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Potentiation of receptor responses induced by prolonged binding of G?13 and leukemia-associated RhoGEF.


ABSTRACT: 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 G?13 and leukemia-associated RhoGEF (LARG). The activation of G?13 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 (t1/2 = 25.3 ± 2.2 s; mean ± sem; n = 22) as described for other G? proteins. The interaction of G?13 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 G?13 deactivation in the absence of LARG several fold. Consequently, we observed an almost 100-fold higher agonist sensitivity of the G?13 LARG interaction compared to the G?13 activation in the absence of LARG.-Bodmann, E.-L., Krett, A.-L., Bünemann, M. Potentiation of receptor responses induced by prolonged binding of G?13 and leukemia-associated RhoGEF.

SUBMITTER: Bodmann EL 

PROVIDER: S-EPMC5503709 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature

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Potentiation of receptor responses induced by prolonged binding of Gα<sub>13</sub> and leukemia-associated RhoGEF.

Bodmann Eva-Lisa EL   Krett Anna-Lena AL   Bünemann Moritz M  

FASEB journal : official publication of the Federation of American Societies for Experimental Biology 20170502 8


Diverse cellular functions are controlled by RhoA-GTPases, which are activated by trimeric G proteins <i>via</i> RhoGEFs, among others. In this study, we focused on the signaling from GPCRs to RhoA <i>via</i> Gα<sub>13</sub> and leukemia-associated RhoGEF (LARG). The activation of Gα<sub>13</sub> 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 (<i>t</i><sub>1/2</sub> = 25.3 ± 2.2 s; me  ...[more]

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