Keenan, Sarah, Lewis, Philip A, Wetherill, Sarah J et al. (2 more authors) (2015) 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. pp. 1995-2000. ISSN 0014-5793
Abstract
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 alternative substrates to C-Src in the brain.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2015, The Authors. This content is made available by the publisher under a Creative Commons Attribution Licence. This means that a user may copy, distribute and display the resource providing that they give credit. Users must adhere to the terms of the licence. |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Biology (York) |
Funding Information: | Funder Grant number BBSRC (BIOTECHNOLOGY AND BIOLOGICAL SCIENCES RESEARCH COUNCIL) BB/E014755/1 |
Depositing User: | Pure (York) |
Date Deposited: | 02 Mar 2016 11:34 |
Last Modified: | 07 Feb 2025 00:11 |
Published Version: | https://doi.org/10.1016/j.febslet.2015.05.033 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1016/j.febslet.2015.05.033 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:95181 |
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Description: Neuronal splicing of C-Src regulates kinase activity and SH3 domain ligand specificity -FEBS Letters