| Reference : Characterization of the interaction between zyxin and members of the Ena/vasodilator-... |
| Scientific journals : Article | |||
| Life sciences : Biochemistry, biophysics & molecular biology | |||
| http://hdl.handle.net/10993/6280 | |||
| Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins. | |
| English | |
| Drees, B. [> >] | |
Friederich, Evelyne  [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >] | |
| Fradelizi, J. [> >] | |
| Louvard, D. [> >] | |
| Beckerle, M. C. [> >] | |
| Golsteyn, R. M. [> >] | |
| 2000 | |
| The Journal of biological chemistry | |
| 275 | |
| 29 | |
| 22503-11 | |
| Yes (verified by ORBilu) | |
| International | |
| 0021-9258 | |
| UNITED STATES | |
| [en] Amino Acid Sequence ; Cell Adhesion Molecules/genetics/metabolism ; Cytoskeletal Proteins ; Glycoproteins ; Humans ; Listeria monocytogenes ; Metalloproteins/genetics/metabolism ; Microfilament Proteins ; Molecular Sequence Data ; Mutation ; Phosphoproteins/genetics/metabolism ; Proline ; Protein Binding ; Zyxin | |
| [en] Zyxin contains a proline-rich N-terminal domain that is similar to the C-terminal domain in the ActA protein of the bacteria, Listeria monocytogenes. We screened the entire amino acid sequence of human zyxin for Mena-interacting peptides and found that, as with ActA, proline-rich sequences were the sole zyxin sequences capable of binding to Ena/vasodilator-stimulated phosphoprotein (VASP) family members in vitro. From this information, we tested zyxin mutants in which the proline-rich sequences were altered. The reduction in Mena/VASP binding was confirmed by peptide tests, immunoprecipitation, and ectopic expression of zyxin variants at the surface of mitochondria. By transfection assays we showed that zyxin interaction with Mena/VASP in vivo enhances the production of actin-rich structures at the apical surface of cells. Microinjection into cells of peptides corresponding to the first proline-rich sequence of zyxin caused the loss of Mena/VASP from focal contacts. Furthermore, these peptides reduced the degree of spreading of cells replated after trypsinization. We conclude that zyxin and proteins that harbor similar proline-rich repeats contribute to the positioning of Mena/VASP proteins. The positioning of Ena/VASP family members appears to be important when the actin cytoskeleton is reorganized, such as during spreading. | |
| http://hdl.handle.net/10993/6280 | |
| 10.1074/jbc.M001698200 |
There is no file associated with this reference.
All documents in ORBilu are protected by a user license.
