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J. Biol. Chem., Vol. 276, Issue 46, 43390-43399, November 16, 2001
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From the Polyphosphoinositides (PPIs) affect the
localization and activities of many cellular constituents, including
actin-modulating proteins. Several classes of polypeptide sequences,
including pleckstrin homology domains, FYVE domains, and short linear
sequences containing predominantly hydrophobic and cationic residues
account for phosphoinositide binding by most such proteins. We report that a ten-residue peptide derived from the phosphatidylinositol 4,5-bisphosphate (PIP2) binding region in
segment 2 of gelsolin, when coupled to rhodamine B has potent
PIP2 binding activity in vitro; crosses the
cell membrane of fibroblasts, platelets, melanoma cells, and
neutrophils by a process not involving endocytosis; and blocks cell
motility. This peptide derivative transiently disassembles actin
filament structures in GFP-actin-expressing NIH3T3 fibroblasts and
prevents thrombin- or chemotactic peptide-stimulated actin assembly in
platelets and neutrophils, respectively, but does not block the initial
[Ca2+] increase caused by these agonists. The blockage of
actin assembly and motility is transient, and cells recover motility
within an hour after their immobilization by 5-20 µM
peptide. This class of reagents confirms the critical relation between
inositol lipids and cytoskeletal structure and may be useful to probe
the location and function of polyphosphoinositides in
vivo.
Cell Permeant Polyphosphoinositide-binding Peptides That Block
Cell Motility and Actin Assembly*
,,, and
Hematology Division, Brigham & Women's
Hospital, Department of Medicine, Harvard Medical School, Boston,
Massachusetts 02115, the § Latvian Organic Synthesis
Institute, Riga LV1006, Republic of Latvia, and the
¶ Department of Physiology, Institute for Medicine and
Engineering, University of Pennsylvania, Philadelphia, Pennsylvania
19063
*
This work was supported by Grant AR38910 from the National
Institutes of Health and the MRSEC program of the National Science Foundation under Award DMR00-79909 and by grants from NATO (to R. B.)
and the Fogarty Foundation (TW00100).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: Institute for
Medicine and Engineering, University of Pennsylvania, 1010 Vagelos Laboratories, 3340 Smith Walk, Philadelphia, PA 19104. Tel.:
215-573-7380; Fax: 215-573-6815; E-mail:
janmey@mail.med.upenn.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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