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J. Biol. Chem., Vol. 276, Issue 34, 32264-32273, August 24, 2001
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From the Office of Clinical Research and Laboratory of Signal
Transduction, NIEHS, National Institutes of Health, Research Triangle
Park, North Carolina, 27709 and the Departments of Medicine and
Biochemistry, Duke University Medical Center,
Durham, North Carolina 27710
Mice lacking the myristoylated alanine-rich
C-kinase substrate, or MARCKS protein, exhibit abnormalities consistent
with a defect in the ability of neurons to migrate appropriately during forebrain development. To investigate the possibility that this phenotype could be due to disruption of normal cellular adhesion to
extracellular matrix, an assay was developed in which 293 cells co-expressing MARCKS and green fluorescent protein were tested for
their adhesion competence on various substrates. Fluorescence-activated cell sorting of adherent and non-adherent green fluorescent
protein-expressing cells demonstrated that wild-type MARCKS inhibited
adhesion of cells to fibronectin, whereas a non-myristoylated mutant
did not inhibit adhesion of cells to a variety of substrates. The
fibronectin competitive inhibitor RGD peptide inhibited adhesion of
cells expressing all MARCKS variants equally. Cytochalasin D inhibited the adhesion of cells expressing non-myristoylated MARCKS, but did not
further decrease the adhesion of cells expressing adhesion-inhibitory proteins. Confocal microscopy demonstrated the presence of inhibitory, myristoylated MARCKS at the plasma membrane, suggesting that
localization at this region might be important for MARCKS to inhibit
cellular adhesion. These data suggest a possible
myristoylation-dependent function of MARCKS to inhibit
cellular adhesion to extracellular matrix proteins, indicating a
potential mechanism for the cell migration defects seen in the
MARCKS-deficient mice.
Overexpression of the Myristoylated Alanine-rich
C-kinase Substrate Inhibits Cell Adhesion to Extracellular Matrix
Components*
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: A2-05 NIEHS, National
Institutes of Health, 111 Alexander Dr., Research Triangle Park, NC
27709. Tel.: 919-541-4899; Fax: 919-541-4571; E-mail: black009@niehs.nih.gov.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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