Mena, a relative of VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics.
Drosophila Enabled is required for proper formation of axonal structures and is genetically implicated in signaling pathways mediated by Drosophila AbI. We have identified two murine proteins, Mena and Evl, that are highly related to Enabled as well as VASP (Vasodilator-Stimulated Phosphoprotein). A conserved domain targets Mena to localized proteins ... containing a specific proline-rich motif. The association of Mena with the surface of the intracellular pathogen Listeria monocytogenes and the G-actin binding protein profilin suggests that this molecule may participate in bacterial movement by facilitating actin polymerization. Expression of neural-enriched isoforms of Mena in fibroblasts induces the formation of abnormal F-actin-rich outgrowths, supporting a role for this protein in microfilament assembly and cell motility.
Mesh Terms:
Actins, Amino Acid Sequence, Animals, Carrier Proteins, Cell Adhesion Molecules, Contractile Proteins, Cytoskeletal Proteins, DNA-Binding Proteins, Fluorescent Antibody Technique, Indirect, Ligands, Listeria monocytogenes, Mice, Microfilament Proteins, Microfilaments, Molecular Sequence Data, Phosphoproteins, Phosphorylation, Profilins, Proteins, Rats, Sequence Alignment, Sequence Homology, Amino Acid, src Homology Domains
Actins, Amino Acid Sequence, Animals, Carrier Proteins, Cell Adhesion Molecules, Contractile Proteins, Cytoskeletal Proteins, DNA-Binding Proteins, Fluorescent Antibody Technique, Indirect, Ligands, Listeria monocytogenes, Mice, Microfilament Proteins, Microfilaments, Molecular Sequence Data, Phosphoproteins, Phosphorylation, Profilins, Proteins, Rats, Sequence Alignment, Sequence Homology, Amino Acid, src Homology Domains
Cell
Date: Oct. 18, 1996
PubMed ID: 8861907
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