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Ras-related GTP-binding protein A (RRAGA) is a member of the Rag family of small GTPases, functioning as a molecular switch that plays a central role in nutrient sensing and regulation of the mammalian target of rapamycin complex 1 (mTORC1) pathway. In its active GTP-bound form, RRAGA forms heterodimers with RRAGC or RRAGD and recruits mTORC1 to the lysosomal membrane in response to amino acid availability, enabling mTORC1 activation and downstream signaling that regulates cell growth, proliferation, and metabolism. RRAGA also interacts with ubiquitin ligases and is targeted by viral proteins, such as adenovirus E3-14.7K, influencing immune signaling and apoptosis. Dysregulation of RRAGA has been implicated in cancer and metabolic diseases due to its pivotal role in mTORC1 signaling
Drugs targeting this molecule would likely modulate mTORC1 activity by regulating the nucleotide-bound state of RRAGA or its interaction with mTORC1 pathway components, affecting cell growth, proliferation, and metabolism
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