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Titolo:
ELECTROSTATICS AND THE MEMBRANE ASSOCIATION OF SRC - THEORY AND EXPERIMENT
Autore:
MURRAY D; MATSUMOTO LH; BUSER CA; TSANG J; SIGAL CT; BENTAL N; HONIG B; RESH MD; MCLAUGHLIN S;
Indirizzi:
SUNY STONY BROOK,DEPT PHYSIOL & BIOPHYS STONY BROOK NY 11794 SUNY STONY BROOK,DEPT PHYSIOL & BIOPHYS STONY BROOK NY 11794 MEM SLOAN KETTERING CANC CTR,CELL BIOL & GENET PROGRAM NEW YORK NY 10021 COLUMBIA UNIV,DEPT BIOCHEM & MOL BIOPHYS NEW YORK NY 10032
Titolo Testata:
Biochemistry
fascicolo: 8, volume: 37, anno: 1998,
pagine: 2145 - 2159
SICI:
0006-2960(1998)37:8<2145:EATMAO>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE KINASE; ROUS-SARCOMA VIRUS; TYPE-1 MATRIX PROTEIN; GROWTH-FACTOR; PHOSPHOLIPID-VESICLES; TRANSFORMING PROTEIN; ACIDIC PHOSPHOLIPIDS; BILAYER-MEMBRANES; PLASMA-MEMBRANE; BASIC RESIDUES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
78
Recensione:
Indirizzi per estratti:
Citazione:
D. Murray et al., "ELECTROSTATICS AND THE MEMBRANE ASSOCIATION OF SRC - THEORY AND EXPERIMENT", Biochemistry, 37(8), 1998, pp. 2145-2159

Abstract

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); GSSKSKPKDPSQRRSLE-NH2] and a phospholipid bilayer, calculatethe 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 ofthe solution is decreased, or the net positive ch;uge 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 increasesthe 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.

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Documento generato il 30/09/20 alle ore 05:36:36