+ |
PKA | up-regulates activity
phosphorylation
|
TRPV4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260885 |
Ser162 |
FDIVSRGsTADLDGL |
Homo sapiens |
|
pmid |
sentence |
19661060 |
We conclude that the serine/threonine kinases PKC and PKA enhance activation of the TRPV4 ion channel by phosphorylation at specific sites and that phosphorylation depends on assembly of PKC and PKA by AKAP79 into a signaling complex with TRPV4. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276232 |
Ser162 |
FDIVSRGsTADLDGL |
in vitro |
|
pmid |
sentence |
19661060 |
We conclude that the serine/threonine kinases PKC and PKA enhance activation of the TRPV4 ion channel by phosphorylation at specific sites and that phosphorylation depends on assembly of PKC and PKA by AKAP79 into a signaling complex with TRPV4. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260883 |
Ser189 |
DEEFREPsTGKTCLP |
Homo sapiens |
|
pmid |
sentence |
19661060 |
We conclude that the serine/threonine kinases PKC and PKA enhance activation of the TRPV4 ion channel by phosphorylation at specific sites and that phosphorylation depends on assembly of PKC and PKA by AKAP79 into a signaling complex with TRPV4. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276233 |
Ser189 |
DEEFREPsTGKTCLP |
in vitro |
|
pmid |
sentence |
19661060 |
We conclude that the serine/threonine kinases PKC and PKA enhance activation of the TRPV4 ion channel by phosphorylation at specific sites and that phosphorylation depends on assembly of PKC and PKA by AKAP79 into a signaling complex with TRPV4. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276231 |
Thr175 |
GLLPFLLtHKKRLTD |
in vitro |
|
pmid |
sentence |
19661060 |
We conclude that the serine/threonine kinases PKC and PKA enhance activation of the TRPV4 ion channel by phosphorylation at specific sites and that phosphorylation depends on assembly of PKC and PKA by AKAP79 into a signaling complex with TRPV4. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260881 |
Thr175 |
GLLPFLLtHKKRLTD |
Homo sapiens |
|
pmid |
sentence |
19661060 |
We conclude that the serine/threonine kinases PKC and PKA enhance activation of the TRPV4 ion channel by phosphorylation at specific sites and that phosphorylation depends on assembly of PKC and PKA by AKAP79 into a signaling complex with TRPV4. |
|
Publications: |
6 |
Organism: |
Homo Sapiens, In Vitro |
+ |
PKC | up-regulates activity
phosphorylation
|
TRPV4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276229 |
Ser162 |
FDIVSRGsTADLDGL |
in vitro |
|
pmid |
sentence |
19661060 |
Activation of the TRPV4 ion channel is enhanced by phosphorylation. TRPV4 is phosphorylated in response to activation of PKC. We conclude that the serine/threonine kinases PKC and PKA enhance activation of the TRPV4 ion channel by phosphorylation at specific sites and that phosphorylation depends on assembly of PKC and PKA by AKAP79 into a signaling complex with TRPV4. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276230 |
Ser189 |
DEEFREPsTGKTCLP |
in vitro |
|
pmid |
sentence |
19661060 |
Activation of the TRPV4 ion channel is enhanced by phosphorylation. TRPV4 is phosphorylated in response to activation of PKC. We conclude that the serine/threonine kinases PKC and PKA enhance activation of the TRPV4 ion channel by phosphorylation at specific sites and that phosphorylation depends on assembly of PKC and PKA by AKAP79 into a signaling complex with TRPV4. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276228 |
Thr175 |
GLLPFLLtHKKRLTD |
in vitro |
|
pmid |
sentence |
19661060 |
Activation of the TRPV4 ion channel is enhanced by phosphorylation. TRPV4 is phosphorylated in response to activation of PKC. We conclude that the serine/threonine kinases PKC and PKA enhance activation of the TRPV4 ion channel by phosphorylation at specific sites and that phosphorylation depends on assembly of PKC and PKA by AKAP79 into a signaling complex with TRPV4. |
|
Publications: |
3 |
Organism: |
In Vitro |
+ |
PRKCA | up-regulates activity
