Ras: Difference between revisions
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The Ras protein is a [[monomeric G-protein|monomeric G-protein]] with weak [[GTPase|GTPase]] [[enzyme|enzyme]] activity. It is a [[signal-transducer protein|signal-transducer protein]] for growth factors and therefore it helps to transfer signals from cell-surface [[Receptor Tyrosine Kinase|Receptor Tyrosine Kinase]] (RTK) receptors to the [[nucleus|nucleus]] <ref>Alberts, B, et al, 2008. Molecular Biology of the Cell. 5th ed. United States of America: Garland Science.</ref>.<br> | The Ras protein is a [[monomeric G-protein|monomeric G-protein]] with weak [[GTPase|GTPase]] [[enzyme|enzyme]] activity. It is a [[signal-transducer protein|signal-transducer protein]] for growth factors and therefore it helps to transfer signals from cell-surface [[Receptor Tyrosine Kinase|Receptor Tyrosine Kinase]] (RTK) receptors to the [[nucleus|nucleus]] <ref>Alberts, B, et al, 2008. Molecular Biology of the Cell. 5th ed. United States of America: Garland Science.</ref>.<br> | ||
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== Active and Inactive forms of Ras == | |||
Ras is in its inactive form when it is bound to GDP, and becomes active once GDP has been exchanged for a GTP molecule. This reaction is initiated by the action of a specific signal molecule binding to a RTK receptor on the cell membrane. The activated RTK has intrinsic kinase activity, and this leads to phosphorylation of docking proteins at the RTK domains. The adaptor protein Grb-2 mediates the reaction between the RTK and Ras GEF, which exchanges GDP for GTP, acvtivating Ras which can transmit of a signal along multiple pathways. The inactivation of Ras is controlled by GTP hydrolysis.<br> | |||
=== References: === | === References: === | ||
<references /> | <references />Alberts, B, et al, 2008. Molecular Biology of the Cell. 5th ed. United States of America: Garland Science.<references /> |
Revision as of 21:18, 27 November 2011
The Ras protein is a monomeric G-protein with weak GTPase enzyme activity. It is a signal-transducer protein for growth factors and therefore it helps to transfer signals from cell-surface Receptor Tyrosine Kinase (RTK) receptors to the nucleus [1].
Active and Inactive forms of Ras
Ras is in its inactive form when it is bound to GDP, and becomes active once GDP has been exchanged for a GTP molecule. This reaction is initiated by the action of a specific signal molecule binding to a RTK receptor on the cell membrane. The activated RTK has intrinsic kinase activity, and this leads to phosphorylation of docking proteins at the RTK domains. The adaptor protein Grb-2 mediates the reaction between the RTK and Ras GEF, which exchanges GDP for GTP, acvtivating Ras which can transmit of a signal along multiple pathways. The inactivation of Ras is controlled by GTP hydrolysis.
References:
- ↑ Alberts, B, et al, 2008. Molecular Biology of the Cell. 5th ed. United States of America: Garland Science.
Alberts, B, et al, 2008. Molecular Biology of the Cell. 5th ed. United States of America: Garland Science.