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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

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Author(s)

  • Sarah Keenan
  • Philip A Lewis
  • Sarah J Wetherill
  • Christopher J R Dunning
  • Gareth J O Evans

Department/unit(s)

Publication details

JournalFEBS Letters
DatePublished - 27 May 2015
Issue number15
Volume589
Number of pages6
Pages (from-to)1995-2000
Original languageEnglish

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.

Bibliographical note

© 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.

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