Title : Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids.

Pub. Date : 1994 Dec 6

PMID : 7527558






4 Functional Relationships(s)
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1 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. Phosphatidylserines SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens
2 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. Phosphatidylserines SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens
3 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. Phosphatidylserines SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens
4 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. Phosphatidylserines SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens