EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.6.5.2 | lipoprotein |
- |
644127 |
| 3.6.5.2 | lipoprotein |
the C-terminus of RhoGTPases comprises, next to the hypervariable region, the CAAX-box to which a lipid anchor is attached allowing GTPase binding to membranes. RhoA, RhoB and RhoC differ in this posttranslational lipid modification which has consequences for their subcellular localization. The lipid anchor regulates the interaction with RhoGDIs and with regions within the plasma membrane (RhoA, RhoC) or endosomal vesicles (RhoB). RhoA and RhoC are geranylgeranylated, whereas RhoB has both a palmitoyl anchor and a farnesyl or geranylgeranyl group |
735276 |
| 3.6.5.2 | lipoprotein |
the enzyme is N-myristoylated |
735220 |
| 3.6.5.2 | lipoprotein |
Wrch-1 undergoes posttranslational lipid modification |
670139 |
| 3.6.5.2 | more |
Arf-like 3 is N-terminally acetylated |
688798 |
| 3.6.5.2 | more |
small GTPases are modified by isoprenylation of the cysteine of the CAAX box, cleavage of the AAX tripeptide, and methylation of the cysteine, isoprenylation and the endoproteolytic cleavage of the tripeptide of Rho GTPases are essential for YopT-induced cleavage, whereas carboxyl methylation is not required |
701098 |
| 3.6.5.2 | more |
the CKIF motif in human RhoH is a target for the in vitro modification by farnesyl-transferase and geranylgeranyl-transferase |
697169 |
| 3.6.5.2 | more |
the CKIF motif in mouse RhoH is a target for the in vitro modification by farnesyl-transferase and geranylgeranyl-transferase |
697169 |
| 3.6.5.2 | phosphoprotein |
PKA- and PKG-mediated phosphorylation of RhoA on Ser188, which is located in the hypervariable C-terminus. This phosphorylation serves as a Rho-inactivating signal, as it promotes GDI binding and membrane dissociation and protects RhoA from proteolytic degradation. In addition, this phosphorylation interferes with RhoA binding to ROCK further underscoring a role of the C-terminus in effector interactions |
735276 |
| 3.6.5.2 | phosphoprotein |
RhoC, but not RhoA, is phosphorylated on Ser73 in the alpha2-helix by the kinase Akt in SUM149 breast cancer cells54 although Ser73 is highly conserved among all 3 Rho-isoforms. Intriguingly, phosphorylation of RhoC is required for downstream signaling and invasiveness, which contrasts markedly with the inactivating phosphorylation at Ser188 in RhoA |
735276 |
