AMPKβ is a regulatory subunit, which does not appear to affect osteoclastogenesis (Quinn et al., 2010), and AMPKγ contains the AMP binding site acting as a sensor for AMP.
Examination of an endothelial-specific Wnt/β-catenin reporter transgene, in which the fusion of the DNA binding domain of Gal4 to the β-catenin binding domain of TCF4 acts as a sensor for nuclear β-catenin (Kashiwada et al., 2015), confirmed that Gpr124 and Reck are both required for Wnt/β-catenin signaling in the PHBCs.
This is the case for photochromic crown ethers, which allow the photochemical control of cation binding, as well as for some optical sensors, designed for cation recognition.
To function as a sensor, metal binding must alter either the electronic structure or the molecular structure of the sensor.
The findings that Ng-mediated potentiation is dependent on neuronal activity, NMDAR, and CaM binding suggest that Ng may act as a sensor to the Ca2+ signal, and increasing its levels within the spine may enhance the spine sensitivity.
For the determination of biotin-binding kinetics, a sensor chip was prepared as follows: diaminoethylene was first attached to the surface using a mixture containing 0.2 M 1-ethyl-3- 3-dimethylaminopropyl) carbodiimide hydrochloride (EDC) and 0.05 M N-hydroxysuccinimide (NHS) in water.
Moreover, it also stabilizes kinetochore microtubule attachments and serves as a sensor of SAC by binding to and regulating the activity of BubR1.
Sandstrom et al. demonstrated that BTN3A1 acts as a sensor of intracellular PAgs by binding them in a surface pocket located in an intracellular domain termed B30.2.
However, adding the name of the system might solve the problem, as we know in this case that regulation is performed by ArcA because ArcB functions as a sensor and not as a DNA-binding transcriptional regulator.
