Lack of evidence for direct phosphorylation of recombinantly expressed P2X(2) and P2X (3) receptors by protein kinase C.

ABSTRACT: P2X(3) and P2X(2+3) receptors are present on sensory neurons, where they contribute not only to transient nociceptive responses, but also to hypersensitivity underlying pathological pain states elicited by nerve injuries. Increased signalling through P2X(3) and P2X(2+3) receptors may arise from an increased routing to the plasma membrane and/or gain of function of pre-existing receptors. An obvious effector mechanism for functional modulation is protein kinase C (PKC)-mediated phosphorylation, since all P2X family members share a conserved consensus sequence for PKC, TXR/K, within the intracellularly located N-terminal domain. Contradictory reports have been published regarding the exact role of this motif. In the present study, we confirm that site-directed elimination of the potential ph

SUBMITTER: Franklin C 

PROVIDER: S-EPMC2072911 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature