Y. T. Hu

Thickness-shear vibration of rotated Y -cut quartz plates with unattached electrodes and asymmetric air gaps

Thickness-shear vibration modes of rotated Y-cut quartz plates with unattached electrodes and asymmetric air gaps are analyzed. An exact solution is obtained from the equations of piezoelectricity. Numerical results calculated from the solution show that the resonant frequencies are sensitive to the dimensions of the air gaps. This offers new design parameters for better resonator performance.

Optimal electrode shape and size for shear mode thin film acoustic wave resonators

We study electrode shape and size for plates of hexagonal crystals or polarized ceramics with the sixfold axis or the poling direction parallel to the plate surfaces so that they can be excited into thickness-shear vibration by an electric field in the plate thickness direction. Electrode size and shape optimal in the sense that they satisfy the criterion of Bechmann’s number in every direction are determined.

Small GTPases SAR1A and SAR1B regulate the trafficking of the cardiac sodium channel Nav1.5

BACKGROUNDnThe cardiac sodium channel Nav1.5 is essential for the physiological function of the heart and causes cardiac arrhythmias and sudden death when mutated. Many disease-causing mutations in Nav1.5 cause defects in protein trafficking, a cellular process critical to the targeting of Nav1.5 to cell surface. However, the molecular mechanisms underlying the trafficking of Nav1.5, in particular, the exit from the endoplasmic reticulum (ER) for cell surface trafficking, remain poorly understood.nnnMETHODS AND RESULTSnHere we investigated the role of the SAR1 GTPases in trafficking of Nav1.5. Overexpression of dominant-negative mutant SAR1A (T39N or H79G) or SAR1B (T39N or H79G) significantly reduces the expression level of Nav1.5 on cell surface, and decreases the peak sodium current density (INa) in HEK/Nav1.5 cells and neonatal rat cardiomyocytes. Simultaneous knockdown of SAR1A and SAR1B expression by siRNAs significantly reduces the INa density, whereas single knockdown of either SAR1A or SAR1B has minimal effect. Computer modeling showed that the three-dimensional structure of SAR1 is similar to RAN. RAN was reported to interact with MOG1, a small protein involved in regulation of the ER exit of Nav1.5. Co-immunoprecipitation showed that SAR1A or SAR1B interacted with MOG1. Interestingly, knockdown of SAR1A and SAR1B expression abolished the MOG1-mediated increases in both cell surface trafficking of Nav1.5 and the density of INa.nnnCONCLUSIONSnThese data suggest that SAR1A and SAR1B are the critical regulators of trafficking of Nav1.5. Moreover, SAR1A and SAR1B interact with MOG1, and are required for MOG1-mediated cell surface expression and function of Nav1.5.