+ |
CSNK2A1 | down-regulates activity
phosphorylation
|
G3BP1 |
0.241 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260748 |
Ser149 |
VTEPQEEsEEEVEEP |
Homo sapiens |
U2-OS Cell |
pmid |
sentence |
27920254 |
We also show that casein kinase 2 phosphorylates G3BP1 at serine 149 in vitro and in cells. These data support a role for casein kinase 2 in regulation of protein synthesis by downregulating stress granule formation through G3BP1.CK2 regulates SG disassembly during stress recovery.G3BP1 is among the strongest SG nucleating proteins, and previous work indicated that G3BP1 phosphorylation at S149 restricts stress granule assembly by partly inhibiting G3BP1 oligomerization |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, SARS-CoV STRESS GRANULES |
+ |
G3BP1 | up-regulates activity
binding
|
EIF2AK2 |
0.312 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260750 |
|
|
Homo sapiens |
|
pmid |
sentence |
25520508 |
We show that G3BP1 can activate effectors of the innate immune transcriptional program, culminating in enhanced expression of a set of cytokines. We demonstrate that a subset of PKR is recruited to SGs, that close-proximity interactions between G3BP1 and PKR complexes increase in response to stress and PKR activation, that once activated PKR no longer associates with SGs, and that the PXXP domain of G3BP1 is essential for PKR recruitment to SGs and PKR activation in cells. Together, these findings suggest that G3BP1 plays an important role in the recruitment of PKR to SGs and suggest that activation of PKR can take place at the SG. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260981 |
|
|
Homo sapiens |
U2-OS Cell, HeLa Cell |
pmid |
sentence |
25784705 |
PKR directly interacts with G3BP1 through the NTF2-like and PXXP domains of G3BP1. The recruitment of inactive PKR to SGs through this interaction correlates with its activation |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Innate Immune Response, SARS-CoV STRESS GRANULES |
+ |
G3BP1 | up-regulates
|
Stress_granules |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260984 |
|
|
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
23279204 |
G3BP1 and G3BP2 form homo‐ and hetero‐multimers to induce SGs |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260747 |
|
|
Homo sapiens |
|
pmid |
sentence |
25520508 |
Ras-GTPase-activating protein (SH3 domain) binding protein 1 (G3BP1) is a stress granule-resident protein that nucleates stress granule assembly and is also inactivated or coopted by many viruses to promote productive infection |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Innate Immune Response, SARS-CoV STRESS GRANULES |
+ |
N | down-regulates activity
binding
|
G3BP1 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260749 |
|
|
Homo sapiens |
|
pmid |
sentence |
32353859 |
N targets stress granule protein G3BP1, an essential antiviral protein which is known to induce innate immune response through multiple mechanisms |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, SARS-CoV STRESS GRANULES |
+ |
G3BP2 | up-regulates activity
binding
|
G3BP1 |
0.469 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260863 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
23279204 |
Ras-GTPase-activating protein SH3 domain-binding protein 1 (G3BP1) is a component of SGs that initiates the assembly of SGs by forming a multimer. In this study, we examined the role of G3BP2, a close relative of G3BP1, in SG formation. Although single knockdown of either G3BP1 or G3BP2 in 293T cells partially reduced the number of SG-positive cells induced by arsenite, the knockdowns of both genes significantly reduced the number. G3BP2 formed a homo-multimer and a hetero-multimer with G3BP1. Moreover, like G3BP1, the overexpression of G3BP2 induced SGs even without stress stimuli. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Innate Immune Response, SARS-CoV STRESS GRANULES |
+ |
G3BP1 | up-regulates quantity
|
DDX58 |
0.346 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261319 |
|
|
Homo sapiens |
|
pmid |
sentence |
31827077 |
We further identified that G3BP1 is able to interact with RIG-I and boost its expression. RIG-I expression could be stabilized by G3BP1 via antagonizing RNF125-mediated RIG-I degradation. Secondly, we demonstrated that G3BP1 potentiates the self-association and auto-ubiquitination of RNF125. Hence, it is more likely that G3BP1 first promotes RNF125 degradation by enhancing self-association and auto-ubiquitination of RNF125, and then RIG-I degradation mediated by RNF125 is alleviated |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Innate Immune Response, SARS-CoV STRESS GRANULES |
+ |
Viral_dsRNA | up-regulates activity
binding
|
G3BP1 |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260979 |
|
|
|
|
pmid |
sentence |
30804210 |
The RGG domain of G3BP1 could mediate the direct binding of HCV-dsRNA and poly(IC) |
|
Publications: |
1 |
Pathways: | COVID-19 Causal Network, Innate Immune Response, SARS-CoV STRESS GRANULES |
+ |
G3BP1 | up-regulates activity
binding
|
G3BP2 |
0.469 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260862 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
23279204 |
Ras-GTPase-activating protein SH3 domain-binding protein 1 (G3BP1) is a component of SGs that initiates the assembly of SGs by forming a multimer. In this study, we examined the role of G3BP2, a close relative of G3BP1, in SG formation. Although single knockdown of either G3BP1 or G3BP2 in 293T cells partially reduced the number of SG-positive cells induced by arsenite, the knockdowns of both genes significantly reduced the number. G3BP2 formed a homo-multimer and a hetero-multimer with G3BP1. Moreover, like G3BP1, the overexpression of G3BP2 induced SGs even without stress stimuli. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Innate Immune Response, SARS-CoV STRESS GRANULES |
+ |
CAPRIN1 | up-regulates activity
binding
|
G3BP1 |
0.608 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260982 |
|
|
Homo sapiens |
|
pmid |
sentence |
17210633 |
Caprin-1 and G3BP-1 were directly or indirectly associated in a stable complex. The Caprin-1/G3BP-1 complex occurs in cytoplasmic RNA granules |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PARP10 | up-regulates activity
post translational modification
|
G3BP1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273727 |
|
|
Homo sapiens |
U2-OS Cell |
pmid |
sentence |
37873303 |
Further, we pinpoint the core SG component, G3BP1, as a PARP10 substrate and find that PARP10 regulates SG assembly driven by both G3BP1 and its modeled mechanism. Intriguingly, while PARP10 only adds a single ADP-ribose unit to proteins, G3BP1 is PARylated, suggesting its potential role as a scaffold for protein recruitment. PARP10 knockdown alters the SG core composition, notably decreasing translation factor presence. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
G3BP1 | down-regulates activity
binding
|
DDX58 |
0.346 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260980 |
|
|
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
30804210 |
G3BP1 binds RIG-I and that this interaction involves the C-terminal RGG domain of G3BP1, G3BP1 significantly enhances RIG-I-induced ifn-b mRNA synthesis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Innate Immune Response, SARS-CoV STRESS GRANULES |