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GTPase inhibiting mutations activate the alpha chain of Gs and stimulate adenylyl cyclase in human pituitary tumours.

Authors: Landis, CA  Masters, SB  Spada, A  Pace, AM  Bourne, HR  Vallar, L 
Citation: Landis CA, etal., Nature. 1989 Aug 31;340(6236):692-6.
Pubmed: (View Article at PubMed) PMID:2549426
DOI: Full-text: DOI:10.1038/340692a0

A subset of growth hormone-secreting human pituitary tumours carries somatic mutations that inhibit GTPase activity of a G protein alpha chain, alpha(s). 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 alpha-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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RGD Object Information
RGD ID: 1601376
Created: 2007-04-18
Species: All species
Last Modified: 2007-04-18
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.