Molecular cloning, structural analysis and functional expression of the proline‐rich focal adhesion and microfilament‐associated protein VASP.

@article{Haffner1995MolecularCS,
  title={Molecular cloning, structural analysis and functional expression of the proline‐rich focal adhesion and microfilament‐associated protein VASP.},
  author={C. Haffner and T. Jarchau and M. Reinhard and J. Hoppe and S. Lohmann and U. Walter},
  journal={The EMBO Journal},
  year={1995},
  volume={14}
}
The vasodilator‐stimulated phosphoprotein (VASP), a substrate for cAMP‐ and cGMP‐dependent protein kinases in vitro and in intact cells, is associated with actin filaments, focal adhesions and dynamic membrane regions. VASP, cloned here from human HL‐60 and canine MDCK cells, is organized into three distinct domains. A central proline‐rich domain contains a GPPPPP motif as a single copy and as a 3‐fold tandem repeat, as well as three conserved phosphorylation sites for cyclic nucleotide… Expand
Ligand recruitment by vinculin domains in transfected cells.
Zyxin: Zinc fingers at sites of cell adhesion
  • M. Beckerle
  • Biology, Medicine
  • BioEssays : news and reviews in molecular, cellular and developmental biology
  • 1997
Structural and functional characterization of the focal adhesion protein FAP52
LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity.
The focal adhesion phosphoprotein, VASP.
...
1
2
3
4
5
...

References

SHOWING 1-3 OF 3 REFERENCES
Advances in molecular and cell biology
Proline-rich focal adhesion protein VASP Luna,E.J. and Hitt,A.L
  • J. MoI. Biol.,
  • 1992
Protein kinases.