+ |
FYN | up-regulates activity
phosphorylation
|
TRIO |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273855 |
Tyr2681 |
LLNPNYIyDVPPEFV |
in vitro |
|
pmid |
sentence |
23230270 |
Here, we demonstrate that Trio is phosphorylated by Src family kinases in the embryonic rat cortex in response to netrin-1. In vitro, Trio was predominantly phosphorylated at Tyr(2622) by the Src kinase Fyn. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PTK2 | up-regulates activity
phosphorylation
|
TRIO |
0.487 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249188 |
Tyr2796 |
KDNFDSFySEVAELG |
Chlorocebus aethiops |
|
pmid |
sentence |
12551902 |
A FAK phosphorylation site, tyrosine residue 2737, was identified in subdomain I of the Trio kinase domain. Additionally, in vitro phosphorylation assays and in vivo co-expression studies indicated that Trio enhances FAK kinase activity. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
TRIO | up-regulates quantity
binding
|
DCC |
0.587 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273856 |
|
|
Rattus norvegicus |
Cerebral Cortical Neuron |
pmid |
sentence |
23230270 |
TrioY2622 is required for both netrin-1-induced activation of Rac1 and enhanced association with DCC. Phosphorylation of Trio at Tyr2622 participates in maintaining the level of surface DCC at the growth cone plasma membrane leading to axon outgrowth. Therefore, we propose that TrioY2622 is essential for the proper assembly and stability of the DCC/Trio signaling complex at the cell surface of growth cones in order to mediate netrin-1-induced cortical axon outgrowth. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
TRIO | up-regulates activity
guanine nucleotide exchange factor
|
RAC1 |
0.678 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260579 |
|
|
Homo sapiens |
|
pmid |
sentence |
32203420 |
We therefore developed a screening-compatible live-cell imaging assay, using FRET-based biosensors for the prototype GTPases RHOA, RAC1 and CDC4215,19,20 (Extended Data Fig. 2 and Supplementary Note 1)|We found catalytic activities for 45/75 RhoGEFs and 48/63 RhoGAPs| Our data thus not only reveal extensive promiscuity among regulators, but also that the inactivating RhoGAPs are less selective than the activating RhoGEFs (p-value=0.02)(Supplementary Table 2). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |