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Vol. 10, Issue 10, 3373-3387, October 1999
and
The Burnham Institute, La Jolla Cancer Research Center, La Jolla,
California 92037
Cells expressing the NG2 proteoglycan can attach, spread, and
migrate on surfaces coated with NG2 mAbs, demonstrating that engagement
of NG2 can trigger the cytoskeletal rearrangements necessary for
changes in cell morphology and motility. Engagement of different
epitopes of the proteoglycan results in distinct forms of actin
reorganization. On mAb D120, the cells contain radial actin spikes
characteristic of filopodial extension, whereas on mAb N143, the cells
contain cortical actin bundles characteristic of lamellipodia. Cells
that express NG2 variants lacking the transmembrane and cytoplasmic
domains are unable to spread or migrate on NG2 mAb-coated surfaces,
indicating that these portions of the molecule are essential for
NG2-mediated signal transduction. Cells expressing an NG2 variant
lacking the C-terminal half of the cytoplasmic domain can still spread
normally on mAbs D120 and N143, suggesting that the membrane-proximal
cytoplasmic segment is responsible for this process. In contrast, this
variant migrates poorly on mAb D120 and exhibits abnormal arrays of
radial actin filaments decorated with fascin during spreading on this
mAb. The C-terminal portion of the NG2 cytoplasmic domain, therefore,
may be involved in regulating molecular events that are crucial for
cell motility.
Department of Physiology and
Neurobiology, University of Connecticut, 3107 Horsebarn Hill Road,
U-156, Storrs, CT 06269-4156.
Corresponding author. E-mail address:
stallcup{at}burnham-inst.org.
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