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XB-ART-22563
Proc Natl Acad Sci U S A 1993 Jun 01;9011:5327-31.
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GAP-43 augments G protein-coupled receptor transduction in Xenopus laevis oocytes.

Strittmatter SM , Cannon SC , Ross EM , Higashijima T , Fishman MC .


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The neuronal protein GAP-43 is thought to play a role in determining growth-cone motility, perhaps as an intracellular regulator of signal transduction, but its molecular mechanism of action has remained unclear. We find that GAP-43, when microinjected into Xenopus laevis oocytes, increases the oocyte response to G protein-coupled receptor agonists by 10- to 100-fold. Higher levels of GAP-43 cause a transient current flow, even without receptor stimulation. The GAP-43-induced current, like receptor-stimulated currents, is mediated by a calcium-activated chloride channel and can be desensitized by injection of inositol 1,4,5-trisphosphate. This suggests that neuronal GAP-43 may serve as an intracellular signal to greatly enhance the sensitivity of G protein-coupled receptor transduction.

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References [+] :
Alexander, Identification and characterization of the calmodulin-binding domain of neuromodulin, a neurospecific calmodulin-binding protein. 1988, Pubmed