+ |
PKA | down-regulates quantity by destabilization
phosphorylation
|
KCNA4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276037 |
Thr601 |
LKKFRSStSSSLGDK |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
15955806 |
In parallel experiments, it was shown that recombinant PKA catalytic subunits (Fig. 3A) or cell extracts from GIP-stimulated GIPR-HEK293-KV cells (Fig. 3B) increased phosphorylation of KV1.4, and active PKA phosphorylated Thr-601 in the C terminus of KV1.4 (Fig. 3D). These results therefore provide compelling evidence for a role for GIP-induced down-regulation of KV1.4, via phosphorylation-dependent endocytosis of the channel protein, in the modulation of insulin secretion. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PKA | down-regulates activity
phosphorylation
|
KCNA4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273778 |
Thr601 |
LKKFRSStSSSLGDK |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
15955806 |
In GIP receptor-expressing HEK293 cells, GIP reduced A-type peak ionic current amplitude of K(V)1.4 via activation of protein kinase A (PKA). Using mutant forms of K(V)1.4 with Ala-Ser/Thr substitutions in a potential PKA phosphorylation site, C-terminal phosphorylation was shown to be linked to GIP-mediated current amplitude decreases. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LNX1 | down-regulates quantity by destabilization
ubiquitination
|
KCNA4 |
0.286 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272899 |
|
|
in vitro |
|
pmid |
sentence |
22889411 |
We used the Ligand of Numb protein X (LNX) family of E3s, a group of PDZ domain-containing RING-type E3 ubiquitin ligases, to demonstrate the feasibility of this strategy. Many potential substrates of LNX E3s were identified. Eight of the nine selected candidates were ubiquitinated in vitro, and two novel endogenous substrates, PDZ-binding kinase (PBK) and breakpoint cluster region protein (BCR), were confirmed in vivo.The C-terminal LNX1 PDZ1-binding motifs of the ATP-binding cassette, subfamily A member 1 (ABC-1), PBK, glutamate receptor, ionotropic, N-methyl d-aspartate 1 (GRIN1), and Claudin-17 significantly promoted the ubiquitination of the corresponding artificial degrons by LNX1ΔPDZ234. |
|
Publications: |
1 |
Organism: |
In Vitro |