+ |
PRKCB | down-regulates activity
phosphorylation
|
TRPV6 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276265 |
Ser184 |
LARRASVsARATGTA |
in vitro |
|
pmid |
sentence |
19805577 |
This regulation requires PKC(betaII) and defined phosphorylation sites within the ARD and the C-terminus. Both regulatory sites act synergistically to constitute a novel mechanism by which ATP stabilizes channel activity and acts as a metabolic switch for Ca(2+) influx. Decreases in ATP concentration or activation of PKC(betaII) disable regulation of the channels by ATP, rendering them more susceptible to inactivation and rundown and preventing Ca(2+) overload. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276266 |
Thr728 |
MPSVSRStSRSSANW |
in vitro |
|
pmid |
sentence |
19805577 |
This regulation requires PKC(betaII) and defined phosphorylation sites within the ARD and the C-terminus. Both regulatory sites act synergistically to constitute a novel mechanism by which ATP stabilizes channel activity and acts as a metabolic switch for Ca(2+) influx. Decreases in ATP concentration or activation of PKC(betaII) disable regulation of the channels by ATP, rendering them more susceptible to inactivation and rundown and preventing Ca(2+) overload. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
PTPN1 | down-regulates
dephosphorylation
|
TRPV6 |
0.615 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-151711 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
17197020 |
We conclude that phosphorylation/dephosphorylation of tyrosines in position 161 and 162 is essential for regulation of ca2+ influx through trpv6 ca2+ channels in hek293 cells. Co-transfection with src led to tyrosine phosphorylation of trpv6 which could be dephosphorylated by ptp1b. y161/162 are essential for tyrosine phosphorylation-dependent modulation of trpv6-mediated ca2+ entry. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPN1 | down-regulates activity
dephosphorylation
|
TRPV6 |
0.615 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248433 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
17197020 |
In HEK293 cells, transfected with the Ca2+ channel protein TRPV6, Ca2+ influx is increased and TRPV6 is tyrosine phosphorylated following addition of the tyrosine phosphatase inhibitor|PTP1B interacts with the N-terminal domain of TRPV6 within a region of amino acids 1-191 as shown by co-immunoprecipitation, bimolecular fluorescence complementation and the yeast 2-hybrid system. Point mutation of both tyrosines 161 and 162 in the TRPV6 protein abolishes the DMHV-effect on Ca2+ influx and tyrosine phosphorylation by Src. Single mutations of Y161 or Y162 shows that each of both tyrosines alone is sufficient for the DMHV-effect. We conclude that phosphorylation/dephosphorylation of tyrosines in position 161 and 162 is essential for regulation of Ca2+ influx through TRPV6 Ca2+ channels in HEK293 cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |