+ |
ERK1/2 | up-regulates activity
phosphorylation
|
CACNB1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262966 |
Ser161 |
CEVGFIPsPVKLDSL |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
16406008 |
Thus, Ser-447 on Ca(v)2.2 and Ser-161 and Ser-348 of Ca(v)beta1b appear to be both necessary and sufficient for ERK-dependent modulation of these channels. Together, our data strongly suggest that modulation of neuronal N-type VDCCs by ERK involves phosphorylation of Ca(v)2.2alpha1 and to a lesser extent possibly also Ca(v)beta subunits. On the basis of the evidence presented here, it is therefore suggested that ERK-dependent up-regulation of Cav2.2 channels is primarily mediated by phosphorylation of Ser-447 on the I–II loop of Cav2.2 and possibly also the two SP sites conserved on Cavβs. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262965 |
Ser348 |
IVYIKITsPKVLQRL |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
16406008 |
Thus, Ser-447 on Ca(v)2.2 and Ser-161 and Ser-348 of Ca(v)beta1b appear to be both necessary and sufficient for ERK-dependent modulation of these channels. Together, our data strongly suggest that modulation of neuronal N-type VDCCs by ERK involves phosphorylation of Ca(v)2.2alpha1 and to a lesser extent possibly also Ca(v)beta subunits. On the basis of the evidence presented here, it is therefore suggested that ERK-dependent up-regulation of Cav2.2 channels is primarily mediated by phosphorylation of Ser-447 on the I–II loop of Cav2.2 and possibly also the two SP sites conserved on Cavβs. |
|
Publications: |
2 |
Organism: |
Chlorocebus Aethiops |