+ |
STK33 | down-regulates quantity by destabilization
phosphorylation
|
HPD |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272958 |
Thr382 |
QNLRGNLtNMETNGV |
Mus musculus |
Hippocampal Cell Line |
pmid |
sentence |
31537781 |
Decreased expression of 4-hydroxyphenylpyruvic acid dioxygenase (HPD), a key enzyme for tyrosine metabolism, is a cause of human tyrosinemia. However, the regulation of HPD expression remains largely unknown. Here, we demonstrate that molecular chaperone TTC36, which is highly expressed in liver, is associated with HPD and reduces the binding of protein kinase STK33 to HPD, thereby inhibiting STK33-mediated HPD T382 phosphorylation. The reduction of HPD T382 phosphorylation results in impaired recruitment of FHA domain-containing PELI1 and PELI1-mediated HPD polyubiquitylation and degradation. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
PELI1 | down-regulates quantity by destabilization
ubiquitination
|
HPD |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272959 |
|
|
Mus musculus |
Hippocampal Cell Line |
pmid |
sentence |
31537781 |
Decreased expression of 4-hydroxyphenylpyruvic acid dioxygenase (HPD), a key enzyme for tyrosine metabolism, is a cause of human tyrosinemia. However, the regulation of HPD expression remains largely unknown. Here, we demonstrate that molecular chaperone TTC36, which is highly expressed in liver, is associated with HPD and reduces the binding of protein kinase STK33 to HPD, thereby inhibiting STK33-mediated HPD T382 phosphorylation. The reduction of HPD T382 phosphorylation results in impaired recruitment of FHA domain-containing PELI1 and PELI1-mediated HPD polyubiquitylation and degradation. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
TTC36 | up-regulates quantity by stabilization
binding
|
HPD |
0.273 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272960 |
|
|
Mus musculus |
Hippocampal Cell Line |
pmid |
sentence |
31537781 |
Decreased expression of 4-hydroxyphenylpyruvic acid dioxygenase (HPD), a key enzyme for tyrosine metabolism, is a cause of human tyrosinemia. However, the regulation of HPD expression remains largely unknown. Here, we demonstrate that molecular chaperone TTC36, which is highly expressed in liver, is associated with HPD and reduces the binding of protein kinase STK33 to HPD, thereby inhibiting STK33-mediated HPD T382 phosphorylation. The reduction of HPD T382 phosphorylation results in impaired recruitment of FHA domain-containing PELI1 and PELI1-mediated HPD polyubiquitylation and degradation. |
|
Publications: |
1 |
Organism: |
Mus Musculus |