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This paper reports on a new type of high-frequency mode-matched gyroscope with significantly reduced dependencies on environmental stimuli such as temperature, vibration, and shock. A novel stress-isolation system is used to effectively decouple an axis-symmetric bulk-acoustic wave (BAW) vibratory gyro from its substrate, minimizing the effect that external sources of error have on the offset and scale factor of the device. Substrate-decoupled (SD) BAW gyros with a resonance frequency of 4.3 MHz and Q values near 60 000 were implemented using the high aspect ratio poly and single-crystal silicon (HARPSS) process to achieve ultra-narrow capacitive gaps. Wafer-level packaged sensors were interfaced with a customized application-specific integrated circuit (ASIC) to achieve low variations in the offset across temperature (±26°s − 1 from − 40 to 85°C), supreme random-vibration immunity (0.012°s − 1 g RMS − 1 ) and excellent shock rejection. With a scale factor of 800 μV (°s, the SD-BAW gyro system attains a large full-scale range (±1250°s) with a non-linearity of less than 0.07%. A measured angle-random walk (ARW) of 0.39°/√h and a bias instability of 10.5°h − 1 are dominated by the thermal and flicker noise of the integrated circuit (IC), respectively. Additional measurements using external electronics show bias-instability values as low as 3.5°h INTRODUCTIONMicromachined gyroscopes have enabled a myriad of applications that range from basic motion detection for gaming to safety control systems in automobiles 1 . More recently, an increased interest in the use of microelectromechanical system inertial sensors for dead reckoning and pedestrian navigation in handheld electronics has placed stringent requirements on the die size, power consumption, and overall performance of this type of device. To date, most commercially available rate sensors have been designed as low-frequency flexural tuning-fork gyroscopes (TFGs), which are typically sensitive to random vibrations and prone to linear accelerations, such as those experienced under shock. These limitations complicate the use of TFG technology in large-volume, high-end applications, particularly in personal navigation, for which dependencies on fluctuations in the environment translate into long-term drift in the output of the system. Additionally, in recent months, concerns about the high sensitivity of consumer-grade gyroscopes in response to lowfrequency pressure signals that can be used to recover audio have increased as a potential threat for eavesdropping 2 , justifying the need for more environmentally robust rotation sensors.Acceleration suppression mechanisms can be implemented in TFGs to alleviate part of this problem using redundant proof masses that reject shock and vibration as common-mode signals 3 .

Membrane contact sites between the cortical endoplasmic reticulum (ER) and the plasma membrane (PM) provide a direct conduit for small molecule transfer and signaling between the two largest membranes of the cell. Contact is established through ER integral membrane proteins that physically tether the two membranes together, though the general mechanism is remarkably non-specific given the diversity of different tethering proteins. Primary tethers including VAMP-associated proteins (VAPs), Anoctamin/TMEM16/Ist2p homologs, and extended synaptotagmins (E-Syts), are largely conserved in most eukaryotes and are both necessary and sufficient for establishing ER-PM association. In addition, other species-specific ER-PM tether proteins impart unique functional attributes to both membranes at the cell cortex. This review distils recent functional and structural findings about conserved and speciesspecific tethers that form ER-PM contact sites, with an emphasis on their roles in the coordinate regulation of lipid metabolism, cellular structure, and responses to membrane stress.

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In yeast, at least seven proteins (Ice2p, Ist2p, Scs2/22p, Tcb1-Tcb3p) affect cortical endoplasmic reticulum (ER) tethering and contact with the plasma membrane (PM). In Δ-super-tether (Δ-s-tether) cells that lack these tethers, cortical ER-PM association is all but gone. Yeast OSBP homologue (Osh) proteins are also implicated in membrane contact site (MCS) assembly, perhaps as subunits for multicomponent tethers, though their function at MCSs involves intermembrane lipid transfer. Paradoxically, when analyzed by fluorescence and electron microscopy, the elimination of the OSH gene family does not reduce cortical ER-PM association but dramatically increases it. In response to the inactivation of all Osh proteins, the yeast E-Syt (extended-synaptotagmin) homologue Tcb3p is post-transcriptionally upregulated thereby generating additional Tcb3p-dependent ER-PM MCSs for recruiting more cortical ER to the PM. Although the elimination of OSH genes and the deletion of ER-PM tether genes have divergent effects on cortical ER-PM association, both elicit the Environmental Stress Response (ESR). Through comparisons of transcriptomic profiles of cells lacking OSH genes or ER-PM tethers, changes in ESR expression are partially manifested through the induction of the HOG (high-osmolarity glycerol) PM stress pathway or the ER-specific UPR (unfolded protein response) pathway, respectively. Defects in either UPR or HOG pathways also increase ER-PM MCSs, and expression of extra “artificial ER-PM membrane staples” rescues growth of UPR mutants challenged with lethal ER stress. Transcriptome analysis of OSH and Δ-s-tether mutants also revealed dysregulation of inositol-dependent phospholipid gene expression, and the combined lethality of osh4Δ and Δ-s-tether mutations is suppressed by overexpression of the phosphatidic acid biosynthetic gene, DGK1. These findings establish that the Tcb3p tether is induced by ER and PM stresses and ER-PM MCSs augment responses to membrane stresses, which are integrated through the broader ESR pathway.