| 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 proteins involved in cell motility in vertebrate and invertebrate animals. EVH proteins are modular proteins that are involved in actin polymerization, as well as interactions with other proteins. Within the cell, ENA/VASP proteins are found at the leading edge of lamellipodia and at the tips of filopodia.[1] ENA, the founding member of the family, was discovered in a fruit fly genetic screen for mutations that act as dominant suppressors of the AB 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 phenotypes including exencephaly, edema, failures in neurite formation, and embryonic lethality.
A sub-domain of EVH is the EVH1 domain.
- ^ Bear and Gertler; Gertler, FB (2009). "Ena/VASP: towards resolving a controversy at the barbed end". J Cell Sci. 122 (Pt 12): 1947–53. doi:10.1242/jcs.038125. PMC 2723151. PMID 19494122.