PIRT Membrane Protein Introduction

Introduction of PIRT

Phosphoinositide-interacting regulator of TRP (PIRT), encode by the gene PIRT, is a transmembrane protein that is expressed in most nociceptive neurons in the dorsal root ganglia (DRG) in the peripheral nerve system (PNS). The C terminus of PIRT contains a cluster of positively charged residues, a characteristic of PIP-binding domains. By binding to several PIPs and TRPV1, PIRT is sufficient to potentiate TRPV1 activity in various sensory systems including thermosensation and nociception.

Basic Information of PIRT
Protein Name	Phosphoinositide-interacting protein
Gene Name	PIRT
Aliases	None
Organism	Homo sapiens (Human)
UniProt ID	P0C851
Transmembrane Times	2
Length (aa)	137
Sequence	MTMETLPKVLEVDEKSPEAKDLLPSQTASSLCISSRSESVWTTTPRSNWEIYRKPIVIMSVGGAILLFGVVITCLAYTLKLSDKSLSILKMVGPGFLSLGLMMLVCGLVWVPIIKKKQKHRQKSNFLRSLKSFFLTR

Function of PIRT Membrane Protein

The best-known function of PIRT is to act as a key modulator and an endogenous enhancer of TRPV1. Coexpression of PIRT and TRPV1 in HEK293 cells can significantly enhance TRPV1-mediated currents. It has been documented that PIRT-deficient DRG neurons have significantly lower noxious heat- and capsaicin-evoked currents those observed in wild-type (WT) neurons. PIRT is regarded as a component of the TRPV1 complex and positively regulates the channel activity via PIP2. It plays a vital role in sensing pain through modulation of the TRPV1 channel, and it is also necessary for proper itch sensation. Considering the crucial role of TRPV1 in neuropathic pain, we hypothesized that PIRT may also play an important role in the development and maintenance of neuropathic pain in CCI models.

PIRT Membrane Protein Introduction Fig.1 Model for activation of Drosophila TRP and TRPL. (Venkatachalam, 2014)

Application of PIRT Membrane Protein in Literature

Wang C., et al. Pirt Together with TRPV1 Is Involved in the Regulation of Neuropathic Pain. Neural Plast. 2018, 4861491. PubMed ID: 29808083

This article shows that the pain behavior attenuated in dysfunction of both Pirt and TRPV1 is much stronger than in dysfunction of Pirt or TRPV1 only in a CCI model in vitro study, indicating that Pirt together with TRPV1 is involved in CCI-induced neuropathic pain.
Hilton J.K., et al. Phosphoinositide-interacting regulator of TRP (PIRT) has opposing effects on human and mouse TRPM8 ion channels. J Biol Chem. 2018, 293: 9423-9434. PubMed ID: 29724821

This article provides the evidence for a direct interaction between PIRT and the TRPM8 S1-S4 domain with a 1:1 binding stoichiometry, suggesting that a functional tetrameric TRPM8 channel has four PIRT-binding sites.
Guo W., et al. Co-localization of Pirt protein and P2X2 receptors in the mouse enteric nervous system. Purinergic Signal. 2016, 12: 489-496. PubMed ID: 27105971

This article provides detailed information about the expression of Pirt in the gut and its co-localization with P2X2, indicating its potential role in influencing P2X2 receptor function.
Tang M., et al. Phosphoinositide interacting regulator of TRP (Pirt) enhances TRPM8 channel activity in vitro via increasing channel conductance. Acta Pharmacol Sin. 2016, 37: 98-104. PubMed ID: 26657057

This article suggests that Pirt and PIP2 synergistically enhance TRPM8 channel activity, and Pirt regulates TRPM8 channel activity by increasing the single channel conductance.
Wang C., et al. Pirt contributes to uterine contraction-induced pain in mice. Mol Pain. 2015, 11: 57. PubMed ID: 26376721

This article indicates that the number of capsaicin-responding neurons and the magnitude of evoked calcium response are markedly reduced in DRG neurons from Pirt^-/- mice, speculating that Pirt plays an important role in mice uterine contraction-induced pain.

PIRT Preparation Options

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Reference

Venkatachalam K, et al. (2014). Evolutionarily conserved, multitasking TRP channels: lessons from worms and flies. Handb Exp Pharmacol. 223: 937-962.

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