Piezo-Type Mechanosensitive Ion Channel Component 1 Proteins (PIEZO1)

Human Piezo-Type Mechanosensitive Ion Channel Component 1 (PIEZO1) interaction partners

1. Piezo1-shRNA could inhibit the invasion of the osteosarcoma cells.

2. Piezo1 plays an important role in the apoptosis of human osteoarthritis-derived chondrocytes through a caspase-12-dependent pathway.

3. MiR (show MLXIP Proteins)-103a might be a potential biomarker of myocardium infarction and could be used as an index for the diagnosis of AMI (show CFD Proteins). It may be involved in the development of HBP (show AZU1 Proteins) and onset of AMI (show CFD Proteins) through regulating the Piezo1 expression.

4. The structural dynamics of the PIEZO1 channel activation and inactivation by coarse-grained modeling has been reported.

5. Additional alterations in mutant PIEZO1 channel kinetics, differences in response to osmotic stress, and altered membrane protein trafficking, predicting variant alleles that worsen or ameliorate erythrocyte hydration.

6. differential regulation of PKA and cell stiffness in unconfined versus confined cells is abrogated by dual, but not individual, inhibition of Piezo1 and myosin II.

7. data demonstrate that PIEZO1 is required for the regulation of NO formation, vascular tone, and blood pressure.

8. The Piezo1 convert a variety of mechanical stimuli into channel activation and subsequent inactivation, and what molecules and mechanisms modulate Piezo function.

9. Because Piezo1 senses both mechanical crowding and stretch, it may act as a homeostatic sensor to control epithelial cell numbers, triggering extrusion and apoptosis in crowded regions and cell division in sparse regions.

10. platelets and Meg (show PTPN4 Proteins)-01 cells express the MS cation channel (show TRPV1 Proteins) Piezo1, which may contribute to Ca(2 (show CA2 Proteins)+) entry and thrombus formation under arterial shear.

Mouse (Murine) Piezo-Type Mechanosensitive Ion Channel Component 1 (PIEZO1) interaction partners

1. three-bladed, propeller-like electron cryo-microscopy structure of mouse Piezo1 and functional revelation of its mechanotransduction components

2. high-resolution cryo-electron microscopy structure of the mouse Piezo1 trimer

3. Both TRPV4 (show TRPV4 Proteins) and PIEZO1 channels contribute to currents activated by stimuli applied at cell-substrate contacts but only PIEZO1 mediates stretch-activated currents. These data demonstrate that there are separate, but overlapping, mechanoelectrical transduction pathways in chondrocytes.

4. Piezo1 is a molecular sensor of physical exercise in the endothelium that triggers endothelial communication to mesenteric vessel muscle cells, leading to vasoconstriction.

5. data demonstrate that PIEZO1 is required for the regulation of NO formation, vascular tone, and blood pressure.

6. Our results suggest that Piezo1 is unlikely to be a component of the mechanoelectrical transducer channel complex in mammalian cochlear outer hair cells

7. Smooth muscle Piezo1 is required for stretch-activated cationic channel activity. PIezo1 is involved in the remodeling of small arteries.

8. This study demonstrated that Piezo1 proteins consist of distinct responsible for ion conduction, mechanical force sensing, and transduction to coordinately fulfill their function as sophisticated MS channels.

9. Astrocytes in optic nerve head express multiple mechanosensitive channels, in particular Piezo1 and 2. The expression of putative mechanosensitive channels in these cells may contribute to their responsiveness to traumatic or glaucomatous injury.

10. cryo-electron microscopy structure of the full-length (2,547 amino acids) mouse Piezo1 (Piezo1) at a resolution of 4.8 A