+ |
PAK1 | down-regulates
phosphorylation
|
ARHGDIA |
0.595 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-126650 |
Ser101 |
LESFKKQsFVLKEGV |
Homo sapiens |
|
pmid |
sentence |
15225553 |
Pak1 binds and phosphorylates rhogdi both in vitro and in vivo at ser101 and ser174. This resulted in dissociation of rac1-rhogdi, but not rhoa-rhogdi, complexes, as determined by in vitro assays of complexation and in vivo by coimmunoprecipitation analysis. We observed that cdc42-induced rac1 activation is inhibited by expression of pak1 autoinhibitory domain. The dissociation of rac1 from rhogdi and its subsequent activation stimulated by pdgf or egf is also attenuated by pak1 autoinhibitory domain, and this is dependent on the ability of rhogdi to be phosphorylated at ser101/174. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-126654 |
Ser174 |
KGMLARGsYSIKSRF |
Homo sapiens |
|
pmid |
sentence |
15225553 |
Pak1 binds and phosphorylates rhogdi both in vitro and in vivo at ser101 and ser174. This resulted in dissociation of rac1-rhogdi, but not rhoa-rhogdi, complexes, as determined by in vitro assays of complexation and in vivo by coimmunoprecipitation analysis. We observed that cdc42-induced rac1 activation is inhibited by expression of pak1 autoinhibitory domain. The dissociation of rac1 from rhogdi and its subsequent activation stimulated by pdgf or egf is also attenuated by pak1 autoinhibitory domain, and this is dependent on the ability of rhogdi to be phosphorylated at ser101/174. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PRKACA | down-regulates
phosphorylation
|
ARHGDIA |
0.364 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-180576 |
Ser174 |
KGMLARGsYSIKSRF |
Homo sapiens |
|
pmid |
sentence |
18768928 |
The results indicate that phosphorylation of gdi_ at ser174 by pka suppresses rhoa activity, providing a potential protective signaling mechanism for inflammatory injury. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SRC | down-regulates
phosphorylation
|
ARHGDIA |
0.41 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-149282 |
Tyr156 |
YGPRAEEyEFLTPVE |
Homo sapiens |
|
pmid |
sentence |
16943322 |
We show here that src kinase binds and phosphorylates rhogdi both in vitro and in vivo at tyr156. analysis of rho gtpase-rhogdi complexes using in vitro assays of complexation and in vivo by coimmunoprecipitation analysis indicates that src-mediated phosphorylation of tyr156 causes a dramatic decrease in the ability of rhogdi to form a complex with rhoa, rac1, or cdc42. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Axon guidance |
+ |
RNF128 | up-regulates quantity by stabilization
polyubiquitination
|
ARHGDIA |
0.27 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271622 |
|
|
Homo sapiens |
JURKAT Cell |
pmid |
sentence |
17114425 |
We found that RhoGDIα and RhoGDIβ are ubiquitin E3 substrates of GRAIL. GRAIL uses nonlysine 48-ubiquitin linkage in polyubiquitinating RhoGDI. GRAIL was subsequently demonstrated to bind and ubiquitinate RhoGDI, although GRAIL-mediated ubiquitination of RhoGDI did not result in proteosomal degradation. Our data suggest that ubiquitination of RhoGDI by GRAIL does not result in proteolytic degradation. In fact, GRAIL activity appeared to increase RhoGDI stability. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ARHGDIA | down-regulates activity
guanine nucleotide exchange factor
|
RAC1 |
0.804 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268436 |
|
|
Rattus norvegicus |
Glioma Cell |
pmid |
sentence |
20696765 |
Here, we report the expression of plexin-B3 in glioma cells, which upon stimulation by its ligand Sema5A results in significant inhibition of cell migration and invasion. A search for the underlying mechanism revealed direct interaction of plexin-B3 with RhoGDP dissociation inhibitor α (RhoGDIα), a negative regulator of RhoGTPases that blocks guanine nucleotide exchange and sequesters them away from the plasma membrane. direct interaction of RhoGDIα and the cytoplasmic domain of plexin-B3 (plexin-B3CD) was confirmed by GST pulldown assays.RhoGDIα is required for Sema5A-induced Rac1 inactivation and inhibition of cell invasion in C6 glioma. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
Pathways: | Axon guidance |
+ |
PTPN12 | up-regulates activity
dephosphorylation
|
ARHGDIA |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277175 |
|
|
Homo sapiens |
|
pmid |
sentence |
25666508 |
Integrin-bound PTP-PEST dephosphorylates RhoGDI1.|Translocation of Src phosphorylated RhoGDI1 to the cell 's leading edge promotes local activation of Rac1 and Cdc42, whereas dephosphorylation of RhoGDI1 by integrin bound PTP-PEST promotes RhoGDI1 release from the membrane and sequestration of inactive Rac1 and Cdc42 in the cytoplasm.|Translocation of Src-phosphorylated RhoGDI1 to the cell's leading edge promotes local activation of Rac1 and Cdc42, whereas dephosphorylation of RhoGDI1 by integrin-bound PTP-PEST promotes RhoGDI1 release from the membrane and sequestration of inactive Rac1/Cdc42 in the cytoplasm. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PLXNB3 | up-regulates activity
binding
|
ARHGDIA |
0.253 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268435 |
|
|
Rattus norvegicus |
Glioma Cell |
pmid |
sentence |
20696765 |
Here, we report the expression of plexin-B3 in glioma cells, which upon stimulation by its ligand Sema5A results in significant inhibition of cell migration and invasion. A search for the underlying mechanism revealed direct interaction of plexin-B3 with RhoGDP dissociation inhibitor α (RhoGDIα), a negative regulator of RhoGTPases that blocks guanine nucleotide exchange and sequesters them away from the plasma membrane. direct interaction of RhoGDIα and the cytoplasmic domain of plexin-B3 (plexin-B3CD) was confirmed by GST pulldown assays. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
Pathways: | Axon guidance |