High impact information on VASP

• These data indicate that the C-terminal domain is required for anchoring VASP at focal adhesion sites, whereas the central domain is suggested to mediate VASP interaction with profilin [1].
• VASP over-expressed in transiently transfected BHK21 cells was predominantly detected at stress fibres, at focal adhesions and in F-actin-containing cell surface protrusions, whereas truncated VASP lacking the C-terminal domain was no longer concentrated at focal adhesions [1].
• Our results provide evidence for the structural basis by which VASP, both a target of the cAMP and cGMP signal transduction pathways and a component of the actin-based cytoskeleton, including the cytoskeleton-membrane interface, may be able to exchange signals between these networks [1].
• Previous work implicated VASP in assembly of cell-cell junctions in keratinocytes and the VASP-binding protein zyxin colocalizes with VASP at cell-cell junctions [2].
• ATP led to rapid activation of cAMP-dependent protein kinase A (PKA), as estimated by phosphorylation of a vasodilator-stimulated phosphoprotein [3].

Biological context of VASP

• Here, we describe different procedures we used to demonstrate that Rab13 interacts with PKA and reversibly controls phosphorylation and recruitment of VASP [4].

Anatomical context of VASP

• The inhibition of VASP phosphorylation abolishes the targeting of VASP to cell-cell junctions, which in turn leads to a delay in the recruitment of claudin1 and ZO1 into tight junctions [4].
• Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP [1].

References