1. The noncatalytic domain of Ras-GAP can affect signaling through G protein-coupled receptors by a poorly understood mechanism. 2. In this study, fusion proteins containing elements of the noncatalytic domain of ras-GAP were examined for their ability to bind beta gamma subunits of heterotrimeric G proteins and phosphotyrosine-containing polypeptides. 3. Our results demonstrate that purified beta gamma dimers associated with bacterially expressed GAP proteins and that this association does not require SH2 or SH3 domains but is dependent on the presence of the GAP pleckstrin-homology (PH) domain. In contrast, only the SH2 domains are necessary for binding to tyrosine phosphorylated proteins. 4. These findings raise the possibility that heterotrimeric G proteins might affect functioning of ras-like proteins through beta gamma subunits acting on their regulatory molecules.

The PH domain of Ras-GAP is sufficient for in vitro binding to beta gamma subunits of heterotrimeric G proteins / N. Z., Xu; O., Coso; D., Mahadevan; DE BLASI, Antonio; P. K., Goldsmith; W. F., Simonds; J. S., Gutkind. - In: CELLULAR AND MOLECULAR NEUROBIOLOGY. - ISSN 0272-4340. - 16:1(1996), pp. 51-59. [10.1007/bf02578386]

The PH domain of Ras-GAP is sufficient for in vitro binding to beta gamma subunits of heterotrimeric G proteins

DE BLASI, ANTONIO;
1996

Abstract

1. The noncatalytic domain of Ras-GAP can affect signaling through G protein-coupled receptors by a poorly understood mechanism. 2. In this study, fusion proteins containing elements of the noncatalytic domain of ras-GAP were examined for their ability to bind beta gamma subunits of heterotrimeric G proteins and phosphotyrosine-containing polypeptides. 3. Our results demonstrate that purified beta gamma dimers associated with bacterially expressed GAP proteins and that this association does not require SH2 or SH3 domains but is dependent on the presence of the GAP pleckstrin-homology (PH) domain. In contrast, only the SH2 domains are necessary for binding to tyrosine phosphorylated proteins. 4. These findings raise the possibility that heterotrimeric G proteins might affect functioning of ras-like proteins through beta gamma subunits acting on their regulatory molecules.
1996
beta gamma subunits; g proteins; ph domain; ras; ras-gap
01 Pubblicazione su rivista::01a Articolo in rivista
The PH domain of Ras-GAP is sufficient for in vitro binding to beta gamma subunits of heterotrimeric G proteins / N. Z., Xu; O., Coso; D., Mahadevan; DE BLASI, Antonio; P. K., Goldsmith; W. F., Simonds; J. S., Gutkind. - In: CELLULAR AND MOLECULAR NEUROBIOLOGY. - ISSN 0272-4340. - 16:1(1996), pp. 51-59. [10.1007/bf02578386]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/453314
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