| + |
SCN2B | form complex 
binding
|
Nax cation channel complex, SCN1B-SCN2B variant |
0.567 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280809 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 22992729 |
Voltage-gated Na(+) channels in the brain are composed of a single pore-forming α subunit, one non-covalently linked β subunit (β1 or β3), and one disulfide-linked β subunit (β2 or β4). The final step in Na(+) channel biosynthesis in central neurons is concomitant α-β2 disulfide linkage and insertion into the plasma membrane. Consistent with this, Scn2b (encoding β2) null mice have reduced Na(+) channel cell surface expression in neurons, and action potential conduction is compromised. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCN7A | form complex
binding
|
Nax cation channel complex, SCN1B-SCN2B variant |
0.575 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280810 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 22992729 |
Voltage-gated Na(+) channels in the brain are composed of a single pore-forming α subunit, one non-covalently linked β subunit (β1 or β3), and one disulfide-linked β subunit (β2 or β4). The final step in Na(+) channel biosynthesis in central neurons is concomitant α-β2 disulfide linkage and insertion into the plasma membrane. Consistent with this, Scn2b (encoding β2) null mice have reduced Na(+) channel cell surface expression in neurons, and action potential conduction is compromised. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCN1B | form complex
binding
|
Nax cation channel complex, SCN1B-SCN2B variant |
0.634 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280811 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 22992729 |
Voltage-gated Na(+) channels in the brain are composed of a single pore-forming α subunit, one non-covalently linked β subunit (β1 or β3), and one disulfide-linked β subunit (β2 or β4). The final step in Na(+) channel biosynthesis in central neurons is concomitant α-β2 disulfide linkage and insertion into the plasma membrane. Consistent with this, Scn2b (encoding β2) null mice have reduced Na(+) channel cell surface expression in neurons, and action potential conduction is compromised. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DLG4 | up-regulates quantity 
binding
|
Nax cation channel complex, SCN1B-SCN2B variant |
0.312 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280815 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 25961826 |
Furthermore, we demonstrated that Nax bound to postsynaptic density protein 95 (PSD95) through its PSD95/Disc-large/ZO-1 (PDZ)-binding motif at the C-terminus in neurons. The interaction between Nax and PSD95 may be involved in promoting the surface expression of Nax channels because the depletion of endogenous PSD95 resulted in a decrease in Nax at the plasma membrane. These results indicated, for the first time, that Nax functions as a [Na+]-sensitive Na channel in neurons as well as in glial cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Nax cation channel complex, SCN1B-SCN2B variant | up-regulates quantity
relocalization
|
sodium(1+) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280819 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 26042603 |
Nax is a sodium-concentration ([Na+])-sensitive Na channel with a gating threshold of ~150 mM for extracellular [Na+] ([Na+]o) in vitro. We previously reported that Nax was preferentially expressed in the glial cells of sensory circumventricular organs including the subfornical organ, and was involved in [Na+] sensing for the control of salt-intake behavior. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
Nax cation channel complex, SCN1B-SCN2B variant
CPX-8694