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Electrostatics and the Membrane Association of Src:  Theory and Experiment

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    Electrostatics and the Membrane Association of Src:  Theory and Experiment†
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    Department of Physiology and Biophysics, State University of New York at Stony Brook, Stony Brook, New York 11794-8661, Cell Biology and Genetics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, and Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032
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    Biochemistry

    Cite this: Biochemistry 1998, 37, 8, 2145–2159
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    https://doi.org/10.1021/bi972012b
    Published February 6, 1998
    Copyright © 1998 American Chemical Society
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    Abstract

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    The binding of Src to phospholipid membranes requires both hydrophobic insertion of its myristate into the hydrocarbon interior of the membrane and nonspecific electrostatic interaction of its N-terminal cluster of basic residues with acidic phospholipids. We provide a theoretical description of the electrostatic partitioning of Src onto phospholipid membranes. Specifically, we use molecular models to represent a nonmyristoylated peptide corresponding to residues 2−19 of Src [nonmyr-Src(2−19); GSSKSKPKDPSQRRRSLE-NH2] and a phospholipid bilayer, calculate the electrostatic interaction by solving the nonlinear Poisson−Boltzmann equation, and predict the molar partition coefficient using statistical thermodynamics. The theoretical predictions agree with experimental data obtained by measuring the partitioning of nonmyr-Src(2−19) onto phospholipid vesicles:  membrane binding increases as the mole percent of acidic lipid in the vesicles is increased, the ionic strength of the solution is decreased, or the net positive charge of the peptide is increased. The theoretical model also correctly predicts the measured partitioning of the myristoylated peptide, myr-Src(2−19); for example, adding 33% acidic lipid to electrically neutral vesicles increases the partitioning of myr-Src(2−19) 100-fold. Phosphorylating either serine 12 (by protein kinase C) or serine 17 (by cAMP-dependent protein kinase) decreases the partitioning of myr-Src(2−19) onto vesicles containing acidic lipid 10-fold. We investigated the effect of phosphorylation on the localization of Src to biological membranes by expressing fusion constructs of Src's N terminus with a soluble carrier protein in COS-1 cells; phosphorylation produces a small shift in the distribution of the Src chimeras from the plasma membrane to the cytosol.

    Copyright © 1998 American Chemical Society

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    †

     This research was supported by Grant MCB-9419175 from the NSF and Grant GM-24971 from the NIH to S.M., Grant BE235 from the American Cancer Society and Grant CA-72309 from the NIH to M.D.R., Grant MCB-9304127 from the NSF and Grant MCA95C015 from the NCSA to B.H., Grant 5T32 NSO 7372-03 from the NIH and a Helen Hay Whitney Foundation Postdoctoral Fellowship to D.M., and the Cancer Research Fund of the Damon Runyon-Walter Winchell Foundation Fellowship to C.A.B.

    ‡

     State University of New York at Stony Brook.

    §

     Memorial Sloan-Kettering Cancer Center.

    ‖

     Present address:  Cancer Research Department, Merck and Co., West Point, PA 19486.

    ⊥

     Present address:  Laboratory of Cellular and Molecular Recognition, National Institute of Mental Health, Bethesda, MD 20892.

    ∇

     Columbia University.

    #

     Present address:  Department of Biochemistry, Tel Aviv University, Ramat Aviv 69978, Israel.

    *

     Address correspondence to this author. Telephone:  516-444-3039. Fax:  516-444-3432. E-mail:  [email protected].

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    Biochemistry

    Cite this: Biochemistry 1998, 37, 8, 2145–2159
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    https://doi.org/10.1021/bi972012b
    Published February 6, 1998
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