GTPase inhibiting mutations activate the α chain of Gs and stimulate adenylyl cyclase in human pituitary tumours
CA Landis, SB Masters, A Spada, AM Pace, HR Bourne… - Nature, 1989 - nature.com
CA Landis, SB Masters, A Spada, AM Pace, HR Bourne, L Vallar
Nature, 1989•nature.comA subset of growth hormone-secreting human pituitary tumours carries somatic mutations
that inhibit GTPase activity of a G protein α chain, αs. The resulting activation of adenylyl
cyclase bypasses the cells' normal requirement for trophic hormone. Amino acids substituted
in the putative gsp oncogene identify a domain of G protein α-chains required for intrinsic
ability to hydrolyse GTP. This domain may serve as a built-in counter-part of the separate
GTPase-activating proteins required for GTP hydrolysis by small GTP-binding proteins such …
that inhibit GTPase activity of a G protein α chain, αs. The resulting activation of adenylyl
cyclase bypasses the cells' normal requirement for trophic hormone. Amino acids substituted
in the putative gsp oncogene identify a domain of G protein α-chains required for intrinsic
ability to hydrolyse GTP. This domain may serve as a built-in counter-part of the separate
GTPase-activating proteins required for GTP hydrolysis by small GTP-binding proteins such …
Abstract
A subset of growth hormone-secreting human pituitary tumours carries somatic mutations that inhibit GTPase activity of a G protein α chain, αs. The resulting activation of adenylyl cyclase bypasses the cells' normal requirement for trophic hormone. Amino acids substituted in the putative gsp oncogene identify a domain of G protein α-chains required for intrinsic ability to hydrolyse GTP. This domain may serve as a built-in counter-part of the separate GTPase-activating proteins required for GTP hydrolysis by small GTP-binding proteins such as p21ras.
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