TBC1D3C, a member of the TBC1 domain family, plays a crucial role in cellular processes such as vesicle trafficking, cell signaling, and membrane dynamics. Specifically, TBC1D3C functions as a GTPase-activating protein (GAP) involved in regulating the activity of Rab GTPases, which are essential for vesicle trafficking and membrane trafficking events within cells. By modulating the activity of Rab GTPases, TBC1D3C influences various cellular processes, including endocytosis, exocytosis, and intracellular vesicle transport, ultimately contributing to the maintenance of cellular homeostasis and signaling.
Activation of TBC1D3C can be achieved through the modulation of several cellular pathways. Compounds such as luteolin, quercetin, and EGCG indirectly activate TBC1D3C by influencing signaling cascades such as the PI3K/Akt, mTOR, and AMPK pathways. These compounds inhibit key signaling molecules within these pathways, thereby relieving the inhibitory effect on TBC1D3C and promoting its activation. Additionally, other chemicals like curcumin, genistein, and resveratrol indirectly activate TBC1D3C by targeting pathways such as NF-κB, Wnt/β-catenin, and Nrf2, respectively. Through modulation of these pathways, these compounds enhance the activity of TBC1D3C, contributing to cellular processes regulated by this protein.
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