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J. Biol. Chem., Vol. 277, Issue 37, 34401-34412, September 13, 2002
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From the A peptide corresponding to the basic (+13),
unstructured effector domain of myristoylated alanine-rich C kinase
substrate (MARCKS) binds strongly to membranes containing
phosphatidylinositol 4,5-bisphosphate (PIP2).
Although aromatic residues contribute to the binding, three experiments
suggest the binding is driven mainly by nonspecific local electrostatic
interactions. First, peptides with 13 basic residues, Lys-13 and
Arg-13, bind to PIP2-containing vesicles with the same high
affinity as the effector domain peptide. Second, removing basic
residues from the effector domain peptide reduces the binding energy by
an amount that correlates with the number of charges removed. Third,
peptides corresponding to a basic region in GAP43 and MARCKS effector
domain-like regions in other proteins (e.g. MacMARCKS,
adducin, Drosophila A kinase anchor protein
200, and N-methyl-D-aspartate receptor) also
bind with an energy that correlates with the number of basic residues. Kinetic measurements suggest the effector domain binds to several PIP2. Theoretical calculations show the effector domain
produces a local positive potential, even when bound to a bilayer with 33% monovalent acidic lipids, and should thus sequester
PIP2 laterally. This electrostatic sequestration was
observed experimentally using a phospholipase C assay. Our results are
consistent with the hypothesis that MARCKS could reversibly sequester
much of the PIP2 in the plasma membrane.
Lateral Sequestration of Phosphatidylinositol 4,5-Bisphosphate by
the Basic Effector Domain of Myristoylated Alanine-rich C Kinase
Substrate Is Due to Nonspecific Electrostatic Interactions*
,,, and
Department of Physiology and Biophysics and
the § Department of Physics and Astronomy, State University
of New York, Stony Brook, New York 11794-8661 and the
¶ Department of Microbiology and Immunology, Weill
Medical College of Cornell University, New York, New York 10021
*
This work was supported by National Institutes of Health
Grant GM24971 and National Science Foundation Grant MCB9729538 (to S. M.).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: Dept. of
Physiology and Biophysics, HSC, SUNY, Stony Brook, NY 11794-8661. Tel.: 631-444-3615; Fax: 631-444-3432; E-mail:
smcl@epo.som.sunysb.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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