Potentiation of receptor responses induced by prolonged binding of G{alpha}13 and leukemia-associated RhoGEF [Research]

Diverse cellular functions are controlled by RhoA-GTPases, which are activated by trimeric G proteins via RhoGEFs, among others. In this study, we focused on the signaling from GPCRs to RhoA via Gα₁₃ and leukemia-associated RhoGEF (LARG). The activation of Gα₁₃ was elucidated in living cells with high temporal and spatial resolution by means of FRET. The inactivation after agonist withdrawal occurred in the same range (t_1/2 = 25.3 ± 2.2 s; mean ± sem; n = 22) as described for other Gα proteins. The interaction of Gα₁₃ and LARG and the thereby-induced LARG translocation to the plasma membrane were at least 1 order of magnitude more stable after agonist withdrawal, exceeding Gα₁₃ deactivation in the absence of LARG several fold. Consequently, we observed an almost 100-fold higher agonist sensitivity of the Gα₁₃ LARG interaction compared to the Gα₁₃ activation in the absence of LARG.—Bodmann, E.-L., Krett, A.-L., Bünemann, M. Potentiation of receptor responses induced by prolonged binding of Gα₁₃ and leukemia-associated RhoGEF.

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