The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin.
The vasodilator-stimulated phosphoprotein (VASP) functions as a cellular regulator of actin dynamics. VASP may initialise actin polymerisation, suggesting a direct interaction with monomeric actin. The present study demonstrates that VASP directly binds to actin monomers and that complex formation depends on a conserved four amino acid motif in the EVH2 domain. Point mutations within this motif drastically weaken VASP/G-actin interactions, thereby abolishing any actin-nucleating activity of VASP. Additionally, actin nucleation was found to depend on VASP oligomerisation since VASP monomers fail to induce the formation of actin filaments. Phosphorylation negatively affects VASP/G-actin interactions preventing VASP-induced actin filament formation.
Walders-Harbeck
Birgit
B
Cell Biology, Zoological Institute, Technical University of Braunschweig, Biocenter, Spielmannstrasse 7, D-38092 Braunschweig, Germany.
Khaitlina
Sofia Y
SY
Hinssen
Horst
H
Jockusch
Brigitte M
BM
Illenberger
Susanne
S
D000199:Actins / Q000378:metabolism*; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001704:Biopolymers; D015815:Cell Adhesion Molecules / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D003285:Contractile Proteins; D051379:Mice; D008840:Microfilament Proteins / Q000378:metabolism; D008969:Molecular Sequence Data; D010750:Phosphoproteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D010766:Phosphorylation; D017354:Point Mutation; D051304:Profilins; D011485:Protein Binding; D017386:Sequence Homology, Amino Acid; D000098662:Vasodilator-Stimulated Phosphoprotein
D000199:Actins; D001704:Biopolymers; D015815:Cell Adhesion Molecules; D003285:Contractile Proteins; D008840:Microfilament Proteins; D010750:Phosphoproteins; D051304:Profilins; D000098662:Vasodilator-Stimulated Phosphoprotein