CCK activates RhoA and Rac1 differentially through Galpha13 and Galphaq in mouse pancreatic acini.

American Journal of Physiology. Cell Physiology
Maria E SabbatiniJohn A Williams

Abstract

Cholecystokinin (CCK) has been shown to activate RhoA and Rac1, as well as reorganize the actin cytoskeleton and, thereby, modify acinar morphology and amylase secretion in mouse pancreatic acini. The aim of the present study was to determine which heterotrimeric G proteins activate RhoA and Rac1 upon CCK stimulation. Galpha(13), but not Galpha(12), was identified in mouse pancreatic acini by RT-PCR and Western blotting. Using specific assays for RhoA and Rac1 activation, we showed that only active Galpha(13) activated RhoA. By contrast, active Galpha(13) and Galpha(q), but not Galpha(s), slightly increased GTP-bound Rac1 levels. A greater increase in Rac1 activation was observed when active Galpha(13) and active Galpha(q) were coexpressed. Galpha(i) was not required for CCK-induced RhoA or Rac1 activation. The regulator of G protein signaling (RGS) domain of p115-Rho guanine nucleotide exchange factor (p115-RGS), a specific inhibitor of Galpha(12/13)-mediated signaling, abolished CCK-stimulated RhoA activation. By contrast, both RGS-2, an inhibitor of Galpha(q), and p115-RGS abolished CCK-induced Rac1 activation, which was PLC pathway-independent. Active Galpha(q) and Galpha(13), but not Galpha(s), induced morphological change...Continue Reading

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Citations

Jul 14, 2010·Current Opinion in Gastroenterology·John A Williams
Jul 23, 2011·Current Opinion in Gastroenterology·Rashmi Chandra, Rodger A Liddle
May 5, 2010·The Journal of Clinical Investigation·Antonia SassmannNina Wettschureck
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Dec 14, 2011·Digestive Diseases·Joachim Mössner
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Sep 25, 2021·Nature Chemical Biology·Lin Cheng, Zhenhua Shao
Sep 25, 2021·Nature Chemical Biology·Qiufeng LiuYi Jiang
Dec 24, 2010·Current Opinion in Endocrinology, Diabetes, and Obesity

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