Reference : Characterization of the interaction between zyxin and members of the Ena/vasodilator-...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins.
Drees, B. [> >]
Friederich, Evelyne mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >]
Fradelizi, J. [> >]
Louvard, D. [> >]
Beckerle, M. C. [> >]
Golsteyn, R. M. [> >]
The Journal of biological chemistry
Yes (verified by ORBilu)
[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.

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