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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
25
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pubmed:dateCreated |
1995-1-11
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pubmed:abstractText |
Membrane targeting of pp60src (Src) is mediated by its myristoylated amino terminus. We demonstrate that, in addition to myristate, six basic residues in the amino terminus are essential for high-affinity binding to the lipid bilayer via electrostatic interaction with acidic phospholipids. Specifically, c-Src was shown to bind 2500-fold more strongly to vesicles composed of the physiological ratio of 2:1 phosphatidylcholine (PC)/phosphatidylserine (PS) than to neutral PC bilayer vesicles. The apparent Kd for binding of c-Src to the PC/PS bilayer was 6 x 10(-7) M. This interaction is sufficiently strong to account for c-Src membrane targeting. Mutants of c-Src in which the amino-terminal basic residues were replaced by neutral asparagine residues exhibited binding isotherms approaching that of wild-type binding to neutral bilayers (apparent Kd of 2 x 10(-3) M). The transforming v-Src and activated c-Src (Y527F) proteins also bound more strongly to PC/PS bilayers (apparent Kd of approximately 1 x 10(-5) M) than to neutral PC bilayers. In vivo experiments with Src mutants confirmed the role of positive charge in mediating membrane binding and cellular transformation.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-1378446,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-1400583,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-1689455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-1694307,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-1717459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-1737030,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-1868070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-1883932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-2034276,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-2164157,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-2208277,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-2250906,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-2482802,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-2546680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-2841581,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-2984663,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-2991884,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-3103925,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-3103926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-3103927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-3141787,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-3917576,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-6091899,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-6092942,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-6093098,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-6251464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-6441887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-7690037,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-7918991,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-7947714,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-8139035,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-8399188,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7527558-8474462
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
91
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12253-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7527558-3T3 Cells,
pubmed-meshheading:7527558-Amino Acid Sequence,
pubmed-meshheading:7527558-Animals,
pubmed-meshheading:7527558-Binding, Competitive,
pubmed-meshheading:7527558-Binding Sites,
pubmed-meshheading:7527558-Electrochemistry,
pubmed-meshheading:7527558-Kinetics,
pubmed-meshheading:7527558-Lipid Bilayers,
pubmed-meshheading:7527558-Mice,
pubmed-meshheading:7527558-Molecular Sequence Data,
pubmed-meshheading:7527558-Mutagenesis, Site-Directed,
pubmed-meshheading:7527558-Oligopeptides,
pubmed-meshheading:7527558-Oncogene Protein pp60(v-src),
pubmed-meshheading:7527558-Phospholipids,
pubmed-meshheading:7527558-Point Mutation,
pubmed-meshheading:7527558-Proto-Oncogene Proteins pp60(c-src),
pubmed-meshheading:7527558-Recombinant Proteins,
pubmed-meshheading:7527558-Structure-Activity Relationship,
pubmed-meshheading:7527558-Transfection
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pubmed:year |
1994
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pubmed:articleTitle |
Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids.
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pubmed:affiliation |
Cell Biology and Genetics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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