The effector interactions of p21ras. [Trends Biochem Sci. 1993]

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1: Trends Biochem Sci. 1993 Jul;18(7):250-4.Links

The effector interactions of p21ras.

Marshall MS.

Department of Medicine, Indiana University School of Medicine, Indianapolis.

Genetic, physical and biochemical methods have been used successfully to identify discrete regions of the p21ras protein involved in protein-protein interactions. Of special interest are the effector residues of p21ras, which are essential for downstream signalling. This review details current understanding of what these residues are and how they bind and activate proteins essential to the ras pathway.

PMID: 8212134 [PubMed - indexed for MEDLINE]

Effector domain mutations dissociate p21ras effector function and GTPase-activating protein interaction.
Mol Cell Biol. 1993 Dec; 13(12):7311-20.

[Mol Cell Biol. 1993]
Interaction of GTPase activating proteins (GAPs) with p21ras measured by a novel fluorescence anisotropy method. Essential role of Arg-903 of GAP in activation of GTP hydrolysis on p21ras.
J Biol Chem. 1993 May 25; 268(15):10914-9.

[J Biol Chem. 1993]
ReviewStructural requirements for the interaction of p21ras with GAP, exchange factors, and its biological effector target.
J Biol Chem. 1993 May 5; 268(13):9157-60.

[J Biol Chem. 1993]
A ras effector domain mutant which is temperature sensitive for cellular transformation: interactions with GTPase-activating protein and NF-1.
Mol Cell Biol. 1991 Jun; 11(6):3132-8.

[Mol Cell Biol. 1991]
ReviewFluorescence approaches to the study of the p21ras GTPase mechanism.
Biochem Soc Trans. 1991 Apr; 19(2):432-7.

[Biochem Soc Trans. 1991]
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