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J. Biol. Chem., Vol. 267, Issue 21, 14616-14621, Jul, 1992
FX Yu, HQ Sun, PA Janmey and HL Yin
Gelsolin is an actin filament-severing and -capping protein that has
profound effects on actin filament organization and assembly. It is
activated by Ca2+ and inhibited by polyphosphoinositides (PPI). We have
previously shown that PPI inhibit actin filament severing by the amino-
terminal half of gelsolin and hypothesized that this is mediated through
inhibition of actin filament side binding (by domains II-III of gelsolin),
a requisite first step in severing. In this paper, we report that the
subsequent step in severing, which is mediated by an actin monomer binding
site located in domain I of gelsolin, is also regulated by PPI. We used
deletional mutagenesis and a synthetic peptide to locate the sequence
required for high affinity PPI binding in domain I. Our results show that
the PPI-binding sequence has a basic charge distribution that is also
present in the PPI-regulated actin filament side binding domain, and the
two gelsolin PPI-binding sites have similar PPI-binding affinities. In
addition, a similar motif is present in several other PPI-binding proteins,
including a highly conserved region in the phospholipase C family. We
propose that the sequences identified in gelsolin may represent a consensus
for PPI binding in a variety of proteins.
Identification of a polyphosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin
Department of Physiology, University of Texas Southwestern Medical Center, Dallas 75235.
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