INT309751

Context Info Confidence 0.08 First Reported 2010 Last Reported 2010 Negated 0 Speculated 0 Reported most in Body Documents 1 Total Number 3 Disease Relevance 0 Pain Relevance 0.23

lyase activity (CA2) transmembrane transport (TRPV4) response to stress (CA2) cytoplasm (CA2) cytosol (CA2) extracellular space (CA2)

CA2 (Homo sapiens) TRPV4 (Homo sapiens)

Pain Link Frequency Relevance Heat adenocard 3 89.48 TRP channel 12 81.64 agonist 9 77.60 qutenza 3 45.48 addiction 6 5.00 imagery 3 5.00

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Key:

Protein

Mutation

Event

Anatomy

Negation

Speculation

Pain term

Disease term

Using protein interaction experiments and functional assays, we show that the molecular correlate of Ca2+-dependent current potentiation is disruption of an interdomain interaction within TRPV4 resulting from CaM binding to a C-terminal site.

Ca2 Binding (interaction) of TRPV4

1) Confidence 0.08 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.07

The first comprises a ternary interaction in which Ca2+-loaded CaM binds to two different sites within the TRPV4 protein thus bringing two regulatory domains in proximity to each other.

Ca2 Binding (binds) of TRPV4 protein

2) Confidence 0.08 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.07

In contrast to these findings, TRPV4 neither binds to CaM in Ca2+-free buffers, nor to CaM1234, and potentiation of its activity directly depends on CaM interaction triggered by a rise in Ca2+.

Ca2 Binding (binds) of TRPV4

3) Confidence 0.07 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.09

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