Reference : An actin-binding site containing a conserved motif of charged amino acid residues is ...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/10993/6291
An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin.
English
Friederich, Evelyne mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >]
Vancompernolle, K. [> >]
Huet, C. [> >]
Goethals, M. [> >]
Finidori, J. [> >]
Vandekerckhove, J. [> >]
Louvard, D. [> >]
1992
Cell
70
1
81-92
Yes (verified by ORBilu)
International
0092-8674
UNITED STATES
[en] Actins/chemistry ; Amino Acid Sequence ; Binding Sites ; Carrier Proteins/chemistry/pharmacology ; Cytoskeleton/drug effects ; Microfilament Proteins/chemistry/pharmacology ; Molecular Sequence Data ; Morphogenesis ; Mutation ; Peptide Fragments/chemical synthesis ; Transfection
[en] The actin-binding protein villin induces microvillus growth and reorganization of the cytoskeleton in cells that do not normally produce this protein. Transfection of mutagenized villin cDNAs into CV-1 cells was used to show that a conserved, COOH-terminally located cluster of charged amino acid residues (KKEK) is crucial for the morphogenic activity of villin in vivo. In vitro experiments with a 22 amino acid synthetic peptide corresponding to this region of villin provide evidence that this motif is part of an F-actin-binding site that induces G-actin to polymerize. Chemical cross-linking of actin to this peptide, the effects of amino acid substitutions in peptides, and the behavior of villin variants further corroborate the participation of the KKEK sequence in actin contacts.
http://hdl.handle.net/10993/6291

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