Do adaptors and innovators subscribe to opposing values?

Many studies reveal that adaptors are more ready to accept the status quo, whereas innovators are less likely to do so. This raises the question: Do adaptors and innovators subscribe to opposing values? A study is conducted with the following hypotheses. H1 predicts that adaptors are more likely to subscribe to CONSERVATION values like security, conformity, and tradition. H2 predicts that innovators are more likely to subscribe to OPENNESS TO CHANGE values like self-direction and stimulation. The respondents consisted of 243 students from Singapore with an average age of 17.9 years and 195 students from Australia with an average age of 19.1 years. These respondents answered a survey that contained the Kirton Adaption-Innovation (KAI) inventory and the Schwartz value survey. For the Singapore sample, KAI was negatively correlated with CONSERVATION: r = -39, p <.0001; but it was positively correlated with OPENNESS TO CHANGE: r = .14, p <.05. For the Australian sample, KAI was negatively correlated with CONSERVATION: r = -.15, p <.05; but it was positively correlated with OPENNESS TO CHANGE: r =.32, p <.0001. A standard regression analysis indicated that CONSERVATION was the most significant predictor (P = -.43, p <.0001) of KAI, followed by OPENNESS TO CHANGE (P =.37, p <.0001) and Nationality (P =.21, p <.0001). The significant finding associated with Nationality could be attributed to the fact that the Singaporean respondents were a highly select and innovative group of individuals who were aspiring to work in the media industry.

Domains of the TGN: Coats, tethers and G proteins

The trans-Golgi network is the major sorting compartment of the secretory pathway for protein, lipid and membrane traffic. There is a constant flow of membrane and cargo to and from this compartment. Evidence is emerging that the trans-Golgi network has multiple biochemically and functionally distinct subdomains, each of which contributes to the combined sorting and transport requirements of this dynamic compartment. The recruitment of distinct arrays of protein complexes to trans-Golgi network membranes is likely to produce the diversity of structure and biochemistry observed amongst subdomains that serve to generate different carriers or maintain resident trans-Golgi network components. This review discusses how these subdomains may be formed and examines the molecular players involved, including G proteins, clathrin adaptors and golgin tethers. Diversity within these protein families is highlighted and shown to be critical for the functionality of the trans-Golgi network, as a mediator of protein sorting and membrane transport, and for the maintenance of Golgi structure.