Pirt, a Phosphoinositide-Binding Protein, Functions as a Regulatory Subunit of TRPV1
作者： Andrew Y. Kim , Zongxiang Tang , Qin Liu , Kush N. Patel , David Maag
DOI: 10.1016/J.CELL.2008.02.053
关键词:
摘要: Transient receptor potential vanilloid 1 (TRPV1) is a molecular sensor of noxious heat and capsaicin. Its channel activity can be modulated by several mechanisms. Here we identify membrane protein, Pirt, as regulator TRPV1. Pirt expressed in most nociceptive neurons the dorsal root ganglia (DRG) including TRPV1-positive cells. null mice show impaired responsiveness to Noxious heat- capsaicin-sensitive currents Pirt-deficient DRG are significantly attenuated. Heterologous expression strongly enhances TRPV1-mediated currents. Furthermore, C terminus binds TRPV1 phosphoinositides, phosphatidylinositol-4,5-bisphosphate (PIP2), potentiate The PIP2 binding dependent on cluster basic residues crucial for regulation Importantly, enhancement requires Pirt. Therefore, key component complex positively regulates activity.
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