Ena/Vasp homology proteins
| Ena/Vasp homology proteins | |
|---|---|
 Domain organisation of EVH proteins | |
| Identifiers | |
| Symbol | VASP/EVL |
| InterPro | IPR017354 |
| VASP tetramerisation domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 human vasp tetramerisation domain l352m | |||||||||
| Identifiers | |||||||||
| Symbol | VASP_tetra | ||||||||
| Pfam | PF08776 | ||||||||
| InterPro | IPR014885 | ||||||||
| |||||||||
ENA/VASP homology proteins or EVH proteins are a family of closely related
abl non receptor tyrosine kinase. Invertebrate animals have one Ena homologue, whereas mammals have three, named Mena, VASP, and Evl
.
Ena/VASP proteins promote the spatially regulated actin polymerization required for efficient chemotaxis in response to attractive and repulsive guidance cues. Mice lacking functional copies of all three family members display pleiotropic
formation, and embryonic lethality.A sub-domain of EVH is the
EVH1 domain
.
VASP
Vasodilator-stimulated phosphoprotein (VASP) 45-residue-long tetramerization protein domain which regulates actin dynamics in the cytoskeleton. This is vital for processes such as cell adhesion and cell migration.[2]
Function
Ena/VASP proteins are
lamellipodia, but the precise function in their formation is controversial. Ena/VASP proteins remain processively bound to growing barbed (+) ends of an actin filaments. They promote actin filament elongation both by delivering monomeric actin to the barbed (+) ends as well as protecting these ends from F-actin capping protein.[3][4]
Structure
The tetramerisation domain has a right-handed
coiled-coil structure.[5]
References
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