phosphorylation
|
TRPV4 |
0.357 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260886 |
Ser162 |
FDIVSRGsTADLDGL |
Homo sapiens |
|
pmid |
sentence |
19661060 |
We conclude that the serine/threonine kinases PKC and PKA enhance activation of the TRPV4 ion channel by phosphorylation at specific sites and that phosphorylation depends on assembly of PKC and PKA by AKAP79 into a signaling complex with TRPV4. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260884 |
Ser189 |
DEEFREPsTGKTCLP |
Homo sapiens |
|
pmid |
sentence |
19661060 |
We conclude that the serine/threonine kinases PKC and PKA enhance activation of the TRPV4 ion channel by phosphorylation at specific sites and that phosphorylation depends on assembly of PKC and PKA by AKAP79 into a signaling complex with TRPV4. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260882 |
Thr175 |
GLLPFLLtHKKRLTD |
Homo sapiens |
|
pmid |
sentence |
19661060 |
We conclude that the serine/threonine kinases PKC and PKA enhance activation of the TRPV4 ion channel by phosphorylation at specific sites and that phosphorylation depends on assembly of PKC and PKA by AKAP79 into a signaling complex with TRPV4. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
GSK1016790A | up-regulates activity
binding
|
TRPV4 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253094 |
|
|
|
|
pmid |
sentence |
23021218 |
We next examined whether chemical activation of TRPV4 would have the opposite impact on these pathways. When added to 3T3-F442A adipocytes, the TRPV4 agonist GSK1016790A repressed the expression of mRNAs encoding Pgc1a, Ucp1, and Cox8b in a TRPV4-dependent manner (Fig- ure 2I). Taken together, these data strongly suggest that TRPV4 functions as a negative regulator of PGC1a and oxidative metabolism in white adipocytes. |
|
Publications: |
1 |
+ |
ITCH | down-regulates activity
ubiquitination
|
TRPV4 |
0.385 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272625 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
17110928 |
AIP4 ubiquitin ligase is involved in the ubiquitination of both TRPV4 and TRPC4.Ubiquitination of TRPV4 is dramatically increased by the HECT (homologous to E6-AP carboxyl terminus)-family ubiquitin ligase AIP4 without inducing degradation of this channel. Instead, AIP4 promotes the endocytosis of TRPV4 and decreases its amount at the plasma membrane. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRPV4 | down-regulates quantity by repression
transcriptional regulation
|
PPARGC1A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253095 |
|
|
Mus musculus |
Adipocyte |
pmid |
sentence |
23021218 |
TRPV4 negatively regulated the expression of PGC1α, UCP1, and cellular respiration. Additionally, it potently controlled the expression of multiple proinflammatory genes involved in the development of insulin resistance. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
OS9 | up-regulates quantity by stabilization
binding
|
TRPV4 |
0.382 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261064 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
17932042 |
Here we report that OS-9, a ubiquitously expressed endoplasmic reticulum (ER)-associated protein, interacts with the cytosolic N-terminal tail of TRPV4.Thus, OS-9 regulates the secretory transport of TRPV4 and appears to protect TRPV4 subunits from the precocious ubiquitination and ER-associated degradation. Our data suggest that OS-9 functions as an auxiliary protein for TRPV4 maturation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRPV4 | down-regulates quantity by repression
transcriptional regulation
|
UCP1 |
0.291 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253096 |
|
|
Mus musculus |
Adipocyte |
pmid |
sentence |
23021218 |
TRPV4 negatively regulated the expression of PGC1α, UCP1, and cellular respiration. Additionally, it potently controlled the expression of multiple proinflammatory genes involved in the development of insulin resistance. |
|
Publications: |
1 |
Organism: |
Mus Musculus |