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Application of diC8\u2010PIP<jats:sub>2<\/jats:sub>, a water soluble form of PIP<jats:sub>2<\/jats:sub>, to quiescent inside\u2010out patches evoked single channel currents with a unitary conductance of 1.9 pS. DiC8\u2010PIP<jats:sub>2<\/jats:sub>\u2010evoked channel currents were inhibited by anti\u2010TRPC1 antibodies and these characteristics are identical to SOCs evoked by cyclopiazonic acid (CPA) and BAPTA\u2010AM. SOCs stimulated by CPA, BAPTA\u2010AM and the phorbol ester phorbol 12,13\u2010dibutyrate (PDBu) were reduced by anti\u2010PIP<jats:sub>2<\/jats:sub> antibodies and by depletion of tissue PIP<jats:sub>2<\/jats:sub> levels by pre\u2010treatment of preparations with wortmannin and LY294002. However, these reagents did not alter the ability of PIP<jats:sub>2<\/jats:sub> to activate SOCs in inside\u2010out patches. Co\u2010immunoprecipitation techniques demonstrated association between TRPC1 and PIP<jats:sub>2<\/jats:sub> at rest, which was greatly decreased by wortmannin and LY294002. Pre\u2010treatment of cells with PDBu, which activates protein kinase C (PKC), augmented SOC activation by PIP<jats:sub>2<\/jats:sub> whereas the PKC inhibitor chelerythrine decreased SOC stimulation by PIP<jats:sub>2<\/jats:sub>. Co\u2010immunoprecipitation experiments provide evidence that PKC\u2010dependent phosphorylation of TRPC1 occurs constitutively and was increased by CPA and PDBu but decreased by chelerythrine. These novel results show that PIP<jats:sub>2<\/jats:sub> can activate TRPC1 SOCs in native vascular myocytes and plays an important role in SOC activation by CPA, BAPTA\u2010AM and PDBu. 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