Islet activating protein-sensitive guanosine triphosphate-binding protein regulates K+-channels coupled with FMRFamide receptors.

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Abstract
A neuropeptide Phe-Met-Arg-Phe-NH2 (FMRFamide) induces K+-dependent outward current in Aplysia neurons. Intracellular application of islet activating protein (TAP) irreversibly and selectively blocked this outward current without affecting resting membrane conductance. An injection of GTPγS, a nonhydrolyzable analogue of guanosine triphosphate (GTP), caused very slow irreversible increase in K+-conductance of the resting membrane. However, repetitive applications of FMRFamide significantly expedited the effect of GTPγS. These results strongly suggest that K+-channel opening induced by FMRFamide is regulated by an IAP-sensitive GTP-binding protein.

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