The International Diffusion of Regulatory Governance

This paper attempts to go beyond actor-centered explanations of the European Union's (EU) presence in regulatory politics by examining the role of the EU in the diffusion of regulatory norms and practices. We explore the international diffusion of public procurement policy, to which multiple organizations and especially the EU and the World Trade Organization have made an active contribution. Using the “opportunity-presence-capability” scheme, we argue that the EU is actively co-shaping the global agenda on public procurement, mainly as a result of the “opportunity” and “presence” dimensions of its global actorness and its role in the horizontal diffusion of public procurement regulations between international organizations. For “EU as a global actor” literature to offer valuable explanations, an in-depth analysis of its relationship with other international organizations, such as the World Trade Organization, reveals significant interactions and the co-shaping of policy agendas

Structural basis for the interaction of the myosin light chain Mlc1p with the myosin v Myo2p IQ motifs

Calmodulin, regulatory, and essential myosin light chain are evolutionary conserved proteins that, by binding to IQ motifs of target proteins, regulate essential intracellular processes among which are efficiency of secretory vesicles release at synapsis, intracellular signaling, and regulation of cell division. The yeast Saccharomyces cerevisiae calmodulin Cmd1 and the essential myosin light chain Mlc1p share the ability to interact with the class V myosin Myo2p and Myo4 and the class II myosin Myo1p. These myosins are required for vesicle, organelle, and mRNA transport, spindle orientation, and cytokinesis. We have used the budding yeast model system to study how calmodulin and essential myosin light chain selectively regulate class V myosin function. NMR structural analysis of uncomplexed Mlc1p and interaction studies with the first three IQ motifs of Myo2p show that the structural similarities between Mlc1p and the other members of the EF-hand superfamily of calmodulin-like proteins are mainly restricted to the C-lobe of these proteins. The N-lobe of Mlc1p presents a significantly compact and stable structure that is maintained both in the free and complexed states. The Mlc1p N-lobe interacts with the IQ motif in a manner that is regulated both by the IQ motifs sequence as well as by light chain structural features. These characteristic allows a distinctive interaction of Mlc1p with the first IQ motif of Myo2p when compared with calmodulin. This finding gives us a novel view of how calmodulin and essential light chain, through a differential binding to IQ1 of class V myosin motor, regulate this activity during vegetative growth and cytokinesis