GTPase-activating protein
GTPase-activating protein (GAP) is a type of enzyme that regulates the activity of G proteins by increasing their rate of GTP hydrolysis. This process is crucial for the regulation of fundamental cellular processes such as signal transduction, cell division, and protein synthesis.
Function[edit | edit source]
GAPs function by binding to activated G proteins and stimulating their intrinsic GTPase activity, thereby accelerating the conversion of bound GTP to GDP. This results in the inactivation of the G protein and termination of the signaling event.
Types of GTPase-activating proteins[edit | edit source]
There are several types of GTPase-activating proteins, each with a specific set of target G proteins. These include:
- RhoGAP: These GAPs specifically target Rho family of G proteins, which are involved in regulating the cytoskeleton and cell migration.
- RasGAP: These GAPs target Ras subfamily of G proteins, which are involved in cell growth, differentiation, and survival.
- RabGAP: These GAPs target Rab family of G proteins, which are involved in vesicle trafficking.
Clinical significance[edit | edit source]
Mutations in GTPase-activating proteins have been implicated in several diseases, including cancer, neurological disorders, and cardiovascular diseases. For example, mutations in the NF1 gene, which encodes a RasGAP, are associated with Neurofibromatosis type I, a genetic disorder characterized by the growth of tumors along nerves in the skin, brain, and other parts of the body.
See also[edit | edit source]
References[edit | edit source]
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Contributors: Prab R. Tumpati, MD