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(Received for publication, January 26, 1995) To determine the molecular basis for the transforming function
of platelet-derived growth factor (PDGF)-A in NIH/3T3 cells, we have
constructed chimerae consisting of the extracellular domain of the
human CSF-1R (fms) linked to the cytoplasmic domain of the
Volume 270,
Number 13,
Issue of March 31, 1995 pp. 7033-7036
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
-Platelet-derived Growth Factor (
PDGF) Receptor for PDGF
Focus Forming Activity Chemotaxis, or Growth
PDGF receptor (R) containing a series of deletion or point
mutations. The ability of fms/R chimerae to mediate
CSF-1-dependent anchorage-independent growth, focus formation, and
chemotaxis of NIH/3T3 cells was then examined. Our results provide
evidence that a domain encompassing amino acid residues 977-1024 of the
PDGFR is required for ligand-dependent focus formation, but not
chemotaxis or anchorage-independent growth, and that tyrosine residues
within this domain constitute the major binding site for phospholipase
C
. Therefore, our findings suggest that: (i) the focus forming
function of PDGFR correlates well with the ability of the receptor
to bind phospholipase C, and (ii) the mechanism of focus formation
mediated by PDGFR may be distinguished from that required for
chemotaxis or anchorage-independent growth.
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