The architecture of the CIB-TMC complex has significant implications for the regulation of mechanotransduction channel activity and ion selectivity. The structural model suggests that CIB proteins, such as CIB2 and CIB3, interact with multiple cytoplasmic domains of TMC proteins, including TMC1 and TMC2. This interaction likely stabilizes the TMC channels, facilitating their proper assembly and function as cation channels. The presence of CIB proteins may influence the conformational dynamics of TMC proteins, thereby modulating their gating properties in response to mechanical stimuli. Furthermore, the specific interactions between CIB proteins and TMC channels could play a role in determining the ion selectivity of the mechanotransduction channels. For instance, the stabilization of the TMC pore structure by CIB proteins may enhance the permeability of specific ions, such as calcium, which is crucial for the transduction of mechanical signals into electrical responses in hair cells. Understanding this complex architecture could lead to insights into how mechanotransduction is fine-tuned in different sensory contexts, potentially informing strategies to manipulate channel activity for therapeutic purposes.