is associated with increased risk of alcoholism. A major determinant of the level of response is the capacity to develop acute functional tolerance (AFT) to ethanol during a single drinking session. Mice lacking protein kinase C epsilon (PKCe) show increased signs of ethanol intoxication and reduced ethanol self-administration. Here, we report that AFT to the motorimpairing effects of ethanol is reduced in PKCe (À/À) mice when compared with wild-type littermates. In wild-type mice, in vivo ethanol exposure produced AFT that was accompanied by increased phosphorylation of PKCe and resistance of GABA A receptors to ethanol. In contrast, in PKCe (À/À) mice, GABA A receptor sensitivity to ethanol was unaltered by acute in vivo ethanol exposure. Both PKCe (À/À) and PKCe ( + / + ) mice developed robust chronic tolerance to ethanol, but the presence of chronic tolerance did not change ethanol preference drinking. These findings suggest that ethanol activates a PKCe signaling pathway that contributes to GABA A receptor resistance to ethanol and to AFT. AFT can be genetically dissociated from chronic tolerance, which is not regulated by PKCe and does not alter PKCe modulation of ethanol preference.

The epsilon isoform of protein kinase C (PKCε) has important roles in the function of the cardiac, immune and nervous systems. As a result of its diverse actions, PKCε is the target of active drug discovery programs. A major research focus is to identify signaling cascades that include PKCε and the substrates that PKCε regulates. In this review we will identify and discuss those proteins that have been conclusively shown to be direct substrates of PKCε by the best currently available means. We will also describe binding partners that anchor PKCε near its substrates. We review the consequences of substrate phosphorylation and discuss cellular mechanisms by which target specificity is achieved. We begin with a brief overview of the biology of PKCε and methods for substrate identification, and proceed with a discussion of substrate categories to identify common themes that emerge and how these may be used to guide future studies.