PIEZO2 Membrane Protein Introduction

Introduction of PIEZO2

Piezo-type mechanosensitive ion channel component 2 (PIEZO2) is a mechanosensitive ion channel protein that in humans is encoded by the gene PIEZO2. PIEZO2 protein is conserved among various species, comprising more than 2,500 amino acids and includes 24-36 transmembrane domains. Three PIEZO2 subunits can form a functional homotrimer of about 1.2 MDa and have been highlighted as a central pore module. PIEZO2 is extensively spliced, producing different PIEZO2 isoforms with distinct properties. PIEZO2 has been shown to be widely expressed in somatic cells: chondrocytes, odontoblasts, endothelial cells, and astrocytes. Especially, PIEZO2 is also expressed in Merkel cells, outer hair cells, enterochromaffin cells of the gut, and in the neurons of the somatosensory ganglia, where it plays a key role in mechanosensation and proprioception.

Function of PIEZO2 Membrane Protein

The mechanosensitive ion channel PIEZO2 can transduce mechanical stimuli into intracellular signals, typically increasing intracellular Ca²⁺ concentration, to regulate mammalian development, physiology, and carcinogenesis. PIEZO2 deficiency may lead to severe deficits in the detection of vibration, fine touch, hair movement, proprioception, and breathing regulation. It is reported that PIEZO2 is required to sense physical cues from the environment to generate Ca²⁺ influx that maintains RhoA activity, which controls the formation and orientation of stress fibers (SFs) and focal adhesions (FAs). This PIEZO2-initiated signaling pathway has implications for different hallmarks of cancer invasion and metastasis. In addition, PIEZO2 is shown to interact with STOML3, an important regulator of mechanosensitivity and STOML3 expression potentiates PIEZO2 activity via a mechanism that leads to cholesterol-dependent stiffening of the plasma membrane. Phosphoinositide depletion from the plasma membrane leads to suppression of PIEZO2 activity.

Fig.1 Hypothetical topology of Piezo2. (Anderson, 2017)

Application of PIEZO2 Membrane Protein in Literature

1. Etem E.O., et al. The increased expression of Piezo1 and Piezo2 ion channels in human and mouse bladder carcinoma. Adv Clin Exp Med. 2018, 27(8): 1025-1031. PubMed ID: 30010255
   
   

   This article shows that Piezo expression is changed on specific days in the different developmental stage, demonstrating the role of these channels in bladder cancer development. The dysfunction of Piezo1/2 expression may contribute to the carcinogenesis of bladder cancer by causing proliferative changes and angiogenesis, providing new prognostic information for disease progression.

2. Feng J., et al. Piezo2 channel-Merkel cell signaling modulates the conversion of touch to itch. Science. 2018, 360(6388): 530-533. PubMed ID: 29724954
   
   

   This study reveals a previously unknown function of Piezo2 in the skin's tactile receptors and may provide new insight into allogeneic development.

3. Narayanan P., et al. Myotubularin related protein-2 and its phospholipid substrate PIP2 control Piezo2-mediated mechanotransduction in peripheral sensory neurons. Elife. 2018, 7. PubMed ID: 29521261
   
   

   This article reveals that myotubularin related protein-2 (Mtmr2) attenuates Piezo2-mediated rapidly adapting mechanically activated (RA-MA) currents, and Mtmr2-dependent Piezo2 inhibition involves the depletion of PI (3,5)P2.

4. Pardo-Pastor C., et al. Piezo2 channel regulates RhoA and actin cytoskeleton to promote cell mechanobiological responses. Proc Natl Acad Sci U S A. 2018, 115 (8): 1925-1930. PubMed ID: 29432180
   
   

   This article suggests a possible mechanism for the Piezo2-mediated activation of RhoA involves the recruitment of the Fyn kinase to the cell leading edge as well as calpain activation, which reveals that Piezo2 regulates RhoA and actin cytoskeleton to promote cell mechanobiological responses.

5. Szczot M., et al. Cell-Type-Specific Splicing of Piezo2 Regulates Mechanotransduction. Cell Rep. 21, 2760-2771. PubMed ID: 29212024
   
   

   This article shows that Piezo2 is extensively spliced, producing different Piezo2 isoforms with distinct properties, which provides a potential mechanism at the molecular level, by which transduction is tuned and the detection of a variety of mechanosensory stimuli is permitted.

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Reference

1. Anderson E.O., et al. (2017). Piezo2 in Cutaneous and Proprioceptive Mechanotransduction in Vertebrates. Curr Top Membr. 79: 197-217.

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