On the Hybrid Extension of CTL and CTL+

The paper studies the expressivity, relative succinctness and complexity of satisfiability for hybrid extensions of the branching-time logics CTL and CTL+ by variables. Previous complexity results show that only fragments with one variable do have elementary complexity. It is shown that H1CTL+ and H1CTL, the hybrid extensions with one variable of CTL+ and CTL, respectively, are expressively equivalent but H1CTL+ is exponentially more succinct than H1CTL. On the other hand, HCTL+, the hybrid extension of CTL with arbitrarily many variables does not capture CTL*, as it even cannot express the simple CTL* property EGFp. The satisfiability problem for H1CTL+ is complete for triply exponential time, this remains true for quite weak fragments and quite strong extensions of the logic

An effector region in Eps8 is responsible for the activation of the Rac-specific GEF activity of Sos-1 and for the proper localization of the Rac-based actin-polymerizing machine

Genetic and biochemical evidence demonstrated that Eps8 is involved in the routing of signals from Ras to Rac. This is achieved through the formation of a tricomplex consisting of Eps8-E3b1-Sos-1, which is endowed with Rac guanine nucleotide exchange activity. The catalytic subunit of this complex is represented by Sos-1, a bifunctional molecule capable of catalyzing guanine nucleotide exchange on Ras and Rac. The mechanism by which Sos-1 activity is specifically directed toward Rac remains to be established. Here, by performing a structure-function analysis we show that the Eps8 output function resides in an effector region located within its COOH terminus. This effector region, when separated from the holoprotein, activates Rac and acts as a potent inducer of actin polymerization. In addition, it binds to Sos-1 and is able to induce Rac-specific, Sos-1-dependent guanine nucleotide exchange activity. Finally, the Eps8 effector region mediates a direct interaction of Eps8 with F-actin, dictating Eps8 cellular localization. We propose a model whereby the engagement of Eps8 in a tricomplex with E3b1 and Sos-1 facilitates the interaction of Eps8 with Sos-1 and the consequent activation of an Sos-1 Rac-specific catalytic ability. In this complex, determinants of Eps8 are responsible for the proper localization of the Rac-activating machine to sites of actin remodeling