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HighlightsPhosphoinositide-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 |
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.
Fig.1 Model for activation of Drosophila TRP and TRPL. (Venkatachalam, 2014)
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.
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.
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.
This article suggests that Pirt and PIP2 synergistically enhance TRPM8 channel activity, and Pirt regulates TRPM8 channel activity by increasing the single channel conductance.
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.
We provide custom membrane protein preparation services for worldwide customers. Leveraging by our advanced Magic™ membrane protein production platform, we are able to present target membrane protein in multiple active formats. Our professional scientists are happy to help you find an ideal method and make your project a success. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-PIRT antibody development services.
Creative Biolabs provides high-quality membrane protein preparation service to facilitate the development of worldwide customer’s research. During the past years, we have successfully established a powerful Magic™ membrane protein platform which enables us to provide a series of membrane protein preparation services. For more detailed information, please feel free to contact us.
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