| + |
MTOR | up-regulates activity 
phosphorylation
|
LARP6 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273679 |
Ser348 |
DPESNPTsPMAGRRH |
Rattus norvegicus |
Hepatic Stellate Cell |
| pmid |
sentence |
| 28112218 |
Binding of La ribonucleoprotein domain family, member 6 (LARP6) to collagen mRNAs regulates their translation and is necessary for high type I collagen expression. Here we show that mTORC1 phosphorylates LARP6 on S348 and S409. The S348A/S409A mutant of LARP6 acts as a dominant negative protein in collagen biosynthesis, which retards secretion of type I collagen and causes excessive posttranslational modifications. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273678 |
Ser409 |
GRLNCSTsPEIFRKC |
Rattus norvegicus |
Hepatic Stellate Cell |
| pmid |
sentence |
| 28112218 |
Binding of La ribonucleoprotein domain family, member 6 (LARP6) to collagen mRNAs regulates their translation and is necessary for high type I collagen expression. Here we show that mTORC1 phosphorylates LARP6 on S348 and S409. The S348A/S409A mutant of LARP6 acts as a dominant negative protein in collagen biosynthesis, which retards secretion of type I collagen and causes excessive posttranslational modifications. |
|
| Publications: |
2 |
Organism: |
Rattus Norvegicus |
| + |
AKT | up-regulates activity
phosphorylation
|
LARP6 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273539 |
Ser451 |
QEKSPGTsPLLSRKM |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26932461 |
This strongly suggested that Akt dependent phosphorylation of LARP6 targets S451.S451A mutant of LARP6 acts as dominant negative protein in collagen synthesis. these results support the hypothesis that phosphorylation of S451 by Akt is a necessary step to activate productive synthesis type I collagen and suggests that secretion and modifications of type I collagen are impaired if LARP6 is not phosphorylated on S451. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT1 | up-regulates activity
phosphorylation
|
LARP6 |
0.361 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277213 |
Ser451 |
QEKSPGTsPLLSRKM |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26932461 |
Akt dependent phosphorylation of LARP6. We provide the first description that LARP6 is phosphorylated at multiple sites and that phosphorylation of S451 is critical to activate the protein in type I collagen biosynthesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VIM | up-regulates activity
binding
|
LARP6 |
0.275 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277624 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21746880 |
Interaction of LARP6 with vimentin.Here, we report that vimentin filaments associate with collagen mRNAs in a 5'SL- and LARP6-dependent manner and stabilize collagen mRNAs. LARP6 interacts with vimentin filaments through its La domain and colocalizes with the filaments in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LARP6 | up-regulates activity
binding
|
DHX9 |
0.42 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273500 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22190748 |
La ribonucleoprotein domain family member 6 (LARP6) is the protein that binds 5' SL with high affinity and specificity and coordinates their translation. Here we show that RNA helicase A (RHA) is tethered to the 5' SL of collagen mRNAs by interaction with the C-terminal domain of LARP6. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
LARP6
- 
- 