Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity, such as axon guidance and lamellipodial and filopodial dynamics in migrating cells [, ]. Ena/VASP proteins possess a modular domain organization, including a conserved tetramerization domain (TD) mediates the formation of Ena/VASP tetramers []. In vertebrates there are three Ena-VASP family members: Mena (Mammalian enabled), VASP, and EVL (Ena-VASP like).Vasodilator-stimulated phosphoproteins (VASP) is one of the founding members of the Ena/VASP family. VASP promotes actin nucleation and increases the rate of actin polymerisation in the presence of capping protein [].
Vasodilator-stimulated phosphoprotein (VASP) is an actin cytoskeletal regulatory protein. This region corresponds to the tetramerisation domain which forms a right handed alpha helical coiled coil structure [].
Vasodilator-stimulated phosphoprotein (VASP) is an actin cytoskeletal regulatory protein. This superfamily corresponds to the tetramerisation domain which forms a right handed alpha helical coiled coil structure [].
Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity, such as axon guidance and lamellipodial and filopodial dynamics in migrating cells [, ]. Ena/VASP proteins possess a modular domain organization, including a conserved tetramerization domain (TD) mediates the formation of Ena/VASP tetramers []. In vertebrates there are three Ena-VASP family members: Mena (Mammalian enabled), VASP, and EVL (Ena-VASP like).This entry includes VASP and Ena/VASP-like (EVL) proteins.
Palladin is a cytoskeletal actin scaffold protein that regulates actin dynamics. The immunoglobulin-like domain of palladin is directly responsible for both actin binding and bundling [, ]. Palladin also interacts with different actin binding proteins and signalling intermediaries required for regulation of cytoskeleton organisation, including profilin [], VASP [], Eps8 [], ezrin [], Lasp-1 [], and Src []. Palladin plays an important role in smooth and skeletal muscle differentiation [, , ], contraction []and cell migration [, , ].Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions []. This entry represents the C-terminal immunoglobulin-like domain (Ig5).
Pleckstrin homology (PH) domains are small modular domains that occur in a large variety of signalling proteins, where they serve as simple targeting domains that bind lipids [, , ]. PH domains have a partly opened β-barrel topology that is capped by an alpha helix. The structure of PH domains is similar to the phosphotyrosine-binding domain (PTB) found in IRS-1 (insulin receptor substrate 1) [], Shc adaptor and Numb []; to the Ran-binding domain, found in Nup nuclear pore complex and Ranbp1 []; to the Enabled/VASP homology domain 1 (EVH1 domain), found in Enabled, VASP (vasodilator-stimulated phosphoprotein), Homer and WASP actin regulatory protein []; and to the third domain of FERM, found in moesin, radixin, ezrin, merlin and talin [].This superfamily represents the PH domain and structurally related domains.
