BackgroundTeamwork is a fundamental aspect of many human activities, from business to art and from sports to science. Recent research suggest that team work is of crucial importance to cutting-edge scientific research, but little is known about how teamwork leads to greater creativity. Indeed, for many team activities, it is not even clear how to assign credit to individual team members. Remarkably, at least in the context of sports, there is usually a broad consensus on who are the top performers and on what qualifies as an outstanding performance.Methodology/Principal FindingsIn order to determine how individual features can be quantified, and as a test bed for other team-based human activities, we analyze the performance of players in the European Cup 2008 soccer tournament. We develop a network approach that provides a powerful quantification of the contributions of individual players and of overall team performance.Conclusions/SignificanceWe hypothesize that generalizations of our approach could be useful in other contexts where quantification of the contributions of individual team members is important.

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Mitotic cell division is the most fundamental task of all living cells. Cells have intricate and tightly regulated machinery to ensure that mitosis occurs with appropriate frequency and high fidelity. A core element of this machinery is the kinesin-5 motor protein, which plays essential roles in spindle formation and maintenance. In this review, we discuss how the structural and mechanical properties of kinesin-5 motors uniquely suit them to their mitotic role. We describe some of the small molecule inhibitors and regulatory proteins that act on kinesin-5, and discuss how these regulators may influence the process of cell division. Finally, we touch on some more recently described functions of kinesin-5 motors in non-dividing cells. Throughout, we highlight a number of open questions that impede our understanding of both this motor's function and the potential utility of kinesin-5 inhibitors.

Spindle formation in mammalian cells requires precise spatial and temporal regulation of the kinesin-5, Eg5, which generates outward force to establish spindle bipolarity. Our results demonstrate that Eg5 is phosphorylated in cultured cells by Src family kinases (SFKs) at three sites in the motor head: Y125, Y211, and Y231. Mutation of these sites diminishes motor activity in vitro, and replacement of endogenous Eg5 with phosphomimetic Y211 in LLC-Pk1 cells results in monopolar spindles, consistent with loss of Eg5 activity. Cells treated with SFK inhibitors show defects in spindle formation, similar to those in cells expressing the non-phosphorylatable Y211 mutant, and distinct from inhibition of other mitotic kinases. We propose that this phosphoregulatory mechanism tunes Eg5 enzymatic activity for optimal spindle morphology.