+ |
PAK1 | down-regulates activity
phosphorylation
|
NET1 |
0.252 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263019 |
Ser152 |
PTPAKRRsSALWSEM |
in vitro |
|
pmid |
sentence |
15684429 |
In this work we show that the Rac/Cdc42hs-regulated protein kinase PAK1 down-regulates the activity of the RhoA-specific guanine nucleotide exchange factor NET1. Specifically, PAK1 phosphorylates NET1 on three sites in vitro: serines 152, 153, and 538. Replacement of serines 152 and 153 with glutamate residues down-regulates the activity of NET1 as an exchange factor in vitro and its ability to stimulate actin stress fiber formation in cells. Using a phospho-specific antibody that recognizes NET1 phosphorylated on serine 152, we show that PAK1 phosphorylates NET1 on this site in cells and that Rac1 stimulates serine 152 phosphorylation in a PAK1-dependent manner. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263017 |
Ser152 |
PTPAKRRsSALWSEM |
in vitro |
|
pmid |
sentence |
15684429 |
In this work we show that the Rac/Cdc42hs-regulated protein kinase PAK1 down-regulates the activity of the RhoA-specific guanine nucleotide exchange factor NET1. Specifically, PAK1 phosphorylates NET1 on three sites in vitro: serines 152, 153, and 538. Replacement of serines 152 and 153 with glutamate residues down-regulates the activity of NET1 as an exchange factor in vitro and its ability to stimulate actin stress fiber formation in cells. Using a phospho-specific antibody that recognizes NET1 phosphorylated on serine 152, we show that PAK1 phosphorylates NET1 on this site in cells and that Rac1 stimulates serine 152 phosphorylation in a PAK1-dependent manner. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263018 |
Ser539 |
LTAQRRAsTVSSVTQ |
in vitro |
|
pmid |
sentence |
15684429 |
In this work we show that the Rac/Cdc42hs-regulated protein kinase PAK1 down-regulates the activity of the RhoA-specific guanine nucleotide exchange factor NET1. Specifically, PAK1 phosphorylates NET1 on three sites in vitro: serines 152, 153, and 538. Replacement of serines 152 and 153 with glutamate residues down-regulates the activity of NET1 as an exchange factor in vitro and its ability to stimulate actin stress fiber formation in cells. Using a phospho-specific antibody that recognizes NET1 phosphorylated on serine 152, we show that PAK1 phosphorylates NET1 on this site in cells and that Rac1 stimulates serine 152 phosphorylation in a PAK1-dependent manner. |
|
Publications: |
3 |
Organism: |
In Vitro |
+ |
NET1 | up-regulates activity
guanine nucleotide exchange factor
|
RHOA |
0.825 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260561 |
|
|
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 |