Identification of novel Ack1-interacting proteins and Ack1 phosphorylated sites in mouse brain by mass spectrometry
Metrics: PDF 931 views | HTML 1940 views | ?
Maria del Mar Masdeu1,2,3,#, Beatriz G. Armendáriz1,2,#, Anna La Torre1,4, Eduardo Soriano1,2,5,6, Ferran Burgaya1,2,* and Jesús Mariano Ureña1,2,*
1Department of Cell Biology, Faculty of Biology, University of Barcelona, Barcelona 08028, Spain
2Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas (CIBERNED), ISCIII, 28031 Madrid, Spain
3Present address: Francis Crick Institute, Mill Hill Laboratory, Mill Hill, London NW7 1AA, United Kingdom
4Present address: Department of Cell Biology and Human Anatomy, University of California Davis, 95616 Davis, California, USA
5Vall d´Hebron Institute of Research, Barcelona 08035, Spain
6Institució Catalana de Recerca i Estudis Avançats (ICREA), Barcelona 08010, Spain
#These authors contributed equally to this work
Eduardo Soriano, email: email@example.com
Ferran Burgaya, email: firstname.lastname@example.org
Jesús Mariano Ureña, email: email@example.com
Keywords: tyrosine kinase, Ack1, central nervous system, development
Received: April 21, 2017 Accepted: August 26, 2017 Published: September 15, 2017
Ack1 (activated Cdc42-associated tyrosine kinase) is a non-receptor tyrosine kinase that is highly expressed in brain. This kinase contains several protein-protein interaction domains and its action is partially regulated by phosphorylation. As a first step to address the neuronal functions of Ack1, here we screened mouse brain samples to identify proteins that interact with this kinase. Using mass spectrometry analysis, we identified new putative partners for Ack1 including cytoskeletal proteins such as Drebrin or MAP4; adhesion regulators such as NCAM1 and neurabin-2; and synapse mediators such as SynGAP, GRIN1 and GRIN3. In addition, we confirmed that Ack1 and CAMKII both co-immunoprecipitate and co-localize in neurons. We also identified that adult and P5 samples contained the phosphorylated residues Thr 104 and Ser 825, and only P5 samples contained phosphorylated Ser 722, a site linked to cancer and interleukin signaling when phosphorylated. All these findings support the notion that Ack1 could be involved in neuronal plasticity.
All site content, except where otherwise noted, is licensed under a Creative Commons Attribution 3.0 License.