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The N2-Src neuronal splice variant of C-Src has altered SH3 domain ligand specificity and a higher constitutive activity than N1-Src

FEBS Letters. 2015-05; 
SarahKeenan,Philip A.Lewis,Sarah J.Wetherill,Christopher J.R.Dunning,Gareth J.O.Evans
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Proteins, Expression, Isolation and Analysis … COVID-19 campus closures … a number of neuronal proteins are reduced or abolished compared to C-Src [15], [16], [17], [18], [19] … Following purification with glutathione resin (Genscript), the His-tagged kinases were cleaved from GST-PTP1B by incubation with PreScission 3C … Get A Quote

摘要

N2-Src is a poorly understood neuronal splice variant of the ubiquitous C-Src tyrosine kinase, containing a 17 amino acid insert in its Src homology 3 (SH3) domain. To characterise the properties of N2-Src we directly compared its SH3 domain specificity and kinase activity with C- and N1-Src in vitro. N2- and N1-Src had a similar low affinity for the phosphorylation of substrates containing canonical C-Src SH3 ligands and synaptophysin, an established neuronal substrate for C-Src. N2-Src also had a higher basal kinase activity than N1- and C-Src in vitro and in cells, which could be explained by weakened intramolecular interactions. Therefore, N2-Src is a highly active kinase that is likely to phosphorylate alt... More

关键词

SrcTyrosine protein kinaseKinase assayEnzyme kineticsSrc homology 3 domainSplice variant