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Maturational changes in mouse cutaneous touch and Piezo2-mediated mechanotransduction

ABSTRACT: Maturational changes in mouse cutaneous touch and Piezo2-mediated mechanotransduction

PROVIDER: PRJNA645293 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12192100.fastq.gz	Fastqsanger.gz
	SRR12192101.fastq.gz	Fastqsanger.gz
	SRR12192102.fastq.gz	Fastqsanger.gz
	SRR12192054_1.fastq.gz	Fastqsanger.gz
	SRR12192054_2.fastq.gz	Fastqsanger.gz

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Maturational changes in mouse cutaneous touch and Piezo2-mediated mechanotransduction

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Project description:Cultured dorsal root ganglia neurons of 4 and 12 weeks old C57Bl/6 mice were first characterized as mechanosensitive (showed rapidly adapting mechanically actived currents in whole-cell votage clamp) and as mechanoreceptors (evoked action potential waveform in whole-cell current clamp). Next, cells were subjected to RNA-seq and sequences were analyzed bioinformatically. We found maturatinal changes comprising age-dependent differential gene expression in these somatosensory mechanoreceptors. The found differences call for tight age-matching of young mice in research and underline found electrophysiological and behavioural maturational changes in somatosensation, see Michel, Niklas and Narayanan, Pratibha and Shomroni, Orr and Schmidt, Manuela, Cutaneous Touch and Piezo2-Mediated Mechanotransduction Decline Throughout Mouse Maturation Until Adulthood. CELL-REPORTS-D-20-00425. Available at SSRN: https://ssrn.com/abstract=3536401 or http://dx.doi.org/10.2139/ssrn.3536401

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Multisite phosphorylation by protein kinase A mediates modality-specific modulation of PIEZO2

Project description:Protein kinase A is a downstream effector of many inflammatory mediators that induce pain hypersensitivity by increasing the mechanosensitivity of nociceptive sensory afferent. Here we examine the molecular mechanism underlying protein kinase-Adependent modulation of the mechanically-activated ion channel PIEZO2, which confers mechanosensitivity to many nociceptors. Using phosphorylation site prediction algorithms, we identified multiple putative and highly conserved PKA phosphorylation sites located on intracellular intrinsically disordered regions of PIEZO2. Site-directed mutagenesis and patch-clamp recordings showed that substitution of one or multiple putative PKA sites within a single intracellular domains does not alter PKA-induced PIEZO2 sensitization, whereas mutation of a combination of nine putative sites located on four different intracellular regions completely abolishes PKA-dependent PIEZO2 modulation, suggesting that the effect requires multisite phosphorylation. By demonstrating that PIEZO1 is not modulated by PKA, our data also reveals a previously unrecognized functional difference between PIEZO1 and PIEZO2. Moreover, by demonstrating that PKA only modulates PIEZO2 currents evoked by focal mechanical indentation of the cell, but not currents evoked by pressure-induced membrane stretch, we provide evidence suggesting that PIEZO2 is a polymodal mechanosensor that engages different protein domains for detecting different types of mechanical stimuli.

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Cell-Type-Specific Splicing of Piezo2 Regulates Mechanotransduction.

Project description:Piezo2 is a mechanically activated ion channel required for touch discrimination, vibration detection, and proprioception. Here, we discovered that Piezo2 is extensively spliced, producing different Piezo2 isoforms with distinct properties. Sensory neurons from both mice and humans express a large repertoire of Piezo2 variants, whereas non-neuronal tissues express predominantly a single isoform. Notably, even within sensory ganglia, we demonstrate the splicing of Piezo2 to be cell type specific. Biophysical characterization revealed substantial differences in ion permeability, sensitivity to calcium modulation, and inactivation kinetics among Piezo2 splice variants. Together, our results describe, at the molecular level, a potential mechanism by which transduction is tuned, permitting the detection of a variety of mechanosensory stimuli.

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Project description:Proprioception, the perception of body and limb position, is mediated by proprioceptors, specialized mechanosensory neurons that convey information about the stretch and tension experienced by muscles, tendons, skin and joints. In mammals, the molecular identity of the stretch-sensitive channel that mediates proprioception is unknown. We found that the mechanically activated nonselective cation channel Piezo2 was expressed in sensory endings of proprioceptors innervating muscle spindles and Golgi tendon organs in mice. Two independent mouse lines that lack Piezo2 in proprioceptive neurons showed severely uncoordinated body movements and abnormal limb positions. Moreover, the mechanosensitivity of parvalbumin-expressing neurons that predominantly mark proprioceptors was dependent on Piezo2 expression in vitro, and the stretch-induced firing of proprioceptors in muscle-nerve recordings was markedly reduced in Piezo2-deficient mice. Together, our results indicate that Piezo2 is the major mechanotransducer of mammalian proprioceptors.

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